A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.
Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.
A subfamily of small heat-shock proteins that function as molecular chaperones that aid in refolding of non-native proteins. They play a protective role that increases cellular survival during times of stress.
A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.
Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.
A constellation of responses that occur when an organism is exposed to excessive heat. Responses include synthesis of new proteins and regulation of others.
A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
LACTAMS forming compounds with a ring size of approximately 1-3 dozen atoms.
Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
A family of low molecular weight heat-shock proteins that can serve as MOLECULAR CHAPERONES.
A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.
A pathological condition manifested by failure to perfuse or oxygenate vital organs.
Sepsis associated with HYPOTENSION or hypoperfusion despite adequate fluid resuscitation. Perfusion abnormalities may include, but are not limited to LACTIC ACIDOSIS; OLIGURIA; or acute alteration in mental status.
A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
A constitutively expressed subfamily of the HSP70 heat-shock proteins. They preferentially bind and release hydrophobic peptides by an ATP-dependent process and are involved in post-translational PROTEIN TRANSLOCATION.
A group of eukaryotic high-molecular mass heat-shock proteins that represent a subfamily of HSP70 HEAT-SHOCK PROTEINS. Hsp110 proteins prevent protein aggregation and can maintain denatured proteins in folding-competent states.
A subfamily of small heat-shock proteins that are closely related to ALPHA B-CRYSTALLIN. Hsp20 heat-shock proteins can undergo PHOSPHORYLATION by CYCLIC GMP-DEPENDENT PROTEIN KINASES.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Basic glycoprotein members of the SERPIN SUPERFAMILY that function as COLLAGEN-specific MOLECULAR CHAPERONES in the ENDOPLASMIC RETICULUM.
One of the alpha crystallin subunits. In addition to being expressed in the lens (LENS, CRYSTALLINE), alpha-crystallin B chain has been found in a variety of tissues such as HEART; BRAIN; MUSCLE; and KIDNEY. Accumulation of the protein in the brain is associated with NEURODEGENERATIVE DISEASES such as CREUTZFELDT-JAKOB SYNDROME and ALEXANDER DISEASE.
A group of conditions that develop due to overexposure or overexertion in excessive environmental heat.
A subfamily of small heat-shock proteins found in a wide variety of organisms.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Acute hemorrhage or excessive fluid loss resulting in HYPOVOLEMIA.
A subclass of crystallins that provides the majority of refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Alpha-crystallins also act as molecular chaperones that bind to denatured proteins, keep them in solution and thereby maintain the translucency of the lens. The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Proteins found in any species of bacterium.
A group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. The protein was originally studied in BACTERIA where it is commonly referred to as GroES protein.
The unfavorable effect of environmental factors (stressors) on the physiological functions of an organism. Prolonged unresolved physiological stress can affect HOMEOSTASIS of the organism, and may lead to damaging or pathological conditions.
Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
A broad-spectrum antibiotic that is being used as prophylaxis against disseminated Mycobacterium avium complex infection in HIV-positive patients.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
Established cell cultures that have the potential to propagate indefinitely.
Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm.
The sum of the weight of all the atoms in a molecule.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
Proteins obtained from ESCHERICHIA COLI.
A condition caused by the failure of body to dissipate heat in an excessively hot environment or during PHYSICAL EXERTION in a hot environment. Contrast to HEAT EXHAUSTION, the body temperature in heat stroke patient is dangerously high with red, hot skin accompanied by DELUSIONS; CONVULSIONS; or COMA. It can be a life-threatening emergency and is most common in infants and the elderly.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Inorganic salts or organic esters of arsenious acid.
Abnormally high temperature intentionally induced in living things regionally or whole body. It is most often induced by radiation (heat waves, infra-red), ultrasound, or drugs.
Proteins prepared by recombinant DNA technology.
Elements of limited time intervals, contributing to particular results or situations.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Cellular proteins and peptides that are induced in response to cold stress. They are found in a broad variety of prokaryotic and eukaryotic organisms.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
A cell line derived from cultured tumor cells.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A flavonol widely distributed in plants. It is an antioxidant, like many other phenolic heterocyclic compounds. Glycosylated forms include RUTIN and quercetrin.
Inorganic compounds that contain sodium as an integral part of the molecule.
The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Shock resulting from diminution of cardiac output in heart disease.
One of the subunits of alpha-crystallins. Unlike ALPHA-CRYSTALLIN B CHAIN the expression of ALPHA-CRYSTALLIN A CHAIN is limited primarily to the lens (LENS, CRYSTALLINE).
A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The application of heat to raise the temperature of the environment, ambient or local, or the systems for accomplishing this effect. It is distinguished from HEAT, the physical property and principle of physics.
The process by which chemical compounds provide protection to cells against harmful agents.
A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
The rate dynamics in chemical or physical systems.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Adaptation to a new environment or to a change in the old.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
(13E,15S)-15-Hydroxy-9-oxoprosta-10,13-dien-1-oic acid (PGA(1)); (5Z,13E,15S)-15-hydroxy-9-oxoprosta-5,10,13-trien-1-oic acid (PGA(2)); (5Z,13E,15S,17Z)-15-hydroxy-9-oxoprosta-5,10,13,17-tetraen-1-oic acid (PGA(3)). A group of naturally occurring secondary prostaglandins derived from PGE; PGA(1) and PGA(2) as well as their 19-hydroxy derivatives are found in many organs and tissues.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
A species of fruit fly much used in genetics because of the large size of its chromosomes.
The non-genetic biological changes of an organism in response to challenges in its ENVIRONMENT.
Transport proteins that carry specific substances in the blood or across cell membranes.
An absence of warmth or heat or a temperature notably below an accustomed norm.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
Shock produced as a result of trauma.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
A protein which is a subunit of RNA polymerase. It effects initiation of specific RNA chains from DNA.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.
Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.
Cytoplasmic proteins that specifically bind glucocorticoids and mediate their cellular effects. The glucocorticoid receptor-glucocorticoid complex acts in the nucleus to induce transcription of DNA. Glucocorticoids were named for their actions on blood glucose concentration, but they have equally important effects on protein and fat metabolism. Cortisol is the most important example.
A mitogen-activated protein kinase subfamily that regulates a variety of cellular processes including CELL GROWTH PROCESSES; CELL DIFFERENTIATION; APOPTOSIS; and cellular responses to INFLAMMATION. The P38 MAP kinases are regulated by CYTOKINE RECEPTORS and can be activated in response to bacterial pathogens.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
A clinical syndrome caused by heat stress, such as over-exertion in a hot environment or excessive exposure to sun. It is characterized by SWEATING, water (volume) depletion, salt depletion, cool clammy skin, NAUSEA, and HEADACHE.
The relationship between the dose of an administered drug and the response of the organism to the drug.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
A group of often glycosylated macrocyclic compounds formed by chain extension of multiple PROPIONATES cyclized into a large (typically 12, 14, or 16)-membered lactone. Macrolides belong to the POLYKETIDES class of natural products, and many members exhibit ANTIBIOTIC properties.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
Proteins found in any species of fungus.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
The functional hereditary units of BACTERIA.
A cadmium halide in the form of colorless crystals, soluble in water, methanol, and ethanol. It is used in photography, in dyeing, and calico printing, and as a solution to precipitate sulfides. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A species of gram-positive, aerobic bacteria that causes LEPROSY in man. Its organisms are generally arranged in clumps, rounded masses, or in groups of bacilli side by side.
Enzymes that oxidize certain LUMINESCENT AGENTS to emit light (PHYSICAL LUMINESCENCE). The luciferases from different organisms have evolved differently so have different structures and substrates.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
A pattern recognition receptor that interacts with LYMPHOCYTE ANTIGEN 96 and LIPOPOLYSACCHARIDES. It mediates cellular responses to GRAM-NEGATIVE BACTERIA.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.
A class of organic compounds containing two ring structures, one of which is made up of more than one kind of atom, usually carbon plus another atom. The heterocycle may be either aromatic or nonaromatic.
High-amplitude compression waves, across which density, pressure, and particle velocity change drastically. The mechanical force from these shock waves can be used for mechanically disrupting tissues and deposits.
The measure of the level of heat of a human or animal.
Immunoglobulins produced in a response to BACTERIAL ANTIGENS.
A genus of CRUSTACEA of the order ANOSTRACA, found in briny pools and lakes and often cultured for fish food. It has 168 chromosomes and differs from most crustaceans in that its blood contains hemoglobin.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A species of CHLAMYDOPHILA that causes acute respiratory infection, especially atypical pneumonia, in humans, horses, and koalas.
Substances elaborated by bacteria that have antigenic activity.
A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
The termination of the cell's ability to carry out vital functions such as metabolism, growth, reproduction, responsiveness, and adaptability.
Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed)
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
The pressure required to prevent the passage of solvent through a semipermeable membrane that separates a pure solvent from a solution of the solvent and solute or that separates different concentrations of a solution. It is proportional to the osmolality of the solution.
The protein complement of an organism coded for by its genome.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
The relationships of groups of organisms as reflected by their genetic makeup.
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
An antibiotic compound derived from Streptomyces niveus. It has a chemical structure similar to coumarin. Novobiocin binds to DNA gyrase, and blocks adenosine triphosphatase (ATPase) activity. (From Reynolds, Martindale The Extra Pharmacopoeia, 30th ed, p189)
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
Proteins, glycoprotein, or lipoprotein moieties on surfaces of tumor cells that are usually identified by monoclonal antibodies. Many of these are of either embryonic or viral origin.
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
Type species of CHLAMYDIA causing a variety of ocular and urogenital diseases.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.
Hybridization of a nucleic acid sample to a very large set of OLIGONUCLEOTIDE PROBES, which have been attached individually in columns and rows to a solid support, to determine a BASE SEQUENCE, or to detect variations in a gene sequence, GENE EXPRESSION, or for GENE MAPPING.
Substances that inhibit or prevent the proliferation of NEOPLASMS.
Chemical substances, produced by microorganisms, inhibiting or preventing the proliferation of neoplasms.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.
A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
An ERYTHROLEUKEMIA cell line derived from a CHRONIC MYELOID LEUKEMIA patient in BLAST CRISIS.
A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
A generic term for any circumscribed mass of foreign (e.g., lead or viruses) or metabolically inactive materials (e.g., ceroid or MALLORY BODIES), within the cytoplasm or nucleus of a cell. Inclusion bodies are in cells infected with certain filtrable viruses, observed especially in nerve, epithelial, or endothelial cells. (Stedman, 25th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Serum glycoprotein produced by activated MACROPHAGES and other mammalian MONONUCLEAR LEUKOCYTES. It has necrotizing activity against tumor cell lines and increases ability to reject tumor transplants. Also known as TNF-alpha, it is only 30% homologous to TNF-beta (LYMPHOTOXIN), but they share TNF RECEPTORS.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.
Serological reactions in which an antiserum against one antigen reacts with a non-identical but closely related antigen.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
Non-antibody proteins secreted by inflammatory leukocytes and some non-leukocytic cells, that act as intercellular mediators. They differ from classical hormones in that they are produced by a number of tissue or cell types rather than by specialized glands. They generally act locally in a paracrine or autocrine rather than endocrine manner.
A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.

In vivo chaperone activity of heat shock protein 70 and thermotolerance. (1/4872)

Heat shock protein 70 (Hsp70) is thought to play a critical role in the thermotolerance of mammalian cells, presumably due to its chaperone activity. We examined the chaperone activity and cellular heat resistance of a clonal cell line in which overexpression of Hsp70 was transiently induced by means of the tetracycline-regulated gene expression system. This single-cell-line approach circumvents problems associated with clonal variation and indirect effects resulting from constitutive overexpression of Hsp70. The in vivo chaperone function of Hsp70 was quantitatively investigated by using firefly luciferase as a reporter protein. Chaperone activity was found to strictly correlate to the level of Hsp70 expression. In addition, we observed an Hsp70 concentration dependent increase in the cellular heat resistance. In order to study the contribution of the Hsp70 chaperone activity, heat resistance of cells that expressed tetracycline-regulated Hsp70 was compared to thermotolerant cells expressing the same level of Hsp70 plus all of the other heat shock proteins. Overexpression of Hsp70 alone was sufficient to induce a similar recovery of cytoplasmic luciferase activity, as does expression of all Hsps in thermotolerant cells. However, when the luciferase reporter protein was directed to the nucleus, expression of Hsp70 alone was not sufficient to yield the level of recovery observed in thermotolerant cells. In addition, cells expressing the same level of Hsp70 found in heat-induced thermotolerant cells containing additional Hsps showed increased resistance to thermal killing but were more sensitive than thermotolerant cells. These results suggest that the inducible form of Hsp70 contributes to the stress-tolerant state by increasing the chaperone activity in the cytoplasm. However, its expression alone is apparently insufficient for protection of other subcellular compartments to yield clonal heat resistance to the level observed in thermotolerant cells.  (+info)

Role of DnaK in in vitro and in vivo expression of virulence factors of Vibrio cholerae. (2/4872)

The dnaK gene of Vibrio cholerae was cloned, sequenced, and used to construct a dnaK insertion mutant which was then used to examine the role of DnaK in expression of the major virulence factors of this important human pathogen. The central regulator of several virulence genes of V. cholerae is ToxR, a transmembrane DNA binding protein. The V. cholerae dnaK mutant grown in standard laboratory medium exhibited phenotypes characteristic of cells deficient in ToxR activity. Using Northern blot analysis and toxR transcriptional fusions, we demonstrated a reduction in expression of the toxR gene in the dnaK mutant strain together with a concomitant increase in expression of a htpG-like heat shock gene that is located immediately upstream and is divergently transcribed from toxR. This may be due to increased heat shock induction in the dnaK mutant. In vivo, however, although expression from heat shock promoters in the dnaK mutant was similar to that observed in vitro, expression of both toxR and htpG was comparable to that by the parental strain. In both strains, in vivo expression of toxR was significantly higher than that observed in vitro, but no reciprocal decrease in htpG expression was observed. These results suggest that the modulation of toxR expression in vivo may be different from that observed in vitro.  (+info)

Cloning and expression of the dnaK gene of Campylobacter jejuni and antigenicity of heat shock protein 70. (3/4872)

Campylobacter jejuni is a leading cause of infectious diarrhea throughout the world. In addition, there is growing evidence that Guillain-Barre syndrome, an inflammatory demyelinating disease of the peripheral nervous system, is frequently preceded by C. jejuni infection. In the present study, the hrcA-grpE-dnaK gene cluster of C. jejuni was cloned and sequenced. The dnaK gene consists of an open reading frame of 1,869 bp and encodes a protein with a high degree of homology to other bacterial 70-kDa heat shock proteins (HSPs). The overall percentages of identity to the HSP70 proteins of Helicobacter pylori, Borrelia burgdorferi, Chlamydia trachomatis, and Bacillus subtilis were calculated to be 78.1, 60.5, 57.2, and 53. 8%, respectively. Regions similar to the Escherichia coli sigma70 promoter consensus sequence and to a cis-acting regulatory element (CIRCE) are located upstream of the hrcA gene. Following heat shock, a rapid increase of dnaK mRNA was detectable, which reached its maximum after 20 to 30 min. A 6-His-tagged recombinant DnaK protein (rCjDnaK-His) was generated in E. coli, after cloning of the dnaK coding region into pET-22b(+), and purified by affinity and gel filtration chromatography. Antibody responses to rCjDnaK-His were significantly elevated, compared to those of healthy individuals, in about one-third of the serum specimens obtained from C. jejuni enteritis patients.  (+info)

Heat shock protein 70 (Hsp70) protects postimplantation murine embryos from the embryolethal effects of hyperthermia. (4/4872)

Previous work has shown that there is a positive correlation between the induction of Hsp70 and its transient nuclear localization and the acquisition and loss of induced thermotolerance in postimplantation rat embryos. To determine whether Hsp70 is sufficient to induce thermotolerance in postimplantation mammalian embryos, we used a transgenic mouse in which the normally strictly inducible Hsp70 is constitutively expressed in the embryo under the control of a beta-actin promoter. Day 8.0 mouse embryos heterozygous for the Hsp70 transgene were not protected from the embryotoxic effects of hyperthermia (43 degrees C); however, homozygous embryos, expressing approximately twice as much Hsp70 as heterozygous embryos, were partially protected (increased embryo viability) from the embryolethal effects of hyperthermia. Although the viability of transgenic embryos was significantly increased compared with that of nontransgenic embryos, this protection did not extend to embryo growth and development. To determine whether the failure to achieve a more robust protection was related to the expression of insufficient Hsp70 in transgenic embryos, we undertook experiments to determine whether the level of Hsp70 correlated with the level of thermotolerance induced by various lengths of a 41 degrees C heat shock. A 41 degrees C, 5-minute heat shock failed to induce Hsp70 or thermotolerance, a 41 degrees C, 15-minute heat shock induced Hsp70 and a significant level of thermotolerance, while a 41 degrees C, 60-minute heat shock induced an even higher level of Hsp70 as well as a higher level of thermotolerance. Quantitation of Hsp70 levels indicated that thermotolerance was associated with levels of Hsp70 of 820 pg/microg embryo protein or greater. Subsequent quantitation of the amount of Hsp70 expressed in homozygous transgenic embryos indicated a level of 577 pg/microg embryo protein, that is, a level below that associated with induced thermotolerance. Overall, results presented indicate that Hsp70 does play a direct role in the induction of thermotolerance in postimplantation mouse embryos; however, the level of thermotolerance is dependent on the level of Hsp70 expressed.  (+info)

Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. (5/4872)

Hsp70 molecular chaperones contain three distinct structural domains, a 44 kDa N-terminal ATPase domain, a 17 kDa peptide-binding domain, and a 10 kDa C-terminal domain. The ATPase and peptide binding domains are conserved in sequence and are functionally well characterized. The function of the 10 kDa variable C-terminal domain is less well understood. We have characterized the secondary structure and dynamics of the C-terminal domain from the Escherichia coli Hsp70, DnaK, in solution by high-resolution NMR. The domain was shown to be comprised of a rigid structure consisting of four helices and a flexible C-terminal subdomain of approximately 33 amino acids. The mobility of the flexible region is maintained in the context of the full-length protein and does not appear to be modulated by the nucleotide state. The flexibility of this region appears to be a conserved feature of Hsp70 architecture and may have important functional implications. We also developed a method to analyze 15N nuclear spin relaxation data, which allows us to extract amide bond vector directions relative to a unique diffusion axis. The extracted angles and rotational correlation times indicate that the helices form an elongated, bundle-like structure in solution.  (+info)

Gene expression and chromatin organization during mouse oocyte growth. (6/4872)

Mouse oocytes can be classified according to their chromatin organization and the presence [surrounded nucleolus (SN) oocytes] or absence [nonsurrounded nucleolus (NSN) oocytes] of a ring of Hoechst-positive chromatin around the nucleolus. Following fertilization only SN oocytes are able to develop beyond the two-cell stage. These studies indicate a correlation between SN and NSN chromatin organization and the developmental competence of the female gamete, which may depend on gene expression. In the present study, we have used the HSP70.1Luc transgene (murine HSP70.1 promoter + reporter gene firefly luciferase) to analyze gene expression in oocytes isolated from ovaries of 2-day- to 13-week-old females. Luciferase was assayed on oocytes after classification as SN or NSN type. Our data show that SN oocytes always exhibit a higher level of luciferase activity, demonstrating a higher gene expression in this category. Only after meiotic resumption, metaphase II oocytes derived from NSN or SN oocytes acquire the same level of transgene expression. We suggest that the limited availability of transcripts and corresponding proteins, excluded from the cytoplasm until GVBD in NSN oocytes, could explain why these oocytes have a lower ability to sustain embryonic development beyond the two-cell stage at which major zygotic transcription occurs. With this study we have furthered our knowledge of epigenetic regulation of gene expression in oogenesis.  (+info)

Genetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesis. (7/4872)

The Hsp90 chaperone protein maintains the activities of a remarkable variety of signal transducers, but its most critical functions in the context of the whole organism are unknown. Point mutations of Hsp83 (the Drosophila Hsp90 gene) obtained in two different screens are lethal as homozygotes. We report that eight transheterozygous mutant combinations produce viable adults. All exhibit the same developmental defects: sterile males and sterile or weakly fertile females. We also report that scratch, a previously identified male-sterile mutation, is an allele of Hsp82 with a P-element insertion in the intron that reduces expression. Thus, it is a simple reduction in Hsp90 function, rather than possible altered functions in the point mutants, that leads to male sterility. As shown by light and electron microscopy, all stages of spermatogenesis involving microtubule function are affected, from early mitotic divisions to later stages of sperm maturation, individualization, and motility. Aberrant microtubules are prominent in yeast cells carrying mutations in HSP82 (the yeast Hsp90 gene), confirming that Hsp90 function is connected to microtubule dynamics and that this connection is highly conserved. A small fraction of Hsp90 copurifies with taxol-stabilized microtubule proteins in Drosophila embryo extracts, but Hsp90 does not remain associated with microtubules through repeated temperature-induced assembly and disassembly reactions. If the spermatogenesis phenotypes are due to defects in microtubule dynamics, we suggest these are indirect, reflecting a role for Hsp90 in maintaining critical signal transduction pathways and microtubule effectors, rather than a direct role in the assembly and disassembly of microtubules themselves.  (+info)

Role of heat shock protein HSP70-2 in spermatogenesis. (8/4872)

The HSP70 heat-shock proteins are molecular chaperones that assist other proteins in their folding, transport and assembly into complexes. Most of these proteins are either constitutively expressed or their expression is induced by heat shock and other stresses. However, two members of the Hsp70 family (HSP70-2 and HSC70T in mice) are regulated developmentally and expressed specifically in spermatogenic cells. The HSP70-2 protein is synthesized during the meiotic phase of spermatogenesis and is abundant in pachytene spermatocytes. The knockout approach was used to determine whether HSP70-2 is a chaperone for proteins involved in meiosis. Male mice lacking HSP70-2 were infertile while females lacking HSP70-2 were fertile. Spermatogenic cell development was arrested in prophase of meiosis I at the G2-M-phase transition and late pachytene spermatocytes were eliminated by apoptosis, resulting in an absence of spermatids. HSP70-2 is required for Cdc2 to form a heterodimer with cyclin B1, suggesting that it is a chaperone necessary for the progression of meiosis in the germ cells of male mice. HSP70-2 is also associated with the synaptonemal complex and desynapsis is disrupted in male mice lacking this protein. Homologues of HSP70-2 are present in the testes of many animals, suggesting that the role of this spermatogenic cell chaperone is conserved across phyla.  (+info)

Human papillomaviruses (HPVs) are small, non-enveloped double stranded DNA viruses that demonstrate a strict species and cell type tropism for human epithelial cells. The association between high-risk HPV types and cervical cancer is well established. Additionally, HPVs have been implicated as causes in development of several other epithelial cancer types. Increasing data indicate heat shock proteins (HSPs) including inducible HSP70 (HSP70i) are involved in the replicative cycles of different viruses including adenoviruses, polyomaviruses (PyV), and some RNA viruses. Cell-free system studies implicate HSP70i in HPV11 genome replication with E1 and E2 proteins, and there is evidence that HSP70 is involved in capsid assembly and disassembly for PyV and PV. HSP70 expression is increased in HPV16 E6/E7 gene transduced human primary keratinocytes, and frequently detected in early stage uterine cervical cancer at levels in conjunction with lesion severity. In this study we carry out analyses with
TY - JOUR. T1 - Glucose-regulated protein GRP78 is up-regulated in prostate cancer and correlates with recurrence and survival. AU - Daneshmand, Siamak. AU - Quek, Marcus L.. AU - Lin, Ed. AU - Lee, Charlotte. AU - Cote, Richard J.. AU - Hawes, Debra. AU - Cai, Jie. AU - Groshen, Susan. AU - Lieskovsky, Gary. AU - Skinner, Donald G.. AU - Lee, Amy S.. AU - Pinski, Jacek. PY - 2007/10/1. Y1 - 2007/10/1. N2 - Chemotherapy resistance is a significant contributor to treatment failure and death in men with hormone-refractory prostate cancer. One unexplored mechanism for drug resistance is the induction of stress response proteins referred to as the glucose-regulated proteins (GRPs). We sought to determine the level of expression of GRP78, the best characterized GRP in lymph node-positive prostate cancer. Archived, paraffin-embedded, radical prostatectomy specimens were obtained from 153 patients with lymph node-positive prostate cancer (stage D1). The level of GRP78 expression was determined by ...
The evolutionary diversity of the HSP70 gene family at the genetic level has generated complex structural variations leading to altered functional specificity and mode of regulation in different cellular compartments. By utilizing Saccharomyces cerevisiae as a model system for better understanding t …
TY - JOUR. T1 - Induction of 78kD glucose-regulated protein (GRP78) expression and redox-regulated transcription factor activity by lead and mercury in C6 rat glioma cells. AU - Qian, Yongchang. AU - Hadi Falahatpisheh, M.. AU - Zheng, Ying. AU - Ramos, Kenneth S.. AU - Tiffany-Astiglioni, Evelyn. PY - 2001/1/1. Y1 - 2001/1/1. N2 - Lead (Pb) and mercury (Hg) are widespread environmental contaminants that induce prominent neural toxicity. Although the brain is not the major Pb and Hg depot in the body, these metals preferentially accumulate in astroglia to exert toxic effects. In this study, we examined the effects of Pb acetate and HgCI2 on the expression of GRP78, a molecular chaperone in the endoplasmic reticulum (ER) that may provide cytoprotection in response to cellular stresses in the C6 rat glioma cell line. We also evaluated the DNA binding activities of several redox-regulated transcription factors in metal-treated cells. Our results showed that mRNA levels of GRP78 were up-regulated by ...
TY - JOUR. T1 - Selective depletion of inducible HSP70 enhances immunogenicity of rat colon cancer cells. AU - Gurbuxani, Sandeep. AU - Bruey, Jean Marie. AU - Fromentin, Annie. AU - Larmonier, Nicolas. AU - Parcellier, Arnaud. AU - Jäättelä, Marja. AU - Martin, François. AU - Solary, Eric. AU - Garrido, Carmen. N1 - Funding Information: We thank M Martin and B Bonnotte for valuable advice and M Moutet for excellent technical assistance. Our group is supported by a special grant from the Ligue Nationale. PY - 2001/11/8. Y1 - 2001/11/8. N2 - Expression of inducible heat shock protein 70 (HSP70) in tumor cells has been proposed to enhance their immunogenicity. However, HSP70 has also been demonstrated to prevent tumor cell death, a key process for the development of tumor cell immunogenicity. In the present study, we investigated the influence of the HSP70 protein level on PRO colon cancer cell growth and immunogenicity in syngeneic BDIX rats and nude mice. These cells have a basal expression ...
The study was aimed at assessing whether the peri-parturient period is associated with changes of intracellular and plasma inducible heat shock proteins (Hsp) 72 kDa molecular weight in dairy cows, and to establish possible relationships between Hsp72, metabolic, and immunological parameters subjected to changes around calving. The study was carried out on 35 healthy periparturient Holstein cows. Three, two, and one week before the expected calving, and 1, 2, 3, 4, and 5 weeks after calving, body conditions score (BCS) was measured and blood samples were collected to separate plasma and peripheral blood mononuclear cells (PBMC). Concentrations of Hsp72 in PBMC and plasma increased sharply after calving. In the post-calving period, BCS and plasma glucose declined, whereas plasma nonesterified fatty acids (NEFA) and tumor necrosis factor-alpha increased. The proliferative responses of PBMC to lipopolysaccharide (LPS) declined progressively after calving. The percentage of PBMC expressing CD14 ...
Heat shock proteins are generally responsible for preventing damage to proteins in response to high levels of heat. Heat shock proteins are classified into six major families based on their molecular mass: small HSPs, HSP40, HSP60, HSP70, HSP90, and HSP110. HSP60 is implicated in mitochondrial protein import and macromolecular assembly. It may facilitate the correct folding of imported proteins and may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSP60 interacts with HRAS and with HBV protein X and HTLV-1 protein p40tax. HSP60 belongs to the chaperonin (HSP60) family. Note: This description may include information from UniProtKB ...
The knowledge of GRPs as molecular chaperones is rapidly evolving. It is anticipated that the GRPs will make special contributions in the areas of basic cell biology, biotechnology, and cancer biology. In particular, they may play a role as the prototype of a class of genes that are regulated by sig …
Seasonal variation in heat shock proteins Hsp70 and Hsp90 expression was studied in the leaves of two naturally growing Iris pumila populations, one inhabiting an open dune site, and the other the understorey of a Pinus silvestris stand. The Hsps were quantified by an immunoblotting procedure. The level of the Hsps was found to vary significantly both across seasons and between habitats. The mean Hsp70 concentration was significantly greater at the open area than in the woodland understorey, reaching its maximum in the summer, especially in plants experiencing full sunlight. Two Hsp90 isoforms, referred to as Hsp90a (86 kDa) and Hsp90b (84 kDa), were detected. At both habitats, the level of Hsp90a was highest in autumn, that of Hsp90b in spring, whereas both of them reached a nadir in summer. Throughout the growing season, the relative abundance of Hsp90b was higher in plants growing under vegetation canopy in comparison to those inhabiting the open dune site. An inverse relationship between the ...
The 90-kDa heat shock protein, Hsp90, was previously shown to capture firefly luciferase during thermal inactivation, thereby preventing its irreversible off-pathway aggregation and maintaining it in a folding-competent state. However, subsequent refolding of the luciferase required addition of rabbit reticulocyte lysate. Here we demonstrate that Hsc70 (cytosolic Hsp70) and Hsp40/Hdj1 (cytosolic DnaJ homologue) are the effective components in a reticulocyte lysate, while other unidentified factor in the lysate is also required for the refolding of Hsp90-captured luciferase. Though another cytosolic DnaJ homologue, Hdj2/HSDJ, was more efficient than Hsp40 in suppressing the aggregation of rhodanese, Hdj2 was less effective for the refolding of luciferase than Hsp40. In the absence of the third factor, Hsp40 could bind to the luciferase captured by Hsp90, which suggested that Hsp40 on its own was able to bind the substrate protein, but Hsc70 could not.
TY - JOUR. T1 - In vitro heat shock of human monocytes results in a proportional increase of inducible Hsp70 expression according to the basal content. AU - Vince, Rebecca V.. AU - Oliver, Katherine. AU - Midgley, Adrian W.. AU - McNaughton, Lars R.. AU - Madden, Leigh A.. PY - 2010/5. Y1 - 2010/5. KW - Heat shock. KW - Stress response. KW - Hsp70. KW - Monocytes. KW - Diurnal variation. U2 - 10.1007/s00726-009-0354-4. DO - 10.1007/s00726-009-0354-4. M3 - Article. VL - 38. SP - 1423. EP - 1428. JO - Amino Acids. JF - Amino Acids. SN - 0939-4451. IS - 5. ER - ...
Domain architectures containing both Actin-like ATPase domain and Heat shock protein 70kD (HSP70), peptide-binding domain in Thelohanellus kitauei. Links to architectures containing these domain pairs in other groups of genomes are provided. Domain pairs which are not adjacent can be added/removed.
The in vivo function of the heat shock protein 90 (Hsp90) molecular chaperone is dependent on the binding and hydrolysis of ATP, and on interactions with a variety of co-chaperones containing tetratricopeptide repeat (TPR) domains. We have now analysed the interaction of the yeast TPR-domain co-chaperones Sti1 and Cpr6 with yeast Hsp90 by isothermal titration calorimetry, circular dichroism spectroscopy and analytical ultracentrifugation, and determined the effect of their binding on the inherent ATPase activity of Hsp90. Sti1 and Cpr6 both bind with sub-micromolar affinity, with Sti1 binding accompanied by a large conformational change. Two co-chaperone molecules bind per Hsp90 dimer, and Sti1 itself is found to be a dimer in free solution. The inherent ATPase activity of Hsp90 is completely inhibited by binding of Sti1, but is not affected by Cpr6, although Cpr6 can reactivate the ATPase activity by displacing Sti1 from Hsp90. Bound Sti1 makes direct contact with, and blocks access to the ...
Hypoxia upregulated protein 1, encoded by the HYOU1 gene, belongs to the heat shock protein 70 family. It is also known as 150 kDa oxygen-regulated protein (ORP150), 170 kDa glucose-regulated protein (GRP170), glucose-regulated protein 170, and HSP12A. The HYOU1 gene is transcribed into three mRNAs, due to the use of alternative transcription sites. A segment at the 5 end of exon 1A is involved in stress-dependent induction and results in the accumulation of ORP150 in the endoplasmic reticulum under low oxygen conditions. Suppression of the HYOU1 gene is associated with accelerated apoptosis, while its upregulation is associated with tumor development and invasiveness.. ...
Eukaryotic genomes encode multiple 70-kDa heat-shock proteins (HSP70s). The Saccharomyces cerevisiae HSP70 family is comprised of eight members. Here we present the nucleotide sequence of the SSA3 and SSB2 genes, completing the nucleotide sequence data for the yeast HSP70 family. We have analyzed these yeast sequences as well as 29 HSP70s from 24 additional eukaryotic and prokaryotic species. Comparison of the sequences demonstrates the extreme conservation of HSP70s; proteins from the most distantly related species share at least 45% identity and more than one-sixth of the amino acids are identical in the aligned region (567 amino acids) among all proteins analyzed. Phylogenetic trees constructed by two independent methods indicate that ancient molecular and cellular events have given rise to at least four monophyletic groups of eukaryotic HSP70 proteins. Each group of evolutionarily similar HSP70s shares a common intracellular localization and is presumed to be comprised of functional ...
Previous studies have shown that different Hsp70 paralogs have both overlapping and diverse functions (Boorstein et al. 1994; Daugaard et al. 2007). The divergent C-terminal SBDs (substrate-binding domains) are necessary for certain co-chaperone interactions and probably define their distinctive function (Brocchieri et al. 2008; Demand et al. 1998; Sung et al. 2001). For example, cytosolic eukaryotic Hsp70s possess GGMP repeats and the EEVD motif at the carboxyl terminus, whereas other Hsp70 family members lack such structural elements (Boorstein et al. 1994; Freeman et al. 1995). It has been shown that in photosynthetic eukaryotes: (1) the Hsp70s are located in four different cell compartments: the cytoplasm, mitochondria, endoplasmic reticulum (ER), and chloroplast (Bukau and Horwich 1998; Sung et al. 2001), and; (2) the most common motif for the cytosolic is EEVD, for the endoplasmic reticulum (ER) is HDEL, for the mitochondrion is PEAEYEEAKK and for the plastid is PEGDVIDADFTDSK (Guy and Li ...
The SCOP classification for the Heat shock protein 70kD (HSP70), peptide-binding domain superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
The importance of HSPs themselves in antigen presentation and cross-presentation remains controversial. Most studies agree that as part of their molecular chaperone function, HSPs can bind and present tumor associated antigens to professional antigen presenting cells through MHC class I and class II molecules, leading to the activation of anti-tumor CD8+ and CD4+ T cells. The regulation of the innate and adaptive immune responses by HSPs is still a matter of intense research. HSPs are seen as important anticancer vaccine adjuvants. They are used through different delivery systems: HSPs/antibodies, peptide/protein-HSP complexes, tumor antigen/HSP gene fusion, viral peptides/HSP complexes or gene fusion, viral proteins/bacterial HSP fusion. In preclinical models different administration routes, subcutaneous, intradermal, intramuscular or even peroral (under special conditions) can be used, and the animal toxicities are non-significant. The HSP-based vaccines can induce specific and non-specific ...
Heat shock protein 90 (Hsp90) is a well-known adenosine 5′-triphosphate (ATP)-dependent protein chaperone that achieves cellular protein homeostasis (1). A remarkable number of Hsp90 client proteins play important roles in the growth and proliferation of cancer cells (2). Beyond their effects on all the clients, kinase levels are highly correlated with the Hsp90 chaperone cycle, which makes Hsp90 an attractive anticancer therapeutic target (3). At present, the main focus of research targeting Hsp90 is competitively inhibiting the adenosine triphosphatase (ATPase) binding site on the Hsp90 N-terminal domain, leading to 17 small-molecule inhibitors with diverse structure types entered into clinical trials. However, current Hsp90 inhibitors exert a variety of toxicities (such as cardiotoxicity, gastrointestinal toxicity, and ocular toxicity) and ineluctable heat shock responses with limited clinical validity, which become the major obstacles restricting their approval to the market (4, 5). During ...
Heat shock proteins, Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region [ (PUBMED:9476895) ]. Hsp70 proteins have an average molecular weight of 70kDa [ (PUBMED:2686623) (PUBMED:2944601) (PUBMED:3282176) ]. In most species, there are many proteins that belong to the Hsp70 family. Some of these are only expressed under stress conditions (strictly inducible), while some are present in cells under normal growth conditions and are not heat-inducible (constitutive or cognate) [ (PUBMED:2143562) (PUBMED:2841196) ]. Hsp70 proteins can be found in different cellular compartments(nuclear, cytosolic, mitochondrial, endoplasmic reticulum, for example). This entry represents the Hsp70 family, and includes chaperone protein DnaK and luminal-binding proteins. It ...
热激蛋白90(heat shock protein 90,HSP90)广泛介导了胁迫信号的传递,在控制人体细胞正常生长和促进肿瘤细胞发育中起着重要作用;目前,HSP90已成为细胞免疫、信号转导以及抗肿瘤研究的前沿课题。植物HSP90的生理功能研究起步较晚,最近的研究发现HSP90在植物发育、胁迫环境的应答以及抗病性中起着重要作用。本文从分子生物学角度,系统综述了植物HSP90分子作用机理研究的最新进展,以及在改良植物抗性上的应用,以期为通过基因工程方法改良作物抗性提供参考。;Heat shock protein 90 (HSP90) widely mediated stress signal transduction, and plays an important role in the control of normal growth of human cells and in the promoting tumor cell development. At present, HSP90 has become forefront projects of cellular immunity, signal transduction and anti-cancer investigation. The physiological function of HSP90 start later in plant than in animal and fungi
In recent years Hsp90 is available to connect to several telomeric proteins at various phases of cell cycle. in an ATP dependent manner with several cochaperones and provides the maturation of the target protein at a near native state [4]. In budding yeast there are two isoforms of Hsp90; Hsc82 (human ortholog of Hsp90β) which is constitutively expressed in the cell and Hsp82 (human ortholog of Hsp90α) which is induced whenever cells are exposed to any kind of stressed condition. It is known that expression of either one of the two isoforms of Hsp90 is required for yeast viability [5]. The two isoforms share 97% sequence identity and they comprise (1-2) % of the total cytosolic proteins. Hsp90 level is significantly increased in the cell upon exposure to stress including temperature nonphysiological pH nutrient deprivation and malignancy [6]. Recent studies possess unraveled novel jobs of Hsp90 where Hsp90 and its own cochaperone p23 get excited about stabilization SU-5402 of different ...
A tumor-selective cell surface localization of warmth shock protein 70 (Hsp70), the major heat-inducible member of the Hsp70 group, correlates with an increased awareness to lysis mediated by individual normal killer (NK) cells and, therefore, may be of clinical relevance. surprise proteins (Hsps) have already been found to try out essential roles in cancers immunity. Members from the Hsp70 and Hsp90 family members are recognized to chaperone tumor-derived peptides to main histocompatibility complicated (MHC) course I substances to elicit an anticancer immune system response mediated by T cells (Tamura et al 1997). Hsp70, the main heat-inducible person in the Hsp70 group, continues to be detected in the cell surface area of tumor cells however, not on regular cells (Ferrarini et al 1992; Multhoff et al 1995a). This uncommon Hsp70 plasma membrane appearance correlates with an elevated level of sensitivity to allogeneic natural killer (NK) cells (Botzler et al 1996a; Botzler et al 1996b; Multhoff ...
The molecular chaperone Hsp90 plays an essential role in protein biogenesis, where it facilitates folding and suppresses aggregation, and in protein degradation, where it contributes to quality control by promoting the recognition and proteolysis of misfolded proteins. In many cell types, including ECs, Hsp90 also participates in the modulation of intracellular signaling events. Indeed, Hsp90 associates with eNOS and regulates its activity in response to endothelium-specific agonists, such as VEGF.11,12,27 Hsp90 activity is controlled by cochaperones, and AHA1 has been identified as an activator of the ATPase activity of Hsp90.20 The present study was designed to assess in ECs the role of AHA1 in the modulation of Hsp90 activity. Our data demonstrate for the first time in primary ECs that changes in AHA1 protein levels influence eNOS phosphorylation and its association with Hsp90 in response to VEGF treatment. In turn, this affects NO production, which contributes to endothelial migration, ...
Polymer-block-peptide conjugates are tailored to render hydrophobic small molecule drugs water soluble. The combinatorial strategy selects for bioconjugates that exhibit sequence-specific solubilization and switchable release profiles of the cargo through incorporation of a disulfide linker moiety into the peptide-library design. While the study focused on the photosensitizer m-THPC and reductive carrier cleavage, the approach is generic and might be expanded toward a broad range of poorly soluble small-molecule drugs and other selective cleavage mechanisms to disassemble a peptide binding domain of the bioconjugate-based solubilizer. Wieczorek, Sebastian; Vigne, Sara; Masini, Tiziana; Ponader, Daniela; Hartmann, Laura; Hirsch, Anna K. H.; Boerner, Hans G.
Title: 17 AAG for HSP90 Inhibition in Cancer - From Bench to Bedside. VOLUME: 9 ISSUE: 5. Author(s):Saad Z. Usmani, Robert Bona and Zihai Li. Affiliation:University of Connecticut School of Medicine, 263 Farmington Avenue, Farmington, CT 06030-1601, USA.. Keywords:17-AAG, heat shock protein 90, cancer, clinical trials. Abstract: Heat shock protein 90 (HSP90) family of proteins are ubiquitous molecular chaperones that are involved in folding, activation, maturation and assembly of many proteins that include essential mediators of signal transduction and cell cycle progression. They are abundant in eukaryotic cells and localized to the cytoplasm, mitochondria as well as the endoplasmic reticulum under normal conditions, making up 1-2% of all cellular proteins. HSP90 proteins have increased expression in a number of malignancies. A large number of HSP90 client proteins have been shown to be necessary for the development, proliferation and survival of specific types of cancers. HSP90 inhibition can ...
First, alterations in thermotolerance were linked to alterations in heat tolerance by three different types of genetic manipulation: inhibiting HSP101 expression through the production of antisense RNAs or by cosuppression of impaired thermotolerance, whereas overexpressing HSP101 enhanced it. Second, in each case, multiple independent transformants that affected HSP101 in the same way displayed the same change in thermotolerance, and no transformants that substantially affected HSP101 expression failed to affect thermotolerance. Third, in experiments in which conditions were sensitive enough to detect them, dosage relationships were apparent. Constitutive lines with the highest levels of HSP101 expression were the best able to withstand heat stress, and antisense lines with the strongest inhibition of HSP101 expression were the most severely affected by heat stress. Fourth, changes in HSP101 expression altered both acquired and basal thermotolerance.. Finally, when the effects of antisense and ...
Tah1 [TPR (tetratricopeptide repeat)-containing protein associated with Hsp (heat-shock protein) 90] has been identified as a TPR-domain protein. TPR-domain proteins are involved in protein-protein interactions and a number have been characterized that interact either with Hsp70 or Hsp90, but a few can bind both chaperones. Independent studies suggest that Tah1 interacts with Hsp90, but whether it can also interact with Hsp70/Ssa1 has not been investigated. Amino-acid-sequence alignments suggest that Tah1 is most similar to the TPR2b domain of Hop (Hsp-organizing protein) which when mutated reduces binding to both Hsp90 and Hsp70. Our alignments suggest that there are three TPR-domain motifs in Tah1, which is consistent with the architecture of the TPR2b domain. In the present study we find that Tah1 is specific for Hsp90, and is able to bind tightly the yeast Hsp90, and the human Hsp90α and Hsp90β proteins, but not the yeast Hsp70 Ssa1 isoform. Tah1 acheives ligand discrimination by ...
Heat shock protein 90 (Hsp90) is an ubiquitous molecular chaperone protein that is involved in folding, activation, and assembly of many proteins, including key mediators of signal transduction, cell cycle control, and transcriptional regulation. In cancer cells that are dependent upon Hsp90 client proteins, the degree to which clients are inhibited correlates closely with induction of growth inhibition and apoptosis with Hsp90 inhibitory drugs. The active pharmaceutical ingredient of CNF2024, CF1983 mesylate, is a synthetic, new chemical entity designed to inhibit Hsp90. CF1983 hada strong affinity for tumor derived Hsp90 and weaker affinity for Hsp90 isolated from normal cells or recombinant Hsp90 ...
Functional roles of heat shock proteins (HSP). The evolutionarily conserved molecular chaperones of the HSP70 (HSPA) family fulfill an essential role in maintai
Previously we demonstrated that Heat shock protein 27 (HSP27) has atheroprotective effects [Circ Res 2008].PURSPOSE: To determine if HSP27 may provide an effective strategy to enhance re-endothelialization of injured vessels, including stented arteries. 72 male and female wild type (WT) and HSP27 over-expressing (HSP27o/e) mice were fed a normal chow and subjected to femoral artery wire injury before being euthanized on days 7, 14 or 28. The circulating CD45dim/Sca-1+/Flk-1+ endothelial progenitor cells (EPCs) from HSP27o/e mice increased 2.8- and 2.7-fold on days 3 and 7 post injury compared to WT (p,0.05). Re-endothelialization increased by 67% and 65% in HSP27o/e males and females on day 7 relative to WT mice (e.g., males: 78.4±7.5% vs. 47.0±6.9%; females: 80.9±4.9% vs. 48.9±4.6%; p,0.05 for both sexes). By 28 days the intima:media ratio was reduced by 52% and 75% in male and female HSP27o/e mice respectively (e.g., males: 0.34±0.06 vs. 0.71±0.14 and females: 0.14±0.05 vs. 0.57±0.06; ...
Complete information for HSPA2 gene (Protein Coding), Heat Shock Protein Family A (Hsp70) Member 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Grace Salsbury*: Characterising the role of molecular chaperone systems in the defective trafficking of mutant channel complexes in the long QT syndromePlatelet transcriptomics and thrombosis, with Prof Paul ...
人Heat Shock Protein 27 ELISA试剂盒(HSP27) ELISA试剂盒datasheet (ab108862).Abcam抗体、ELISA、激动剂拮抗剂、表观遗传试剂、蛋白多肽,使用效果保证,中国70%以上现货。
Hsp90 as a capacitor for morphological evolution. A high-affinity confrontation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
Hsp70 chaperones are required for key cellular processes and response to environmental changes and survival but they have not been fully characterized yet. The human hsp70-gene family has an unknown number of members (eleven counted over ten years ago); some have been described but the information is incomplete and inconsistent. A coherent body of knowledge encompassing all family components that would facilitate their study individually and as a group is lacking. Nowadays, the study of chaperone genes benefits from the availability of genome sequences and a new protocol, chaperonomics, which we applied to elucidate the human hsp70 family. We identified 47 hsp70 sequences, 17 genes and 30 pseudogenes. The genes distributed into seven evolutionarily distinct groups with distinguishable subgroups according to phylogenetic and other data, such as exon-intron and protein features. The N-terminal ATP-binding domain (ABD) was conserved at least partially in the majority of the proteins but the C-terminal
HEADER CHAPERONE 05-JUN-12 4AWQ TITLE COMPLEX OF HSP90 ATPASE DOMAIN WITH TROPANE DERIVED INHIBITORS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: ATPASE DOMAIN, RESIDUES 9-236; COMPND 5 SYNONYM: HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA ANTIGEN COMPND 6 NY-REN-38, HSP90; COMPND 7 EC: 3.6.4.10; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CHAPERONE EXPDTA X-RAY DIFFRACTION AUTHOR J.C.LOUGHEED,T.J.STOUT REVDAT 2 28-JUN-17 4AWQ 1 REMARK REVDAT 1 29-AUG-12 4AWQ 0 JRNL AUTH J.BUSSENIUS,C.M.BLAZEY,N.AAY,N.K.ANAND,A.ARCALAS,T.BAIK, JRNL AUTH 2 O.J.BOWLES,C.A.BUHR,S.COSTANZO,J.K.CURTIS,S.C.DEFINA, JRNL AUTH 3 L.DUBENKO,T.S.HEUER,P.HUANG,C.JAEGER,A.JOSHI,A.R.KENNEDY, JRNL AUTH 4 A.I.KIM,K.LARA,J.LEE,J.LI,J.C.LOUGHEED,S.MA,S.MALEK, JRNL ...
HEADER CHAPERONE 05-JUN-12 4AWP TITLE COMPLEX OF HSP90 ATPASE DOMAIN WITH TROPANE DERIVED INHIBITORS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: ATPASE DOMAIN, RESIDUES 9-236; COMPND 5 SYNONYM: HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA ANTIGEN COMPND 6 NY-REN-38, HSP90; COMPND 7 EC: 3.6.4.10; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CHAPERONE, INHIBITOR EXPDTA X-RAY DIFFRACTION AUTHOR J.C.LOUGHEED,T.J.STOUT REVDAT 1 29-AUG-12 4AWP 0 JRNL AUTH J.BUSSENIUS,C.M.BLAZEY,N.AAY,N.K.ANAND,A.ARCALAS,T.BAIK, JRNL AUTH 2 O.J.BOWLES,C.A.BUHR,S.COSTANZO,J.K.CURTIS,S.C.DEFINA, JRNL AUTH 3 L.DUBENKO,T.S.HEUER,P.HUANG,C.JAEGER,A.JOSHI,A.R.KENNEDY, JRNL AUTH 4 A.I.KIM,K.LARA,J.LEE,J.LI,J.C.LOUGHEED,S.MA,S.MALEK, JRNL AUTH 5 ...
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The heat-shock protein 90 (HSP90) family is a group of highly conserved molecular chaperones with important functions in protein folding and in signal transduction. The HSP90 protein structure is so well conserved that some HSP90 antibodies are reactive with a broad range of species from humans to chickens.
Get this from a library! Immunity, tumors and aging : the role of HSP70. [Igor Malyshev] -- The book is dedicated to the topical area of biology and medicine and the role of stress proteins HSP70 in the regulation of intracellular protein homeostasis, signaling transduction and cell ...
View mouse Hsp90b1 Chr10:86690209-86705509 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
View mouse Hsp90ab1 Chr17:45567778-45573261 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
JG-98, an allosteric heat shock protein 70 (Hsp70) inhibitor, which binds tightly to a conserved site on Hsp70 and disrupts the Hsp70-Bag3 interaction. JG-98 shows anti-cancer activities affecting both cancer cells and tumor-associated macrophages. - Mechanism of Action & Protocol.
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The protein encoded by this gene contains an atypical heat shock protein 70 (Hsp70) ATPase domain and is therefore a distant member of the mammalian Hsp70 family. This gene may be involved in susceptibility to atherosclerosis. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2015 ...
Method: Induction of HSP70B mRNA is carried out by treatment of cells with TRC051384 (6.25 and 12.5 μM) for 4 hours duration for HeLa cell line and total RNA is isolated. For all RNA samples, cDNAs are synthesized and expression of HSP70B mRNA along with expression of 18S rRNA is monitored by real-time PCR employing ABI 7000 system.. ...
HSP27, clone: STRSN, eBioscience™ 25μg; Unconjugated HSP27, clone: STRSN, eBioscience™ Primary Antibodies He to Hf
Chaperonopathies and chaperonotherapy. Hsp60 as therapeutic target in cancer: potential benefits and risks.: In this minireview we focus on Hsp60 as a target fo
At the cellular level, the stress response involves the synthesis of a highly conserved family of heat shock proteins (Hsps). These proteins are essential for maintenance of cellular homeostasis, both in times of stress and in normal cell functioning. Some of the most abundant forms of Hsps in the cell are members of the 70 kDa family. Intracellular heat shock protein 70 (Hsp70) expression in response to proteotoxicity is a highly conserved cellular stress response, but little is known about the role of extracellular Hsp70 (eHsp70) in fish. In order to begin characterizing eHsp70 in fish, the hypothesis that an acute stressor will elevate plasma Hsp70 levels in rainbow trout (Oncorhynchus mykiss) was tested. Subsequent in vitro studies examined whether eHsp70 level was modulated by cortisol and if this involved the action of the glucocorticoid receptor (GR), a ligand-activated transcription factor. The effect of cortisol on the eHsp70 response is important to consider because this steroid is ...
The human heat-shock protein multigene family comprises several highly conserved proteins with structural and functional properties in common, but which vary in the extent of their inducibility in response to metabolic stress. We have isolated and characterized a novel human HSP70 cDNA, HSP70B cDNA, and its corresponding gene sequence. HSP70B cDNA hybrid-selected an mRNA encoding a more basic 70 kDa heat-shock protein than both the major stress-inducible HSP70 and constitutively expressed HSC70 heat-shock proteins, which in common with other heat-shock 70 kDa proteins bound ATP. The complete HSP70B gene was sequenced and, like the major inducible HSP70 gene, is devoid of introns. The HSP70B gene has 77% sequence similarity to the HSP70 gene and 70% similarity to HSC70 cDNA, with greatest sequence divergence towards the 3-terminus. The HSP70B gene represents a functional gene, as indicated by Northern-blot analysis with specific oligonucleotides, hybrid-selected translation with a specific ...
TY - JOUR. T1 - Structure and expression of the human gene encoding major heat shock protein HSP70. AU - Wu, B. AU - Hunt, C. AU - Morimoto, R. PY - 1985/2. Y1 - 1985/2. N2 - We have cloned a human gene encoding the 70,000-dalton heat shock protein (HSP70) from a human genomic library, using the Drosophila HSP70 gene as a heterologous hybridization probe. The human recombinant clone hybridized to a 2.6-kilobase polyadenylated mRNA from HeLa cells exposed to 43 degrees C for 2 h. The 2.6-kilobase mRNA was shown to direct the translation in vitro of a 70,000-dalton protein similar in electrophoretic mobility to the HSP70 synthesized in vivo. From the analysis of S1 nuclease-resistant mRNA-DNA hybrids, the HSP70 gene appears to be transcribed as an uninterrupted mRNA of 2.3 kilobases. We show that the cloned HSP70 gene contains the sequences necessary for heat shock-induced expression by two criteria. First, hamster cells transfected with a subclone containing the HSP70 gene and flanking sequences ...
Extracellular heat shock protein-90 (eHsp90) proteins, which include the membrane-bound, released and secreted forms were first cited in scientific literature late in the 70s. It was not until the recent decade that researchers began to understand the role of exported Hsp90 in normal and tumor cells. In normal cells, Hsp90 is secreted in response to tissue injury. Tumor cells, on the other hand, have managed to constitutively secrete Hsp90 for the purpose of tissue invasion. Cells abundantly store Hsp90 in their cytoplasm, insuring a sufficient supply of extracellular Hsp90 at a moments notice. A well-characterized function of secreted Hsp90α is to promote cell motility, a crucial event in both wound healing and cancer. One of the primary targets for extracellular Hsp90α is the cell surface LRP-1 receptor. The promotility activity of secreted Hsp90α resides within a fragment at the boundary between linker region and middle domain. Inhibiting Hsp90α secretion, neutralizing its extracellular ...
The ability to resolve protein members of the hsp70 multigene family by two-dimensional Western blotting permitted the characterization of antibodies which were specific in discriminating constitutively expressed hsc70 isoforms from stress-inducible hsp70 isoforms. This antibody characterization demonstrated that basal levels of hsp70 isoforms were present in the cerebellum of the control rabbit and that these were elevated following hyperthermia, whereas levels of hsc70 were similar in control and hyperthermic tissue. Multiple isoforms of hsp70 were detected but tissue-specific differences were not apparent in various organs of the rabbit. However, species differences were observed as fewer hsp70 isoforms were noted in rat and mouse. In the control rabbit, higher levels of hsc70 protein were present in neural tissues compared to non-neural tissues. Following physiologically relevant hyperthermia, induction of hsp70 was greatest in non-neural tissues such as liver, heart, muscle, spleen, and kidney
Nucleotide binding to the 70 kDa heat-shock cognate protein (Hsc70) from mung bean seeds and pig brain was investigated, as well as the clathrin uncoating activity of Hsc70 in the presence of these nucleotides. The two enzymes were found to behave identically. ATP bound to two different forms of Hsc70, with dissociation constants of 1.1±0.1 µM and 1.4±0.7 mM respectively at 25 °C. This corresponds to ΔG0´ = -34 and -16 kJ/mol respectively. From the temperature-dependence of the dissociation constant of the high-affinity site, ΔH0´ was calculated to -36±2 kJ/mol. This gives ΔS0´ = 6.7 J/mol per K. Adenosine 5´-[γ-thio]triphosphate, ADP, adenosine 5´-[β,γ-imino]triphosphate and adenosine 5´-[β,γ-methylene]triphosphate showed dissociation constants of 2.3, 11, 31 and 284 µM respectively. The order of affinities corresponded to the order of effectiveness in uncoating of pig brain coated vesicles. The implications of these findings for the mechanism of Hsc70 action are discussed. ...
TY - JOUR. T1 - A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE. AU - Sugimoto, Shinya. AU - Higashi, Chihana. AU - Saruwatari, Kozue. AU - Nakayama, Jiro. AU - Sonomoto, Kenji. PY - 2007/6/26. Y1 - 2007/6/26. N2 - We describe importance of the characteristic segment in ATPase domain of DnaK chaperone which is present in all gram-negative bacteria but is absent in all gram-positive bacteria. In vitro studies, ATPase activity, luciferase-refolding activity, and surface plasmon resonance analyses, demonstrated that a segment-deletion mutant DnaKΔ74-96 became defective in the cooperation with the co-chaperones DnaJ and GrpE. In addition, in vivo complementation assay showed that expression of DnaKΔ74-96 could not rescue the viability of Escherichia coli ΔdnaK mutant at 43 °C. Consequently, we suggest evolutionary significance for this DnaK ATPase domain segment in gram-negative bacteria ...
Results: In comparison with non-immune IgG, anti-HSC70 reduced myocardial expression of KC and MCP-1 mRNAs and proteins following I/R. Moreover, treatment with anti-HSC70 improved postischemic cardiac functional recovery (66±5.4% of baseline vs. 28±5.1% of baseline in hearts treated with non-immune IgG, p,0.01). Recombinant HSC70 induced myocardial expression of KC and MCP-1 mRNAs and proteins and caused cardiac dysfunction (72±2.6% of baseline vs. 98±3.9% of baseline in perfusion controls, p,0.001) in hearts with competent TLR4 (C3H/HeN). Interestingly, these effects of HSC70 were abrogated in hearts with defective TLR4 (C3H/HeJ). The potency of HSC70 was completely lost in the absence of its substrate-binding domain.. Conclusions: Taken together, our studies demonstrate, for the first time, that HSC70 plays an important role in the induction of myocardial chemokines and cardiac dysfunction during I/R. The effect of HSC70 is dependent on TLR4 and requires the presence of the ...
TY - JOUR. T1 - Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure. AU - Carrigan, Patricia E.. AU - Sikkink, Laura A.. AU - Smith, David F.. AU - Ramirez-Alvarado, Marina. N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.. PY - 2006/3. Y1 - 2006/3. N2 - The major heat shock protein (Hsp) chaperones Hsp70 and Hsp90 both bind the co-chaperone Hop (Hsp70/Hsp90 organizing protein), which coordinates Hsp actions in folding protein substrates. Hop contains three tetratricopeptide repeat (TPR) domains that have binding sites for the conserved EEVD C termini of Hsp70 and Hsp90. Crystallographic studies have shown that EEVD interacts with positively charged amino acids in Hop TPR-binding pockets (called carboxylate clamps), and point mutations of these carboxylate clamp positions can disrupt Hsp binding. In this report, we use circular dichroism to assess the effects of point mutations and Hsp70/Hsp90 peptide ...
Heat shock proteins (HSPs) are endogenous proteins whose function is to maintain the cells tolerance to insult, and glutamine supplementation is known to increase HSP expression during intense exercise. Since few studies have addressed the possibility that supplementation with other amino acids could have s
Heat shock protein 72 (HSP72) is expressed in response to stress and has been demonstrated to follow a diurnal expression pattern within monocytes and is sensitive to changes in core temperature. Numerous studies have shown changes in HSP72 expression within cell lines exposed to hyperbaric conditions. No studies have investigated changes in HSP72 expression in vivo. Six males participated in the study and were exposed to hyperbaric air and hyperbaric oxygen a week apart. Monocyte HSP72 was analyzed by flow cytometry at 09:00, 13:00, 17:00, 21:00 with hyperbaric oxygen or hyperbaric air breathing commencing at 15:00 for 78 min at a pressure of 2.8 ATA. HSP72 under normoxia followed the established trend; however, following the hyperbaric air or oxygen exposure a reduction in detectable HSP72 was observed at 17:00 and 21:00. No changes in core temperature were observed between 13:00 and 21:00 for any condition. The data show that HSP72 expression is impaired following hyperbaric air (HA) exposure, when
Heat shock proteins (HSPs) are ubiquitous in living organisms. HSPs are an essential component for cell growth and survival; the main function of HSPs is controlling the folding and unfolding process of proteins. According to molecular function and mass, HSPs are categorized into six different families: HSP20 (small HSPS), HSP40 (J-proteins), HSP60, HSP70, HSP90, and HSP100. In this paper, improved methods for HSP prediction are proposed—the split amino acid composition (SAAC), the dipeptide composition (DC), the conjoint triad feature (CTF), and the pseudoaverage chemical shift (PseACS) were selected to predict the HSPs with a support vector machine (SVM). In order to overcome the imbalance data classification problems, the syntactic minority oversampling technique (SMOTE) was used to balance the dataset. The overall accuracy was 99.72% with a balanced dataset in the jackknife test by using the optimized combination feature SAAC+DC+CTF+PseACS, which was 4.81% higher than the
Since the discovery of gp96 in the 1980s as a tumor rejection antigen, Heat Shock Proteins (HSPs) have received attention from immunologists for their ability to prime immune responses. Originally known for their important intracellular roles as chaperones to newly synthesized, misfolded, and/or recently degraded proteins, it is now understood that HSPs released into the extracellular environment can also initiate immune responses. Shown both in vitro and in vivo, HSPs act on antigen presenting cells (APC) to 1) deliver antigenic peptides for presentation by both MHC class I and class II molecules and 2) activate APC to increase expression of co-stimulatory molecules. Both of these activities contribute to productive T cell responses, which has led to current trials using HSP-peptide complexes as cancer vaccines. However, the cell populations responsible for monitoring exogenous HSPs and priming resulting immune responses have yet to be fully characterized. This study identifies the cells ...
This gene encodes a member of the DnaJ or Hsp40 (heat shock protein 40 kD) family of proteins. DNAJ family members are characterized by a highly conserved amino acid stretch called the J-domain and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. The encoded protein is a molecular chaperone that stimulates the ATPase activity of Hsp70 heat-shock proteins in order to promote protein folding and prevent misfolded protein aggregation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015 ...
Current models derived from in vitro studies propose that sHsps prevent irreversible substrate aggregation by binding heat-denatured substrates, and then present substrate to other cellular components for ATP-dependent refolding (Waters et al., 1996; Ehrnsperger et al., 1997;Lee et al., 1997; Veinger et al., 1998). Our data extend this model for sHsp chaperone activity in several important ways. First, we determined that the chaperones required for high levels of refolding of Hsp18.1-bound Luc were Hsp/Hsc70 plus DnaJ homologs. The addition of Hsp90 and Hop gave minimal or no further enhancement of refolding. Despite the eukaryotic origin of Hsp18.1, the highest Luc refolding rates were observed when Hsp18.1-bound Luc was reactivated in the presence of the prokaryotic DnaK system. These findings imply that the mechanism of sHsp action in conjunction with Hsp70 systems is universal among eukaryotes and prokaryotes, and suggest that sHsps may not physically interact with the Hsp70 systems. Also, ...
The ARG1 gene is predicted to encode a 410-aa polypeptide with a molecular mass of 45.5 kDa (Fig. 3A). Database searches revealed that the NH2 terminus shares strong sequence similarity with the highly conserved J domain of DnaJ-like molecular chaperone proteins found in prokaryotes and eukaryotes (Fig. 3 A and B; refs. 49-53). DnaJ-like proteins are involved in a variety of processes including protein folding, protein partitioning into organelles, signal transduction, and targeted protein degradation (54). The J domain has been shown to interact directly with Hsp70, thereby regulating its ATPase activity, which affects protein binding and folding. The Saccharomyces cerevisiae DnaJ-like protein YDJ1, together with Hsp70 and Hsp90, participates in a number of signal-transduction pathways involving steroid hormones as well as tyrosine kinases and serine-threonine kinases (55). Interestingly, these heteroligomeric complexes bind actin filaments in a Ca2+/calmodulin-regulated manner (56).. Computer ...
DNAJC4 (DnaJ heat shock protein family (Hsp40) member C4), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
DNAJC21 (DnaJ heat shock protein family (Hsp40) member C21), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
In the current investigation, we focused on Mortalin/mthsp70/GRP75, a member of the heat shock protein (Hsp) 70 family, which is enriched in human cancer cells [4, 9, 13]. It has been established that Mortalin has various subcellular localizations, interacts with multiple binding partners, and plays a role in carcinogenesis. Also, it is elevated in immortalized cell lines and tumor cells, and additional upregulation of Mortalin expression at later stages of carcinogenesis coincides with the acquisition of invasiveness [4]. Moreover, it has multiple functions contributing to continued proliferation of cancer cells, including mitochondrial-biogenesis, ATP production, anti-apoptosis, chaperoning, inactivation of tumor suppressor p53 and PI3K/AKT activities [14, 15]. Targeting Mortalin by siRNA, ribozymes and small molecules including MKT-077 and Withaferin A resulted in growth arrest/apoptosis of cancer cells [16-22].. Here, we confirmed that the level of Mortalin was elevated in breast cancer, ...
1NGA: Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.
International Journal of Inflammation is a peer-reviewed, Open Access journal that publishes original research and review articles on the molecular basis, cell biology and pharmacology of inflammation, including acute/chronic inflammation, mediators of inflammation, as well as cellular processes and molecular mechanisms involved in the production of inflammatory responses. The journal especially welcomes the submission of articles on anti-inflammatory drug development, trials and therapies.
Authors: Sghaier, Haïtham , Ai, Thuy Le Huyen , Horiike, Tokumasa , Shinozawa, Takao Article Type: Research Article Abstract: Molecular chaperones are a wide group of unrelated protein families whose role is to assist others proteins. Comparably, under environmental stress, stress proteins behave as biocatalysts of protein stabilization. Stress proteins include a large class of proteins that were originally termed heat shock proteins (HSPs) due to their initial discovery in tissues exposed to elevated temperatures. Many, but not all, stress proteins and HSPs are molecular chaperones. Moreover, not all HSPs are derivable from stress. HSPs …are structurally diversified by the contribution of various domains having specific roles. HSPs have been grouped, mainly on the basis of their molecular masses, into specific families that include small HSPs (sHSPs)/α-crystallins, HSP10s, HSP40s, HSP60s, HSP70s, HSP90s, HSP100s and HSP110s. The names of these major families are historical artefacts with ...
This gene is a member of the J protein family. J proteins function in many cellular processes by regulating the ATPase activity of 70 kDa heat shock proteins. This gene is a member of the type 2 subgroup of DnaJ proteins. The encoded protein is localized to the endoplasmic reticulum. This protein is induced by endoplasmic reticulum stress and plays a role in protecting stressed cells from apoptosis. [provided by RefSeq, Dec 2010 ...
Alzheimers disease (AD) is the most prevalent neurodegenerative pathology in the growing population of elderly humans and leads eventually to dementia and death. Despite tremendous efforts, no effective treatment for AD is currently available. The severity of cognitive impairment in patients with AD usually correlates with the extent of the observed abnormality of neurons, including the quantity of neurofibrillary tangles, the decrease in synaptic density, the enhanced concentration of soluble Aβ-amyloid oligomers, and the amount of neurons that die by apoptosis (1). Heat shock proteins (Hsps) have emerged as critical regulators of neurodegenerative processes associated with protein misfolding in the brains of AD patients (2). Various data suggest that Hsp70 and other molecular chaperones function as a complex neuroprotective system, which fails in the brains of AD patients. Hsp70 confer protection against oxidative stress and inflammation which play a major role in many age-related ...
Heat shock proteins are synthesized in response to increased growth temperatures and other stress factors in virtually all organisms. The analysis of the molecular mechanism of Hsps has so far been focused mostly on the ATP‐dependent Hsp70 and GroE families, whereas the function of the members of the ATP‐independent group of small Hsps is still poorly understood.. While the expression of Hsps is ubiquitous and a similar set of proteins is produced from prokaryotes to mammals, the importance and apparent function of the different Hsps seem to vary in different organisms (Parsell and Lindquist, 1994). In yeast, thermotolerance is conveyed predominantly by Hsp104, whereas in Drosophila Hsp70 seems to be the important factor. Finally, GroE is essential for protein folding in prokaryotes and organelles; however, a functional counterpart seems to be lacking in the eukaryotic cytosol, since the structurally related TCP‐1 complex appears to be restricted to actin and tubulin folding (Lewis et al., ...
The 60 kDa heat shock protein (HSP60) has been reported to influence T-cell responses in two ways: as a ligand of toll-like receptor 2 signalling and as an antigen. Here we describe a new mechanism of T-cell immuno-regulation focused on HSP60: HSP60 is up-regulated and presented by activated T cells (HSP60 is an ergotope) to regulatory (anti-ergotypic) T cells. Presentation of HSP60 by activated T cells was found to be MHC-restricted and dependent on accessory molecules - CD28, CD80 and CD86. Anti-ergotypic T cells responded to T-cell HSP60 by proliferation and secreted IFNγ and TGFβ1. In vitro, the anti-ergotypic T cells inhibited IFNγ production by their activated T-cell targets. In vivo, adoptive transfer of an anti-ergotypic HSP60-specific T-cell line led to decreased secretion of IFNγ by arthritogenic T cells and ameliorated adjuvant arthritis (AA). Thus, the presentation of HSP60 by activated T cells turns them into targets for anti-ergotypic regulatory T cells specific for HSP60. ...
The administration of the H2O2-specific scavenger catalase attenuated the generation of apoptosis by the antitumor drugs etoposide, camptothecin, doxorubicin, and cisplatin in U-937 human promonocytic cells. By contrast, the antioxidant potentiated the generation of apoptosis by the inducers of the stress response, heat shock and cadmium, in this and other myeloid cell types. Catalase also increased the heat shock-provoked stimulation of caspase-3 and -9 activities, as well as the release of cytochrome c from mitochondria to the cytosol. The potentiation of cell death by catalase correlated with its capacity to inhibit the stress response, as demonstrated by the suppression of 70- or 27-kDa heat-shock protein expression and the inhibition of heat-shock transcription factor 1 binding activity. Conversely, the toxicity of catalase plus heat shock was attenuated when the cells were preconditioned with a soft heating, which elevated the 70-kDa heat-shock protein levels. By contrast with catalase, ...
TY - JOUR. T1 - HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor. AU - Patricia Hernández, M.. AU - Chadli, Ahmed. AU - Toft, David O.. PY - 2002/4/5. Y1 - 2002/4/5. N2 - The progesterone receptor (PR) can be isolated in its native conformation able to bind hormone, yet its ligand-binding domain rapidly loses its activity at elevated temperature. However, an in vitro chaperoning system consisting of five proteins (HSP40, HSP70, HOP, HSP90, and p23) with ATP is capable of restoring this function. The first step of this chaperoning mechanism is usually thought to be the binding of HSP70 to PR. Our findings here show that the binding of HSP40 to PR is, instead, the first step. HSP40 binding occurred rapidly and was not dependent on ATP or other proteins. The stoichiometry of HSP40 to native PR in these complexes was ∼1:1. HSP40 bound specifically and with a high affinity to native PR (Kd = 77 nM). The binding of HSP40 to PR was sustained and did not ...
Magmas-like proteins have been previously implicated in tethering the J-proteins to the translocation channel (16, 17). Our results indicate that Magmas, in addition to its conserved function at human presequence translocase, regulates the distribution of individual J-proteins associated with the complex and thereby activates the translocases for neoplastic transformation under overexpressed conditions. In agreement with the idea, intrinsic overexpression of Magmas in prostate cancer and pituitary adenomas remodels the J-protein distribution at the TIM23 complex. A similar phenotype was observed upon exogenous elevation of Magmas protein levels that lead to redistribution and recruitment of J-proteins to either of the translocases, suggesting that Magmas plays a critical role in governing translocase activity. Indeed, reorganization of J-proteins at the import channel results in equivalent translocation activity for both translocases, and they play a synergistic role in the import of precursors ...
Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs. Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species. As their name implies, heat shock proteins protect cells when stressed by elevated temperatures. They account for 1-2% of total protein in unstressed cells. However, when cells are heated, the fraction of heat shock proteins increases to 4-6% of cellular proteins. Heat shock protein 90 (Hsp90) is one of the most common of the heat-related proteins. The 90 comes from the fact that it weighs roughly 90 kiloDaltons. A 90 kDa protein is considered fairly large for a non-fibrous protein. Hsp90 is found in bacteria and all branches of eukarya, but it is apparently absent in archaea. Whereas ...
Inhibition of the ATPase activity of the chaperone protein HSP90 is a potential strategy for treatment of cancers. We have determined structures of the HSP90alpha N-terminal domain complexed with the purine-based inhibitor, PU3, and analogs with enhanced potency both in enzyme and cell-based assays. The compounds induce upregulation of HSP70 and downregulation of the known HSP90 client proteins Raf-1, CDK4, and ErbB2, confirming that the molecules inhibit cell growth by a mechanism dependent on HSP90 inhibition. We have also determined the first structure of the N-terminal domain of HSP90beta, complexed with PU3. The structures allow a detailed rationale to be developed for the observed affinity of the PU3 class of compounds for HSP90 and also provide a structural framework for design of compounds with improved binding affinity and drug-like properties ...
The emergence of complementary electrostatic potentials after the prokaryotic-to-eukaryotic split drives physical and functional cooperation between canonical class A and class B J-proteins to boost protein disaggregation.
In the present study, we have shown that long-term administration of Ang II increases expression of HSP70 and HSP25, as well as HSP32 (HO-1), in the rat kidney. Losartan completely blocked Ang II-induced upregulation of all 3 HSPs. On the other hand, hydralazine completely blocked Ang II-induced HO-1 upregulation but failed to block Ang II-induced upregulation of HSP70 or HSP25, which suggested that different mechanisms may regulate Ang II-induced HO-1 upregulation compared with renal HSP70 and HSP25 induction in the kidney. Interestingly, NE did not alter expression of these HSPs, suggesting that hypertension alone was not a sufficient stimulus to increase renal expression of these HSPs.. We found that HSP70 is upregulated in the rat kidney with long-term infusion of Ang II but not NE. Xu et al18 have previously reported that HSP70 was induced in the rat kidney after bolus vasopressin injection. They also showed that vasopressin-induced upregulation of renal HSP70 is a pressor-independent ...
In field trials, heat-exposed chickens given Actigen®, a second generation mannan oligosaccharide (MOS) from Saccharomyces cerevisiae, maintained good intestinal health and performance. This investigation explored the influence of Actigen® on heat shock protein (HSP) responses in Ross 708 broiler chickens. Gender-segregated broilers were given either a control or Actigen®-supplemented (800 g/ton in starter, 400 g/ton in grower and 200 g/ton in finisher) diet over a 6 week growing period. At 3 and 6 weeks of age, broilers of each gender on each diet were exposed to 41°C for 1 h in a temperature-controlled chamber while controls were maintained at 24°C. After heat exposure, liver and ileum tissues were collected and preserved in RNAlater for determination of gene expression via Real Time PCR. Significant differences in mRNA expression for HSP90A, HSP90AA and HSP90B due to gender were found in the ileum, but no gender-related differences for these HSPs were found in the liver. In all ...
TY - JOUR. T1 - Extracellular Hsp70 Enhances Mesoangioblast Migration via an Autocrine Signaling Pathway. AU - Sconzo, Gabriella. AU - Geraci, Fabiana. AU - Spinello, Walter. AU - Barreca, Maria Magdalena. AU - Cavalieri, Vincenzo. AU - Tinnirello, Rosaria. AU - Turturici, Giuseppina. AU - Tinnirello, Rosaria. AU - Kaur, Punit. AU - Geraci, Fabiana. AU - Asea, Alexzander A. A.. PY - 2017. Y1 - 2017. N2 - Mouse mesoangioblasts are vessel-associated progenitor stem cells endowed with the ability of multipotent mesoderm differentiation. Therefore, they represent a promising tool in the regeneration of injured tissues. Several studies have demonstrated that homing of mesoangioblasts into blood and injured tissues are mainly controlled by cytokines/chemokines and other inflammatory factors. However, little is known about the molecular mechanisms regulating their ability to traverse the extracellular matrix (ECM). Here, we demonstrate that membrane vesicles released by mesoangioblasts contain Hsp70, ...
TY - JOUR. T1 - IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis. AU - Hung, Chin Sheng. AU - Huang, Chien Yu. AU - Lee, Chia Hwa. AU - Chen, Wei Yu. AU - Huang, Ming Te. AU - Wei, Po Li. AU - Chang, Yu Jia. PY - 2017. Y1 - 2017. N2 - Heat shock protein 27 (Hsp27) is a key chaperone that interacts with over 200 client proteins. The expression of Hsp27 might be correlated with poor outcome in many types of cancer. Previous study indicated that Hsp27 might be an important biomarker in hepatocellular carcinoma (HCC). However, the detailed mechanism is less well understood. The shRNA-mediated silencing of Hsp27 decreased the proliferation, migration and invasion of HCC cells. In a xenograft model, the silencing of Hsp27 reduced tumor progression. We revealed that the silencing of Hsp27 led to a reduction in insulinlike growth factor binding protein 2 (IGFBP2), which might mediate proliferation and metastasis through vimentin, snail and beta-catenin. ...
hsp18.5, heat, shock, protein, 18.5, Hsp18.5 | heat shock protein 18.5, Anti-HSP18.5 | clss IV heat shock protein ANTIBODY, O64564.1, AS11 1628
Although heat shock proteins are best characterized in associated with temperature, mounting evidence suggests that heat shock proteins are expressed and play vital roles during many types of cell stress. Heat shock proteins work by helping other proteins fold properly and have been classified in a functional category of proteins called molecular chaperones. Molecular chaperones catalyze the folding of a newly-translated peptide into the secondary and tertiary structures that characterize the mature protein product. Improperly-folded proteins are unstable, prone to aggregation, and dysfunctional. Correct protein folding is extremely important for protein and cell function. . Alterations in protein structure, including secondary and tertiary structure, lead to altered protein function. Similarly, improperly or incompletely folded proteins are likely to be dysfunctional and lead to complications for the cell. It should come as no surprise that improper protein folding in cells of the human body ...
HSP25 is a member of the ubiquitous family of small heat shock proteins belonging to the big class of stress proteins. It is related to acquiring of cellular thermotolerance, can act as molecular chaperone, is able to inhibit polymerization of actin in vitro and can form high molecular weight complexes. In this thesis the isolation, structural and functional characteri-zation of this protein as well as its abundance in different tissues of rats suffering on patho-logical forms of hypertension is analyzed: · A method for rapid isolation of HSP25 out of Ehrlich-ascites-tumor (EAT) was estab-lished. From isolated HSP25 low and high molecular weight material could be obtained. · Analysis of high molecular weight complexes by means of electron microscopy and ana-lytical ultracentrifugation results in a structural model characterized by a cylindrical structure composed of four stacked rings each containing eight HSP25 monomers. · High-molecular weight complexes of recombinant HSP25 are organized as ...
Unfolded proteins in the endoplasmic reticulum (ER) activate the ER transmembrane sensor Ire1 to trigger the unfolded protein response (UPR), a homeostatic signaling pathway that adjusts ER protein folding capacity according to need. Ire1 is a bifunctional enzyme, containing cytoplasmic kinase and RNase domains whose roles in signal transduction downstream of Ire1 are understood in some detail. By contrast, the question of how its ER-luminal domain (LD) senses unfolded proteins has remained an enigma. The 3.0-A crystal structure and consequent structure-guided functional analyses of the conserved core region of the LD (cLD) leads us to a proposal for the mechanism of response. cLD exhibits a unique protein fold and is sufficient to control Ire1 activation by unfolded proteins. Dimerization of cLD monomers across a large interface creates a shared central groove formed by alpha-helices that are situated on a beta-sheet floor. This groove is reminiscent of the peptide binding domains of major ...
Background: In a previous study, we found that heat shock protein 27 (HSP27) was over-expressed in gastric adenocarcinoma (GA) tissue. In this study, our goal was to further verify the expression profile of HSP27 in patients with GA. Methods: Western blot and immunohistochemistry were employed to determine HSP27 expression in 50 paired tumor and adjacent normal tissue. ELISA was used to quantify serum HSP27 concentrations in the same 50 GA patients and 50 healthy individuals. Results: Compared to adjacent normal tissues, HSP27 was over-expressed in 25 (50%, p=0.000) and 24 (48%, p=0.000) cases of GA tissue by Western blot and immunohistochemistry, respectively. ELISA revealed significantly higher serum concentrations of HSP27 in patients with GA patients (mean=986 pg/mL) compared to healthy individuals (mean=573 pg/mL) (p=0.003). In addition, infection with Helicobacter pylori (HP) in healthy individuals was associated with increased expression of HSP27 in both gastric mucosa and serum. ...
The impact of microRNAs (miRNAs) known to regulate numerous biologic processes on complement-dependent cytotoxicity (CDC) was investigated in K562 cells. The C5b-9 complex is the executioner of CDC. Cells protect themselves from CDC by C5b-9 elimination, a process involving the mitochondrial chaperone mortalin/GRP75. Potential miR-200 (b and c) and miR-217 regulatory sites were identified in mortalin mRNA. Overexpression of miR-200b/c or miR-217 lowered the expression of mortalin mRNA. miRNA inhibitors for miR-200b, miR-200c, or miR-217 enhanced mortalin mRNA level. Unexpectedly, these miRNA modulators had no significant effect on mortalin protein level. Metabolic labeling analysis demonstrated that, to compensate for reduction in mortalin mRNA level, the cells increased the rate of synthesis of mortalin protein. Cells overexpressing miR-200b/c or miR-217 showed reduced sensitivity to CDC, whereas inhibition of miR-200c and miR-217 enhanced cell death. miR-200b/c overexpression reduced C5b-9 ...
Pharmacological inhibition of molecular chaperone Hsp90 is an attractive approach for anticancer therapy, since the chaperone activity of Hsp90 is critical for the stability and activity of a variety of cellular client proteins. The list of Hsp90 client proteins is always expanding and includes transcription factors, steroid hormone receptors, protein kinases, oncogenes, proto-oncogenes and signaling molecules.1,2 Since many of these client proteins promote tumor growth, metastasis and angiogenesis, inhibition of Hsp90 can be the one punch that cripples the tumorigenic and metastatic potential of tumors regardless of their tissue or cellular origin. Hsp90 inhibitors have been combined with a variety of chemotherapy and targeted treatment drugs, but the rationale for such combinations is largely empirical. The study by Iwai et al. not only demonstrates potent synergistic antitumor activity upon combining a Wee1 kinase inhibitor and several Hsp90 inhibitors, but the rationale for simultaneous ...
Recently, it has been shown that Akt can be immunoisolated in a complex with hsp90 from cell lysates via a direct interaction between residues 229-309 of Akt and residues 327-340 of the M domain of hsp90.19 In cells, the binding of hsp90 to Akt prevents dephosphorylation of threonine 308 by reducing PP2A-mediated dephosphorylation. To verify the interaction between hsp90 and Akt in our system, we incubated recombinant Akt or endothelial cell lysates with GST-N, -M, and -C domains of hsp90. As seen in Figure 3B, recombinant Akt (left panel) or Akt from cell lysates (right panel) does not significantly interact with GST alone, but interacts with the M domain of hsp90 and binds to a lesser extent to the C domain. The low-level binding to the C domain may represent an additional site of interaction to stabilize Akt to hsp90. The binding of Akt to residues 327-340 and eNOS to residues 442-600 of hsp90β of the M domain suggests that hsp90 can serve as a scaffold for the kinase and it substrate. To ...
Hsp90α is a molecular chaperone protein involved in the structural maturation of oncogenic signaling proteins. Hsp90 was recently identified as an anticancer target; various studies are ongoing to find ways for managing cancer through Hsp90α. However, this approach is limited by reported side-effects. Hypoxia is a hallmark of solid tumors, including those of breast cancer and the extent of tumor hypoxia is associated with resistance to treatment and poor prognosis. One of the major signaling pathways in cancer cells, the Jak2/STAT5b pathway, has been found to be closely correlated with hypoxia. The objective of this study was to investigate the role of Jak2/STAT5b in the regulation of Hsp90α expression so that Hsp90α targeting can be achieved indirectly by modulating the Jak2/STAT5b pathway. We examined the role of the Jak2/STAT5b pathway in the expression of Hsp90α under hypoxic conditions by immunoblotting, reporter gene assays, EMSA and RNA interference analysis. With the help of in vivo ...
Multidrug resistance is a reoccurring obstacle faced in the chemotherapeutic treatments of cancer. Multidrug resistance (MDR) is characterized by high levels of resistance to a number of chemically unrelated drugs. MDR is established in cell lines by expressing high levels of plasma membrane efflux pumps such as P-glycoprotein and MRP-1, both members of the ABC superfamily of transporters. These transporters decrease cellular levels of a particular drug, and through a molecular mechanism not yet identified, also create cellular resistance for other drugs. Interestingly, in a number of cases associated with MDR, cell lines have shown signs of reverse transformation. Reverse transformation is a phenomenon that occurs in transformed cell lines, in which the malignant cells revert back to a normal phenotype and become significantly less tumorigenic ...
Description: The heat-shock proteins (HSPs) belong to a larger group of polypeptides, the stress proteins, that are induced in various combinations in response to environmental challenges and developmental transitions. Synthesis of the small (27-kD) HSP has been shown to be correlated with the acquisition of thermotolerance. The deduced 199-amino acid HSP27 protein shows sequence similarity to mammalian alpha-crystallins. Approximately 20% of its residues are susceptible to phosphorylation. The HSP27 gene, which is mapped to 7q11.23 and has 3 exons1, produced a 2.2-kb transcript in an in vitro transcription assay. Decreasing ROS in cells expressing mutant huntingtin, HSP27 protects cells against oxidative stress2. In other words, HSP27 is a suppressor of polyglutamine (polyQ)-mediated cell death3. Furthermore, MAPKAPK5 is a major stress-activated kinase that can phosphorylate HSP27 in vitro.. Primary Antibody. ...
Heat Shock Protein-27, -60 and -90 expression in gastric cancer: association with clinicopathological variables and patient survival
Acknowledgements. This work was supported by National Science Council, Taiwan, ROC. under Grants NSC84-2311-B-002-007 B01 and NSC85-2311-B-002-010 B13 to C.-Y. L.. Literature Cited. Baumann, G., E. Raschke, M. Bevan, and F. Sch ffl. 1987. Functional analysis of sequence required for transcriptional activation of a soybean heat shock gene in transgenic tobacco plants. EMBO J. 6: 1161-1166.. Chang, P.-F.L., M.L. Narasimhan, P.M. Hasegawa, and R.A. Bressan. 1993. Quantitative mRNA-PCR for expression analysis of low-abundance transcripts. Plant Mol. Biol. Rep. 11: 237-248.. Chou, M., Y.M. Chen, and C.Y. Lin. 1989. Thermotolerance of isolated mitochondria associated with heat shock proteins. Plant Physiol. 89: 617-621.. Czarnecka, E., P.C. Fox, and W.B. Gurley. 1990. In vivo interaction of nuclear proteins with the promoter of soybean heat shock gene Gmhsp 17.5E. Plant Physiol. 94: 935-943.. Czarnecka, E., W.B. Gurley, R.T. Nagao, L.A. Mosquera, and J.L. Key. 1985. DNA sequence and transcript mapping ...
The Bcl-2 oncoprotein is a potent inhibitor of apoptosis and is overexpressed in a variety of different malignancies. Bcl-2 function is regulated through heterodimerization with other members of the Bcl-2 protein family. In addition, several proteins that are not members of the Bcl-2 family can bind to Bcl-2, including BAG-1 protein. In this study, we screened for proteins that bind to Bcl-2, and isolated two additional members of the BAG-1 protein family, BAG-3 and BAG-4. The BAG-4 protein that we cloned also corresponds to the recently isolated suppressor of death domains (SODD) protein, a molecule that binds and inhibits signaling by tumor necrosis factor receptor 1 (TNFR1). Both BAG-3 and BAG-4/SODD were found to physically associate with Bcl-2, and both proteins are well conserved from human to mouse. A region of homology, comprising 68 amino acids, is present in the carboxyl termini of BAG-3 and BAG-4/SODD, and this region corresponds with sequences termed BAG domains that are found in ...
Heat shock proteins Hsp70 Milner CM, Campbell RD (1990). "Structure and expression of the three MHC-linked HSP70 genes". ... Heat shock 70kDa protein 1B, also known as HSPA1B, is a human gene. This intronless gene encodes a 70kDa heat shock protein ... which is a member of the heat shock protein 70 family. In conjunction with other heat shock proteins, this protein stabilizes ... "Entrez Gene: HSPA1A heat shock 70kDa protein 1B". Ito Y, Ando A, Ando H, Ando J, Saijoh Y, Inoko H, Fujimoto H (August 1998). " ...
DnaJ heat-shock proteins play a role in regulating the ATPase activity of Hsp70 heat-shock proteins. Besides stimulating the ... In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein. It is ... The J domain of DnaJ interacts with Hsp70 heat shock proteins. ... protein family that functions with hsp70 stress proteins". ... Douglas MG, Cyr DM, Langer T (1994). "DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70". Trends ...
Michels AA, Kanon B, Bensaude O, Kampinga HH (2000). "Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells". J ... 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and ... a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone ... Hata M, Okumura K, Seto M, Ohtsuka K (Mar 1997). "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its ...
Additionally, NFAT5 induces heat shock proteins, Hsp70, and osmotic stress proteins. NFAT5 is also implicated in cytokine ... Nakayama M, Kikuno R, Ohara O (2003). "Protein-protein interactions between large proteins: two-hybrid screening using a ... The largest Rel protein, it consists of nearly 1,500 amino acid residues. Like the other Rel proteins, NFAT5 contains the Rel ... Proteins belonging to this family play a central role in inducible gene transcription during the immune response. This protein ...
September 2003). "Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma". Cancer. 98 (5): 970-7. ... Heat shock protein 60, HSP-60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1 Heat shock protein 60 ( ... Heat shock proteins are primarily responsible for maintaining the integrity of cellular proteins particularly in response to ... Heat shock proteins are amongst the most evolutionarily conserved of proteins. The significant function, structural, and ...
Hashimoto, K; Tomitaka, S; Narita, N; Minabe, Y; Iyo, M; Fukui, S (1996). "Induction of heat shock protein Hsp70 in rat ... "electric shock". Dextromethorphan's effects have been divided into four plateaus. The first plateau (1.5 to 2.5 mg per kg body ...
Heat shock proteins: gp96, hsp70, hsp90, heparin cofactor II, Hepatic lipase, ITGB1BP1, Lactoferrin, Lipoprotein lipase, LPL, ... "CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin". Immunity. 14 (3): 303-13. doi:10.1016/ ... Li Z, Dai J, Zheng H, Liu B, Caudill M (Mar 2002). "An integrated view of the roles and mechanisms of heat shock protein gp96- ... In humans, the LRP1 protein is encoded by the LRP1 gene. LRP1 is also a key signalling protein and, thus, involved in various ...
Hashimoto, K; Tomitaka, S; Narita, N; Minabe, Y; Iyo, M; Fukui, S (1996). "Induction of heat shock protein Hsp70 in rat ...
"Human Heat Shock Protein HSP70 Interacts with HSF, the Transcription Factor That Regulates Heat Shock Gene Expression". Genes ... Morimoto, R.I. (1998). "Regulation of the Heat Shock Transcriptional Response: Crosstalk between a Family of Heat Shock Factors ... "The Structure and Expression of the Human Gene Encoding the Major Heat Shock Protein HSP70". Mol. Cell. Biol. 5 (2): 330-341. ... "Attenuation of the heat shock response in HeLa cells is mediated by the release of bound heat shock transcription factor and is ...
Feder ME (July 1999). "Engineering Candidate Genes in Studies of Adaptation: The Heat-Shock Protein Hsp70 in Drosophila ... Feder on heat-shock proteins and their function in Drosophila melanogaster. Feder designed a holistic approach to study Hsp70, ... He concluded that the results of these studies gave a multi-faceted view of Hsp70. The manipulation of candidate genes is also ... using site-specific homologous recombination and the expression of various proteins), as well as examining the natural ...
Chen S, Smith DF (Dec 1998). "Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery". The ... heat shock protein 90 kDa alpha, class B, member 1) (this protein) HSP90B1 (heat shock protein 90 kDA beta, member 1) TRAP1 ( ... heat shock protein 90 kDa alpha, class A, member 1) HSP90AA3P (heat shock protein 90 alpha family class A member 3, pseudogene ... HSP90AB1 heat shock protein 90 alpha family class B member 1". Retrieved 2019-08-30. Lindquist S (June 1986). "The heat-shock ...
The protein encoded by this gene is an adaptor protein that mediates the association of the heat shock proteins HSP70 and HSP90 ... Chen S, Smith DF (1999). "Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery". J. Biol. Chem ... 2005). "The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor". Mol. Endocrinol. ... Hsp70 interacting protein)". Prapapanich V, Chen S, Toran EJ, et al. (1996). "Mutational analysis of the hsp70-interacting ...
Samborski P, Grzymisławski M (2015). "The Role of HSP70 Heat Shock Proteins in the Pathogenesis and Treatment of Inflammatory ... It exerts cytoprotection through regulating heat shock proteins and chemokines, and by stabilizing mast cells. It does so ... It has a potential to stimulate Hsp70 expression, with overexpression of Hsp70 being found to prevent the development of ... In experimental studies, overexpression of HSP70 was found to prevent the development of inflammatory process in the large ...
The protein encoded by this gene is a member of the Hsp70 family of heat shock proteins. Leung TK, Hall C, Rajendran M, Spurr ... Heat shock 70kDa protein 7 (HSP70B) also known as HSPA7 is a human gene. ... "The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1". Genomics. 12 (1): 74-9. doi: ... HSPA7+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH) v t e. ...
Heat shock 70kDa protein 12A also known as HSPA12A is a human gene. The protein encoded by this gene is a member of the Hsp70 ... family of heat shock proteins. Han Z, Truong QA, Park S, Breslow JL (February 2003). "Two Hsp70 family members expressed in ... HSPA12A+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH) v t e. ...
"An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins". Proceedings ... His group has developed systems in the areas of protein structure prediction, protein interactions and protein networks, ... U Göbel 1, C Sander, R Schneider, A Valencia<, Correlated mutations and residue contacts in proteins, Proteins 18(4):309-17. ( ... Krallinger, M; Leitner, F; Rodriguez-Penagos, C; Valencia, A (2008). "Overview of the protein-protein interaction annotation ...
... heat shock protein 70 (HSP-70)), and concomitantly downregulates pro-apoptotic factors. Lithium has been shown to reduce ... Oxidative stress can directly cause neuron cell death or it can trigger a cascade of events that leads to protein misfolding, ... Liu T, Bitan G (March 2012). "Modulating self-assembly of amyloidogenic proteins as a therapeutic approach for ... "G-protein-coupled receptor 30 mediates rapid neuroprotective effects of estrogen via depression of NR2B-containing NMDA ...
"The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression". ... "The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression". ... Heat shock 70 kDa protein 4 is a protein that in humans is encoded by the HSPA4 gene. The protein encoded by this gene was ... Agostini I, Popov S, Li J, Dubrovsky L, Hao T, Bukrinsky M (Sep 2000). "Heat-shock protein 70 can replace viral protein R of ...
The J domain of DnaJ interacts with Hsp70 heat shock proteins.[4] DnaJ heat-shock proteins play a role in regulating the ATPase ... In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein. It is ... activity of Hsp70 heat-shock proteins.[5][6] Besides stimulating the ATPase activity of DnaK through its J-domain, DnaJ also ... a diverse protein family that functions with hsp70 stress proteins". Molecular Biology of the Cell. 4 (6): 555-63. doi:10.1091/ ...
These proteins function in many cellular processes by regulating the ATPase activity of 70 kDa heat shock proteins (Hsp70). ... 2005). "The variable C-terminus of cysteine string proteins modulates exocytosis and protein-protein interactions". ... This protein has been proposed as a key element of the synaptic molecular machinery devoted to the rescue of synaptic proteins ... This protein makes up ~1% of the protein content of the synaptic vesicles. DNAJC5 appears to have a role in stimulated ...
This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 (Hsp70) family. As a ... "In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human ... This protein is a member of the Hsp70 family. In conjunction with other heat shock proteins, this protein stabilizes existing ... "The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression". ...
When under heat stress condition, the supporting cells could express heat shock protein 70 (HSP70) which is not up regulate in ... The mutations in connexin 26, which is an important gap junction protein found in the organ of Corti, would results in severe ... regeneration of hair cells by supporting cells in the vertebrates were proved by the expression of green fluorescent protein ( ...
... is triggered when high temperatures cause the dissociation of inactive HSF1 from complexes with heat shock proteins Hsp40/Hsp70 ... Other activated proteins interact with adaptor proteins that facilitate signaling protein interactions and coordination of ... most commonly protein phosphorylation catalyzed by protein kinases, which ultimately results in a cellular response. Proteins ... Shamovsky I, Ivannikov M, Kandel ES, Gershon D, Nudler E (March 2006). "RNA-mediated response to heat shock in mammalian cells ...
... heat shock proteins (hsp70, hsp90) and immunophilins. Upon activation, due to hormone binding to ligand binding pocket, the ... Smith DF, Stensgard BA, Welch WJ, Toft DO (Jan 1992). "Assembly of progesterone receptor with heat shock proteins and receptor ... Oñate SA, Estes PA, Welch WJ, Nordeen SK, Edwards DP (Dec 1991). "Evidence that heat shock protein-70 associated with ... of mammalian progesterone receptors occurs in the absence of DNA and is related to the release of the 90-kDa heat shock protein ...
Other important surface exposed DAMPs are heat-shock proteins (HSPs), namely HSP70 and HSP90, which under stress condition also ... Spisek R, Dhodapkar MV (August 2007). "Towards a better way to die with chemotherapy: role of heat shock protein exposure on ... These proteins contain oligomerization NACHT domains, CARD domains and some also contain similar pyrin (PYR) domains. Caspase 1 ... Peptidylprolyl isomerase F (CYPD) is the only known required protein for MPT-driven necrosis. The loss of IMM impermeability is ...
As a member of the heat shock protein 70 (Hsp70) family and a chaperone protein, it facilitates the proper folding of newly ... Along with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of ... "Entrez Gene: HSPA1L heat shock 70kDa protein 1-like". Mayer MP, Bukau B (Mar 2005). "Hsp70 chaperones: cellular functions and ... Heat shock 70 kDa protein 1L is a protein that in humans is encoded by the HSPA1L gene on chromosome 6. ...
The eukaryotic Hsp70, which is the heat shock protein of 70 kDa, typically localized in the cytoplasm is also found in the IMS ... The resulting hypothesis states that co-localization of Hsp70 is important for efficient translocation of protein precursors ... Channel proteins called porins in the outer membrane allow free diffusion of ions and small proteins about 5000 daltons or less ... The IMS is involved in the mitochondrial protein translocation. The precursor proteins called small TIM chaperones which are ...
In plants, 14-3-3 proteins only bind to chloroplast preproteins. It is also bound by the heat shock protein Hsp70 that keeps ... The heat shock protein and the 14-3-3 proteins together form a cytosolic guidance complex that makes it easier for the ... a chloroplast preprotein can still attach to a heat shock protein or Toc159. These complexes can bind to the TOC complex on the ... the protein import tunnel Toc75, plus the proteins Toc64 and Toc12. The first three proteins form a core complex that consists ...
... but rather relies on the help of two heat shock proteins (HSP90 and HSP70). HRI is mainly found in the precursors of red blood ... HRI activation can also occur due to other stressors such as heat shock, osmotic stress and proteasome inhibition. Activation ... Stress signals can cause protein kinases, known as EIF-2 kinases, to phosphorylate the α subunit of a protein complex called ... This complex is negatively regulated by two proteins: growth arrest and DNA damage‐inducible protein (GADD34), also known as ...
This gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 (Hsp70) family. As a Hsp70 protein ... Heat shock 70 kDa protein 8 also known as heat shock cognate 71 kDa protein or Hsc70 or Hsp73 is a heat shock protein that in ... proteins. The heat shock 70 kDa protein 8 also known as Hsc70 belongs to the heat-shock cognate subgroup. This protein binds to ... Hsc70 forms a chaperone complex by interacting with the heat shock protein of 40 kDa (Hsp40), the heat shock protein of 90 kDa ...
The heat shock protein and the 14-3-3 proteins together form a cytosolic guidance complex that makes it easier for the ... 14-3-3 proteins only bind to chloroplast preproteins.[43] It is also bound by the heat shock protein Hsp70 that keeps the ... a chloroplast preprotein can still attach to a heat shock protein or Toc159. These complexes can bind to the TOC complex on the ... Protein targeting and importEdit. See also: Protein targeting. The movement of so many chloroplast genes to the nucleus means ...
... and gram-positive bacteria also share conserved indels in a number of important proteins, such as Hsp70 and glutamine ... Extremophile archaea, particularly those resistant either to heat or to extremes of acidity and alkalinity, are a source of ... including thick-walled structures that are resistant to osmotic shock and allow the archaea to survive in water at low salt ... Proteins related to the cytoskeleton components of other organisms exist in archaea,[89] and filaments form within their cells, ...
... heat shock, or oxidative damage - heat shock proteins that identify misfolded or unfolded proteins and target them for ... The CHIP protein (carboxyl terminus of Hsp70-interacting protein) is itself regulated via inhibition of interactions between ... "Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties". Cell Cycle. 5 (22): 2592-601. doi:10.4161/ ... This complex of heat shock proteins is thought to resemble the ancestor of the modern proteasome. ...
These include the heat shock proteins (Hsp70s) and fatty acid binding proteins for anandamide (FABPs).[6][7] FABPs such as ... "Molecular identification of albumin and Hsp70 as cytosolic anandamide-binding proteins". Chemistry & Biology. 16 (6): 624-632. ... As reviewed in 2016; "Many of the AMT (EMT) proposals have fallen by the wayside." [18] To date a transmembrane protein ... The endocannabinoid transporters (eCBTs) are transport proteins for the endocannabinoids. Most neurotransmitters are water- ...
"Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate". The Journal of ... Hsp70 and Hsp10". Novartis Foundation Symposium. Novartis Foundation Symposia. 291: 59-68; discussion 69-73, 137-40. doi: ... protein binding. • heme binding. • electron carrier activity. Cellular component. • cytosol. • protein phosphatase type 2A ... Soltys BJ, Gupta RS (2000). "Mitochondrial proteins at unexpected cellular locations: export of proteins from mitochondria from ...
protein folding. Heat shock proteins/. Chaperonins. *Hsp10/GroES. *Hsp27. *Hsp47. *HSP60/GroEL ... to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ... The E3 molecule is responsible for binding the target protein substrate and transferring the ubiquitin from the E2 cysteine to ... Risseeuw EP, Daskalchuk TE, Banks TW, Liu E, Cotelesage J, Hellmann H, Estelle M, Somers DE, Crosby WL (2003). "Protein ...
The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. ... "Heat Shock Response" and the proteins were termed the "Heat Shock Proteins" (Hsps). ... Heat shock protein 70 (Hsp70) internal ribosome entry site (IRES). References[edit]. *^ Flaherty KM, DeLuca-Flaherty C, McKay ... HSP70+Heat-Shock+Proteins at the US National Library of Medicine Medical Subject Headings (MeSH) ...
"Heat shock protein derivatives for delivery of antigens to antigen presenting cells". International Journal of Pharmaceutics. ... For example, since Hsp70 plays an important role in the presentation of antigens of destroyed cells including cancer cells,[12] ... "Prophylactic Admission of an In Vitro Reconstructed Complexes of Human Recombinant Heat Shock Proteins and Melanoma Antigenic ... One approach to cancer vaccination is to separate proteins from cancer cells and immunize patients against those proteins as ...
protein folding. Heat shock proteins/. Chaperonins. *Hsp10/GroES. *Hsp27. *Hsp47. *HSP60/GroEL ... protein K48-linked ubiquitination. • protein K11-linked ubiquitination. • regulation of growth. • protein ubiquitination. ... ubiquitin-protein transferase activity. • transferase activity. • protein binding. Cellular component. • cell nucleus. • ... 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. ...
protein folding. Heat shock proteins/. Chaperonins. *Hsp10/GroES. *Hsp27. *Hsp47. *HSP60/GroEL ... protein complex. • extracellular exosome. Biological process. • ubiquitin-dependent protein catabolic process. • protein ... protein autoubiquitination. • protein ubiquitination. • MyD88-independent toll-like receptor signaling pathway. Sources:Amigo ... ubiquitin-protein transferase activity. • protein binding. • ATP binding. • ubiquitin conjugating enzyme activity. ...
Gupta RS, Singh B. Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic ... Evolution of HSP70 gene and its implications regarding relationships between archaebacteria, eubacteria, and eukaryotes. J Mol ... Stechmann A, Cavalier-Smith T. Phylogenetic analysis of eukaryotes using heat-shock protein Hsp90. J Mol Evol. 2003 ... Germot a, Philippe H. Critical analysis of eukaryotic phylogeny: a case study based on the HSP70 family. J Eukaryot Microbiol. ...
Gupta RS, Aitken K, Falah M, Singh B (April 1994). "Cloning of Giardia lamblia heat shock protein HSP70 homologs: implications ... However, when cells are heated, the fraction of heat shock proteins increases to 4-6% of cellular proteins. Heat shock protein ... heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat ... Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species. As their name ...
protein folding. Heat shock proteins/. Chaperonins. *Hsp10/GroES. *Hsp27. *Hsp47. *HSP60/GroEL ... protein binding. • enzyme binding. • metal ion binding. • identical protein binding. • ubiquitin protein ligase binding. • p53 ... protein ubiquitination. • negative regulation of protein processing. • establishment of protein localization. • response to ... protein deubiquitination. • protein sumoylation. • transcription factor catabolic process. • protein autoubiquitination. • ...
Heat-shock proteins are named according to their molecular weight. For example, Hsp60, Hsp70 and Hsp90 (the most widely studied ... Heat-shock proteins as DAMPs[edit]. Extracellular heat-shock proteins can be sensed by our immunity as danger associated ... How heat-shock proteins get into extracellular space[edit]. Heat-shock proteins can be secreted from immune cells or tumour ... Wikimedia Commons has media related to Heat-shock proteins.. *Heat-Shock+Proteins at the US National Library of Medicine ...
Deshaies discovered a role for 70 kilodalton heat shock proteins (Hsp70s) in enabling the post-translational insertion of ... and biochemically-validated function to be discovered for a member of the Hsp70 family of proteins. ... to tether cellular proteins to a ubiquitin ligase, resulting in ubiquitination and degradation of the tethered protein.[23] ... Effects on protein synthesis. Plant Physiol. 74, 956-961 *^ Stirling, C.J., Rothblatt, J., Hosobuchi, M., Deshaies, R., and ...
"Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate". J. Biol. Chem. 271 ... Hsp70 and Hsp10". Novartis Found. Symp. 291: 59-68; discussion 69-73, 137-40. PMID 18575266.. ... Soltys BJ, Gupta RS (2000). "Mitochondrial proteins at unexpected cellular locations: export of proteins from mitochondria from ... Neupert W (1997). "Protein import into mitochondria". Annu. Rev. Biochem. 66: 863-917. PMID 9242927. doi:10.1146/annurev. ...
protein dimerization activity. • transcription factor activity, sequence-specific DNA binding. • protein complex binding. • ... "Cell cycle-dependent switch of up-and down-regulation of human hsp70 gene expression by interaction between c-Myc and CBF/NF-Y ... 3.4) Heat shock factors. *HSF *1. *2. *4. (3.5) Tryptophan clusters. *ELF *2 ... protein complex. • nucleolus. • nucleus. • nuclear chromatin. Biological process. • Notch signaling pathway. • chromatin ...
DnaJ heat shock protein family (Hsp40) member C19. External IDs. OMIM: 608977 MGI: 3709029 HomoloGene: 87176 GeneCards: DNAJC19 ... which has been involved in Hsp40/Hsp70 chaperone systems.[6][7] As a mitochondrial chaperone, TIM14 functions as part of the ... protein transport. • protein folding. • visual perception. • genitalia development. • protein targeting to mitochondrion. • ... protein binding. • ATPase activator activity. • protein transporter activity. Cellular component. • integral component of ...
Archaea and gram-positive bacteria also share conserved indels in a number of important proteins, such as Hsp70 and glutamine ... Extremophile archaea, particularly those resistant either to heat or to extremes of acidity and alkalinity, are a source of ... including thick-walled structures that are resistant to osmotic shock and allow the archaea to survive in water at low salt ... Proteins related to the cytoskeleton components of other organisms exist in archaea,[86] and filaments form within their cells, ...
... the heat shock protein 70 (hsp70) and the protein FKBP4 (FK506-binding protein 4). The endogenous glucocorticoid hormone ... resides in the cytosol complexed with a variety of proteins including heat shock protein 90 (hsp90), ... resulting in release of the heat shock proteins. The resulting activated form GR has two principal mechanisms of action, ... "Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR ...
Heat of fusion - Heat of vaporization - heat shock protein - Hsp70 (70 kDa heat shock proteins) - Hsp90 (90 kDa heat shock ... protein - protein biosynthesis - Protein Data Bank - protein design - protein expression - protein folding - protein isoform - ... protein P16 - protein P34cdc2 - protein precursor - protein structure prediction - protein subunit - protein synthesis - ... proto-oncogene protein C-kit - proto-oncogene proteins c-abl - proto-oncogene proteins c-bcl-2 - Proto-oncogene proteins c-fos ...
The polypeptide unfolds and is then allowed to refold either by itself or with the help of heat shock proteins. Misfolded ... Hsp70 interacts with the protein aggregates and recruits Hsp100. Hsp70 stabilizes an activated Hsp100. Hsp100 proteins have ... In mammalian cells, the E3 ligase, carboxy-terminal Hsp70 interacting protein (CHIP), targets Hsp70-bound proteins. In yeast, ... Protein aggregation is a biological phenomenon in which intrinsically disordered proteins or mis-folded proteins aggregate (i.e ...
Endocannabinoid transporters for anandamide and 2-arachidonoylglycerol include the heat shock proteins (Hsp70s) and fatty acid ... "Molecular identification of albumin and Hsp70 as cytosolic anandamide-binding proteins". Chemistry & Biology. 16 (6): 624-632. ... binding proteins (FABPs). It is found that anandamide prefer cholesterol and ceramide more than other membrane lipids, and ...
Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSC70 Heat-Shock ProteinsHSP110 Heat-Shock ProteinsHSP72 Heat-Shock Proteins ... Heat Shock 70 kDa Protein. All MeSH CategoriesChemicals and Drugs CategoryAmino Acids, Peptides, and ProteinsProteinsMolecular ... HSP70 Heat-Shock Proteins. A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic ... HSP70 Heat Shock Proteins. *Heat-Shock Proteins, HSP70. *Heat-Shock Protein 70 ...
Heat shock protein hsp70 overexpression confers resistance against nitric oxide.. Bellmann K1, Jäättelä M, Wissing D, Burkart V ... We report here for the first time that protection against nitric oxide is mediated by the major heat shock protein, hsp70, even ... Constitutive expression of hsp70 caused protection from NO-induced cell lysis which was of the same extent as seen after heat ... Heat stress is known to render rat islet cells resistant against the toxic effects of nitric oxide, reactive oxygen ...
Heat shock protein family A (Hsp70) member 12B is a protein that in humans is encoded by the HSPA12B gene. The protein encoded ... "Entrez Gene: Heat shock protein family A (Hsp70) member 12B". Retrieved 2018-07-16. Harris SE, Fox H, Wright AF, Hayward C, ... by this gene contains an atypical heat shock protein 70 (Hsp70) ATPase domain and is therefore a distant member of the ... and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration". J. Proteome Res. 11 (4): 2533 ...
The heat shock protein 70 (Hsp70) internal ribosome entry site (IRES) is an RNA element that allows cap independent translation ... Page for Heat shock protein 70 (Hsp70) internal ribosome entry site (IRES) at Rfam v t e. ... during conditions such as heat shock and stress. It has been shown that the 216 nucleotide long 5 UTR contains internal ... untranslated region of human hsp70 mRNA". The Journal of Biological Chemistry. 278 (25): 22350-22356. doi:10.1074/jbc. ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex ... Synonyms : HSP70-2 Previous Names: "heat shock 70kD protein 1B", "heat shock 70kDa protein 1B" ... White boxes represent UTRs (untranslated regions). Orange: protein coding regions. The black lines connecting boxes represent ...
... cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and ... C. G. Evans, L. Chang, and J. E. Gestwicki, "Heat shock protein 70 (Hsp70) as an emerging drug target," Journal of Medicinal ... Investigating the Chaperone Properties of a Novel Heat Shock Protein, Hsp70.c, from Trypanosoma brucei. Adélle Burger, Michael ... M. Daugaard, M. Rohde, and M. Jäättelä, "The heat shock protein 70 family: highly homologous proteins with overlapping and ...
... heat shock protein acts as central integrators of protein homeostasis in cell. The form of these functions is to help setting ... seconds with primary antibody anti-Hsp40 or Hsp70 protein and then added with second antibody HRP anti-Hsp40 or Hsp70 protein, ... Method: We examined protein levels in all samples using Dotblott with monoclonal antibody anti-Hsp40 and anti-Hsp70. Levels of ... OSCC patients have increased Hsp70 levels, so it is possible that something is going wrong in protein folding. Errors in ...
Hsp70,. 70-kDa heat shock protein;. TNF,. tumor necrosis factor;. asHsp70,. antisense Hsp70 cDNA;. Hsc70,. heat shock cognate ... Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases ... Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases ... Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases ...
View protein in InterPro. IPR018181 Heat_shock_70_CS. IPR029048 HSP70_C_sf. IPR029047 HSP70_peptide-bd_sf. IPR013126 Hsp_70_fam ... View protein in InterPro. IPR018181 Heat_shock_70_CS. IPR029048 HSP70_C_sf. IPR029047 HSP70_peptide-bd_sf. IPR013126 Hsp_70_fam ... Heat shock protein family A (Hsp70) member 4 likeImported. ,p>Information which has been imported from another database using ... tr,G3SLN5,G3SLN5_LOXAF Heat shock protein family A (Hsp70) member 4 like OS=Loxodonta africana OX=9785 GN=HSPA4L PE=3 SV=1 ...
... assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress ... Hsp70s are key components that facilitate folding of de novo synthesized proteins, ... View protein in InterPro. IPR018181 Heat_shock_70_CS. IPR029048 HSP70_C_sf. IPR029047 HSP70_peptide-bd_sf. IPR013126 Hsp_70_fam ... View protein in InterPro. IPR018181 Heat_shock_70_CS. IPR029048 HSP70_C_sf. IPR029047 HSP70_peptide-bd_sf. IPR013126 Hsp_70_fam ...
Hsp70-2) ATPase domain in complex with ADP and inorganic phosphate ... Crystal structure of the human 70kDa heat shock protein 2 ( ... Heat shock-related 70 kDa protein 2. A. 404. Homo sapiens. ... Crystal structure of the human 70kDa heat shock protein 2 (Hsp70-2) ATPase domain in complex with ADP and inorganic phosphate. ... Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B, and ...
Heat shock proteins (Hsp) impart an age-old defense mechanism for all forms of life on earth. Misfolded proteins... ... Intracellular protein homeostasis is largely controlled by Heat shock proteins (Hsp). ... Intracellular protein homeostasis is largely controlled by Heat shock proteins (Hsp). Heat shock proteins (Hsp) impart an age- ... 2012). Tonicity enhancer binding protein (TonEBP) and hypoxia-inducible factor (HIF) coordinate heat shock protein 70 (Hsp70) ...
Diagnostic yield of heat shock protein 70 (HSP-70) and anti-HSP-70 in Behcet-induced uveitis. Download Prime PubMed App to ... Diagnostic Yield of Heat Shock Protein 70 (HSP-70) and anti-HSP-70 in Behcet-induced Uveitis. Scand J Immunol. 2013;77(6):476- ... Diagnostic yield of heat shock protein 70 (HSP-70) and anti-HSP-70 in Behcet-induced uveitis. Scand J Immunol. 2013;77(6):476- ... Diagnostic yield of heat shock protein 70 (HSP-70) and anti-HSP-70 in Behcet-induced uveitis.. Scand J Immunol. 2013 Jun; 77(6 ...
HSP70), peptide-binding domain superfamily including the families contained in it. Additional information provided includes ... The SCOP classification for the Heat shock protein 70kD ( ... Heat shock protein 70kD (HSP70), peptide-binding domain [. ... Browse and view proteins in genomes which have different domain combinations including a Heat shock protein 70kD (HSP70), ... protein binding. 0.003724. 0.7276. --. INHERITED FROM: protease binding ,, heat shock protein binding ,, unfolded protein ...
Exposure of cells to a heat shock temperature of 42 degrees C results in transient activation of HSF; its DNA-b … ... Transcriptional regulation of the human hsp70 gene in response to heat shock and other forms of physiological stress occurs ... through the activation of heat shock transcription factor (HSF). ... The human heat shock protein hsp70 interacts with HSF, the ... human hsp70 gene in response to heat shock and other forms of physiological stress occurs through the activation of heat shock ...
Using western blot analysis of levels of heat-shock protein 70 (Hsp70), we … ... Using western blot analysis of levels of heat-shock protein 70 (Hsp70), we examined the heat-shock responses of four Lottia ... Heat-shock protein 70 (Hsp70) expression in four limpets of the genus Lottia: interspecific variation in constitutive and ... constitutive levels of Hsp70 in their cells as a mechanism for protection against periods of extreme and unpredictable heat ...
In this study, we identified members of two major heat shock proteins (HSPs) families, Hsp70 and Hsp90, in Symbiodinium sp. ( ... Reduced expression of the Hsp90 gene under heat stress can indicate a reduced role in inhibiting the heat shock transcription ... resulted in an increase in algal Hsp70 gene expression from 39% to 57%, while extreme heat stress (+9°C) reduced Hsp70 ... Elevated temperatures decreased an Hsp90 expression under both rapid and gradual heat stress scenarios. Comparable Hsp70 and ...
1988a). Evidence for protection by heat-shock proteins against photoinhibition during heat-shock. EMBO J. 7, 1-6. ... 1993). The protective effect of heat shock proteins against photoinhibition under heat shock in barley (Hordeum vulgare). J. ... Members of the heat shock protein 70 (HSP70) family, also known as stress 70 molecular chaperones, have been found in almost ... A Chloroplast-Targeted Heat Shock Protein 70 (HSP70) Contributes to the Photoprotection and Repair of Photosystem II during and ...
HSP70), peptide-binding domain in Thelohanellus kitauei. Links to architectures containing these domain pairs in other groups ... Domain architectures containing both Actin-like ATPase domain and Heat shock protein 70kD ( ... Home > Genomes > Thelohanellus kitauei Actin-like ATPase domain and Heat shock protein 70kD (HSP70), peptide-binding domain ... Sequences with adjacent and non-adjacent Actin-like ATPase domain and Heat shock protein 70kD (HSP70), peptide-binding domain ...
Human Heat Shock Protein 70 (HSP70) ELISA Kit-NP_001006686.1 (MBS2020836) product datasheet at MyBioSource, ELISA Kits ... HSP70 elisa kit :: Human Heat Shock Protein 70 (HSP70) ELISA Kit. Catalog #. MBS2020836 (SPECIAL PROMOTION: Get FREE Starbucks ... HSP70).. No significant cross-reactivity or interference between Heat Shock Protein 70 (HSP70) and analogues was observed. ... The concentration of Heat Shock Protein 70 (HSP70) in the samples is then determined by comparing the O.D. of the samples to ...
70 kDa heat-shock protein than both the major stress-inducible HSP70 and constitutively expressed HSC70 heat-shock proteins, ... The human heat-shock protein family: expression of a novel heat-inducible HSP70 (HSP70B) and isolation of its cDNA and genomic ... The human heat-shock protein family: expression of a novel heat-inducible HSP70 (HSP70B) and isolation of its cDNA and genomic ... The human heat-shock protein multigene family comprises several highly conserved proteins with structural and functional ...
... that induction of HSP70 and other heat shock proteins by heat shock protects astrocytes against subsequent lethal heat shock. ... that induction of HSP70 and other heat shock proteins by heat shock protects astrocytes against subsequent lethal heat shock. ... that induction of HSP70 and other heat shock proteins by heat shock protects astrocytes against subsequent lethal heat shock. ... that induction of HSP70 and other heat shock proteins by heat shock protects astrocytes against subsequent lethal heat shock. ...
These studies suggest that the amount of preexisting constitutive hsc70 protein may influence the level of induction of hsp70 ... Multiple isoforms of hsp70 were detected but tissue-specific differences were not apparent in various organs of the rabbit. ... However, species differences were observed as fewer hsp70 isoforms were noted in rat and mouse. In the control rabbit, higher ... Given this observation, caution is required in the employment of hsp70 induction as an index of cellular stress since ...
Human Heat Shock Protein 70 (GenBank Accession No. NM_005345), a.a. 2-641 with C-terminal His-tag, MW = 71 kDa, expressed in ,i ... Human Heat Shock Protein 70 (GenBank Accession No. NM_005345), a.a. 2-641 with C-terminal His-tag, MW = 71 kDa, expressed in E ... In cooperation with other chaperones, Hsp70 stabilizes preexistent proteins against aggregation and mediate the folding of ... chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. ...
Chicken HSP70(Heat Shock Protein 70) ELISA Kit. Chicken HSP70(Heat Shock Protein 70) ELISA Kit. To Order Contact us: ... Alias: DAAP-21F2.7, FLJ54328, HSP70-1B, HSP70-2, HSPA1A, heat shock 70kD protein 1B ... The Intra-assay Precision is determined when 3 samples with low, middle and high level of Gallus Heat Shock Protein 70 (HSP70) ... The Intra-assay Precision is determined when 3 samples with low, middle and high level of Gallus Heat Shock Protein 70 (HSP70) ...
... belongs to the heat shock protein 70 family. It was isolated as a putative Rictor interacting protein and interaction with ... 26-101 HSPA4 (Hsp70) belongs to the heat shock protein 70 family. It was isolated as a putative Rictor interacting protein and ... Hsp70) belongs to the heat shock protein 70 family. It was isolated as a putative Rictor interacting protein and interaction ... Product name : HSPA4 (Hsp70) belongs to the heat shock protein 70 family. It was isolated as a putative Rictor interacting ...
Heat Shock Protein 70) ELISA Kit OSCAR DIAGNOSTIC SERVICES PVT. LTD.is an India based Company in Delhi. ... Mouse HSP-70 (Heat Shock Protein 70) ELISA Kit » Mouse HSP-70 (Heat Shock Protein 70) ELISA Kit. Mouse HSP-70 (Heat Shock ... Mouse HSP-70 (Heat Shock Protein 70) ELISA Kit. Mouse HSP-70 (Heat Shock Protein 70) ELISA Kit. Mouse HSP-70 (Heat Shock ... Mouse HSP-70 (Heat Shock Protein 70) ELISA Kit. Mouse HSP-70 (Heat Shock Protein 70) ELISA Kit. Mouse HSP-70 (Heat Shock ...
Anti- HSP70/HSC70 ; Heat shock protein 70/Heat shock cognate protein 70, Affinity purified ... Goat Anti-Heat Shock Protein 70, Heat Shock Cognate Protein 70 Antibody ...
The Heat Shock Proteins (HSP) are expressed at stress situations, such as hypovolemia, also they are involved at the process of ... As Heat Shock Proteins (HSP) estão expressas em situações de estresse, tais como a hipovolemia, além de participarem da síntese ... Besides, there are a few information about HSP70 expression at the healing process. OBJECTIVES: To determine the HSP70 ... a expressão da HSP70. RESULTADOS: A expressão da HSP70 no intestino grosso diminuiu com a hipovolemia (p. ...
HSP70 Heat-Shock Proteins / physiology*. Mice. Proto-Oncogene Proteins c-mos / physiology*. ... 0/HSP70 Heat-Shock Proteins; EC 2.7.11.1/Proto-Oncogene Proteins c-mos ... the Hsp70 antibody immunoprecipitated Mos as the major protein. Of importance, the Mos protein present in anti-Hsp70 ... In the absence of ATP from cell extracts, protein kinase activity of Mos was lost within 6 h on ice even though the Mos protein ...
  • A. A. Arif, L. Gao, C. D. Davis, and D. S. Helm, "Antibody response to heat shock proteins and histopathology in mice infected with Trypanosoma cruzi and maintained at elevated temperature," Journal of Parasitology , vol. 85, no. 6, pp. 1089-1099, 1999. (hindawi.com)
  • We examined protein levels in all samples using Dotblott with monoclonal antibody anti-Hsp40 and anti-Hsp70. (scirp.org)
  • The ELISA analytical biochemical technique of the MBS2020836 kit is based on HSP70 antibody-HSP70 antigen interactions (immunosorbency) and an HRP colorimetric detection system to detect HSP70 antigen targets in samples. (mybiosource.com)
  • The microtiter plate provided in this kit has been pre-coated with an antibody specific to Heat Shock Protein 70 (HSP70). (mybiosource.com)
  • Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody specific to Heat Shock Protein 70 (HSP70). (mybiosource.com)
  • After TMB substrate solution is added, only those wells that contain Heat Shock Protein 70 (HSP70), biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. (mybiosource.com)
  • HSP70 protein was detected with the C92 monoclonal antibody (Welch and Suhan: J Cell Biol. (elsevier.com)
  • Anti-heat Shock 70 kDa Protein Antibody Induced Neuronal Cell Death. (semanticscholar.org)
  • Despite a low-abundance of Mos, the Hsp70 antibody immunoprecipitated Mos as the major protein. (biomedsearch.com)
  • For comparison analysis of surface proteins, we required an antibody control specific for an intracellular protein. (hindawi.com)
  • Identified proteins are heterologously expressed, purified, and used for antibody production. (hindawi.com)
  • Western Blot: HSP70/HSPA1A Antibody [NBP1-35969] - Analysis of 293T cell lysate. (novusbio.com)
  • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine," Cell , vol. 101, no. 2, pp. 199-210, 2000. (hindawi.com)
  • The aim of this study was to investigate pathogenic roles of a panel of cytosolic HSPs including HSP90, HSP70, HSP60 and HSP27 in GC. (waocp.org)
  • An indirect immunoperoxidase method was applied using polyclonal antibodies against HSP70 and HSP90 on formalin-fixed paraffin-embedded tissues. (uth.gr)
  • Seasonal variation in heat shock proteins Hsp70 and Hsp90 expression was studied in the leaves of two naturally growing Iris pumila populations, one inhabiting an open dune site, and the other the understorey of a Pinus silvestris stand. (ac.rs)
  • Heat shock protein 90 (HSP90) is an ATPase-dependent molecular chaperone ubiquitously expressed in eukaryotic cells. (plos.org)
  • HSP90 is essential for posttranslational conformational maturation and stability of client proteins including protein kinases and transcription factors, many of which are important for the proliferation and survival of cancer cells. (plos.org)
  • For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100. (springer.com)
  • [8] HOP (the H sp70/Hsp90 O rganizing P rotein) can bind to both Hsp70 and Hsp90 at the same time, and mediates the transfer of peptides from Hsp70 to Hsp90. (wikipedia.org)
  • The human hsp70 gene was stably transfected into the rat insulinoma cell line RINm5F. (nih.gov)
  • Heat shock protein family A (Hsp70) member 12B is a protein that in humans is encoded by the HSPA12B gene. (wikipedia.org)
  • The protein encoded by this gene contains an atypical heat shock protein 70 (Hsp70) ATPase domain and is therefore a distant member of the mammalian Hsp70 family. (wikipedia.org)
  • p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence. (uniprot.org)
  • Transcriptional regulation of the human hsp70 gene in response to heat shock and other forms of physiological stress occurs through the activation of heat shock transcription factor (HSF). (nih.gov)
  • We have isolated and characterized a novel human HSP70 cDNA, HSP70B' cDNA, and its corresponding gene sequence. (nus.edu.sg)
  • The complete HSP70B' gene was sequenced and, like the major inducible HSP70 gene, is devoid of introns. (nus.edu.sg)
  • The HSP70B' gene has 77% sequence similarity to the HSP70 gene and 70% similarity to HSC70 cDNA, with greatest sequence divergence towards the 3'-terminus. (nus.edu.sg)
  • We have cloned a human gene encoding the 70,000-dalton heat shock protein (HSP70) from a human genomic library, using the Drosophila HSP70 gene as a heterologous hybridization probe. (houstonmethodist.org)
  • From the analysis of S1 nuclease-resistant mRNA-DNA hybrids, the HSP70 gene appears to be transcribed as an uninterrupted mRNA of 2.3 kilobases. (houstonmethodist.org)
  • We show that the cloned HSP70 gene contains the sequences necessary for heat shock-induced expression by two criteria. (houstonmethodist.org)
  • First, hamster cells transfected with a subclone containing the HSP70 gene and flanking sequences synthesized a HSP70-like protein upon heat shock. (houstonmethodist.org)
  • Second, human cells transfected with a chimeric gene containing the 5' flanking sequences of the HSP70 gene and the coding sequences of the bacterial chloramphenicol acetyltransferase gene transcribed the chimeric gene upon heat shock. (houstonmethodist.org)
  • HSPA6 (Heat Shock Protein Family A (Hsp70) Member 6) is a Protein Coding gene. (genecards.org)
  • Gene Ontology (GO) annotations related to this gene include enzyme binding and heat shock protein binding . (genecards.org)
  • This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. (nih.gov)
  • The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. (nih.gov)
  • Background: The Y-box protein-1 (YB-1) fulfills pleiotropic functions relating to gene transcription, mRNA processing, and translation. (uth.gr)
  • We carried out a case-control study among 367 coke oven workers in northwest China, focused on three common HSP70 polymorphisms (HSP70-1 G190C, HSP70-2 A1267G and HSP70-hom T2437C), and evaluated the association of HSP70 gene polymorphisms with work sites for high risk of hypertension. (cdc.gov)
  • Context The role of heat shock protein (HSP) 70-2 gene polymorphism (at position 1267, A to G transition) in patients withpancreatic disorders is not clear. (imedpub.com)
  • Experiments with gene-targeted mice have shown that different BH3-only proteins are required for apoptosis initiation in response to distinct developmental cues and cytotoxic stimuli ( 6 ). (pnas.org)
  • When examining the chromosomes, Ritossa found a "puffing pattern" that indicated the elevated gene transcription of an unknown protein. (wikipedia.org)
  • The relative amount of HSP70 gene transcription was significantly higher in "High Se + F group" than the other groups. (fluoridealert.org)
  • CEA as a target antigen of tumor therapy has been extensively evaluated in murine models and human by means of vaccinating recombinant CEA proteins ( 15 ), recombinant viruses carrying the CEA gene ( 16 ), CEA anti-idiotype antibodies ( 17 ), dendritic cells transfected with CEA RNA ( 18 ), or dendritic cells pulsed with agonist epitopes of CEA ( 14 , 19 - 21 ). (aacrjournals.org)
  • these proteins are likely to represent global regulators of gene expression. (genetics.org)
  • PcG proteins form a family based upon their common role in gene expression rather than extensive shared homologies or structural motifs. (genetics.org)
  • We reported previously that a tilapia ( Oreochromis mossambicus ) heat shock protein 70 (HSP70) promoter is able to confer heat shock response on a reporter gene after transient expression both in cell culture and in microinjected zebrafish embryos. (biochemj.org)
  • Fulda M, Heinz E, Wolter F. The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family. (labome.org)
  • HSP70B' cDNA hybrid-selected an mRNA encoding a more basic 70 kDa heat-shock protein than both the major stress-inducible HSP70 and constitutively expressed HSC70 heat-shock proteins, which in common with other heat-shock 70 kDa proteins bound ATP. (nus.edu.sg)
  • In contrast with HSP70 mRNA, which is present at low concentrations in HeLa cells and readily induced by heat or CdCl2 treatment in both fibroblasts and HeLa cells, HSP70B' mRNA was induced only at higher temperature and showed no basal expression. (nus.edu.sg)
  • Brief exposure of cultured cortical astrocytes to acid (pH 5.2 for 40 min) or heat shock (45°C for 40 min) markedly induced hsp70 mRNA and HSP70 protein. (elsevier.com)
  • The 2.6-kilobase mRNA was shown to direct the translation in vitro of a 70,000-dalton protein similar in electrophoretic mobility to the HSP70 synthesized in vivo. (houstonmethodist.org)
  • We show that the HSP70 mRNA transcribed in an adenovirus 5 transformed human cell line (293 cells) is identical to the HSP70 mRNA induced by heat shock. (houstonmethodist.org)
  • Among its related pathways are mRNA Splicing - Major Pathway and Protein processing in endoplasmic reticulum . (genecards.org)
  • The effects of exposure to sublethal doses of CdCl2 (0.05, 0.1 and 0.2 LC50) during 14 days on mRNA-hsp70 expression in liver and gillwere investigated in juveniles of Persian sturgeon (Acipenser persicus). (jifro.ir)
  • The result showed that in both study tissues, gill and liver, the relative mRNA-hsp70 expression level significantly increased (p≤0.05) on all study days compared to control group. (jifro.ir)
  • Relative mRNA-hsp70 showed a clear time- dependent response in both tissues following the exposure to CdCl2. (jifro.ir)
  • A significant increase (p≤0.05) was observed on the second day and then decreased up to day 7 of the exposure and increase level of mRNA-hsp70 expression was observed on day 14. (jifro.ir)
  • Southern and Northern blot analysis, and partial nucleotide sequence analysis indicated that pGA 3 and pGE 4 were the HSP70 cDNA clones, and that pGB 1 and pGD 3 were the HSC70 cDNA clones, which selectively recognized HSP70 or HSC70 mRNA, respectively. (elsevier.com)
  • HSP70 mRNA is present in a very small amount in normal controls, and is greatly induced after the transient ischaemia. (elsevier.com)
  • In situ hybridization study demonstrated that the HSP70 mRNA was present in a very small amount in the hippocampal pyramidal and dentate granule cells in the sham control, and that the mRNA was greatly induced in the cells of hippocampus, dentate gyrus, medial habenula, ventral thalamic nuclei, caudate putamen, ventromedial and arcuate hypothalamic nuclei, amygdaloid nuclei and cerebral cortex after 8 h of reperfusion. (elsevier.com)
  • Our results indicate that HSP70 and HSC70 cDNA clones were first isolated from post-ischaemic gerbil brain, and selectively recognize HSP70 or HSC70 mRNA, respectively. (elsevier.com)
  • A regional difference in the induction of the HSP70 and HSC70 mRNA in post-ischaemic gerbil brain was observed by in situ hybridization. (elsevier.com)
  • RT-PCR of heat shock protein HsP70 mRNA evidenced cell stress. (archives-ouvertes.fr)
  • Electrotransfer-induced cellular stress was evidenced by increased HsP70 mRNA. (archives-ouvertes.fr)
  • 0.01) as well as an increase in HSP70 mRNA when compared with the hypoxia group. (medsci.org)
  • S. V. Slepenkov and S. N. Witt, "The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? (hindawi.com)
  • The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolizing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. (wikipedia.org)
  • The 70 kilodalton heat shock proteins ( Hsp70 s or DnaK ) are a family of conserved ubiquitously expressed heat shock proteins . (wikipedia.org)
  • This entry represents the Hsp70 family, and includes chaperone protein DnaK and luminal-binding proteins. (embl.de)
  • M. P. Mayer and B. Bukau, "Hsp70 Chaperones: Cellular Functions and Molecular Mechanism," Cellular and Molecular Life Sciences, Vol. 62, No. 6, 2005, pp. 670-684. (scirp.org)
  • Under normal conditions, Hsp70 proteins function as ATP-dependent molecular chaperones by assisting the folding of newly synthesized polypeptides, the assembly of multiprotein complexes, and the transport of proteins across cellular membranes ( 9 - 12 ). (pnas.org)
  • In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. (uniprot.org)
  • Here we present the current knowledge on the role of molecular chaperones in particular heat shock protein 70 (Hsp70) in human gastrointestinal cancers along with their therapeutic targeting. (springer.com)
  • In cooperation with other chaperones, Hsp70 stabilizes preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. (bpsbioscience.com)
  • These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. (bpsbioscience.com)
  • The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). (nih.gov)
  • Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. (nih.gov)
  • Right here we review the existing condition of Hsp70 like a medication target with a particular emphasis on the key challenges and possibilities enforced by its co-chaperones protein-protein relationships and allostery. (cancer-ecosystem.com)
  • In keeping with this variety of features deletion studies possess suggested that each J-protein co-chaperones play specific cellular roles. (cancer-ecosystem.com)
  • Based on our identification of c-Mos-Hsp70 interaction, one of the roles of ATP may be to assist the regulation of c-Mos via ATP involvement in the protein-folding function of Hsp70 and possibly other molecular chaperones. (biomedsearch.com)
  • Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. (springer.com)
  • This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. (springer.com)
  • The broad spectrum of cellular functions of Hsp70 proteins is achieved through (i) the amplification and diversification of hsp70 genes in evolution, which has generated specialized Hsp70 chaperones, (ii) co-chaperones which are selectively recruited by Hsp70 chaperones to fulfill specific cellular functions and (iii) cooperation of Hsp70s with other chaperone systems to broaden their activity spectrum. (springer.com)
  • Hsp70 proteins with their co-chaperones and cooperating chaperones thus constitute a complex network of folding machines. (springer.com)
  • A more complex folding situation exists for the Hsp70-dependent control of regulatory proteins since several steps in the folding and activation process of these substrates are assisted by multiple chaperones. (springer.com)
  • Hsp70 proteins together with their co-chaperones of the J-domain protein (JDP) family prevent the aggregation of non-native proteins through association with hydrophobic patches of substrate molecules, which shields them from intermolecular interactions ('holder' activity). (springer.com)
  • The mechanism by which Hsp70-chaperones assist the folding of non-native substrates is still unclear. (springer.com)
  • Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during synthesis and in times of cellular stress. (wikipedia.org)
  • The protein is then free to fold on its own, or to be transferred to other chaperones for further processing. (wikipedia.org)
  • Most heat shock proteins (Hsp) function as molecular chaperones that help organisms to cope with stress of both an internal and external nature. (wiley.com)
  • Heat shock genes are a subset of a larger group of genes coding for molecular chaperones, i.e. proteins that are involved in 'house-keeping' functions in the cell. (wiley.com)
  • Apart from this function, molecular chaperones are involved in transport, folding, unfolding, assembly and disassembly of multi-structured units and degradation of misfolded or aggregated proteins ( Fig. 1 ). (wiley.com)
  • The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. (novusbio.com)
  • also called chaperones) are intimately involved in intracellular protein folding. (powershow.com)
  • Heat shock proteins, Hsp70 chaperones help to fold many proteins. (embl.de)
  • Consistent with a coupling between translocation across the SecYEG translocon and folding by periplasmic chaperones, a lack of PpiD retards the release of a translocating outer membrane protein into the periplasm. (labome.org)
  • This pretreatment has been shown to induce the expression of several nuclear heat shock protein 70 ( HSP70 ) genes, including HSP70B , encoding a chloroplast-localized chaperone. (plantcell.org)
  • In addition, NSY50 adjusted the transcription levels of genes related to those proteins. (frontiersin.org)
  • Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). (novusbio.com)
  • In most eukaryotes hsp70 genes exist as part of a multigene family. (novusbio.com)
  • This system employed the Su(Hw) DNA-binding domain (ZnF) to direct PcG proteins to transposons that carried the white and yellow reporter genes. (genetics.org)
  • Heat shock proteins (HSPs) are intracellular proteins with pro- and anti-inflammatory actions, playing an important role in the pathogenesis of Behcet's disease (BD). (unboundmedicine.com)
  • Because heat shock proteins (Hsps) are typically found in the cytosol, ER, and mitochondria of a cell [ 4 ], we chose to examine the Hsp70-related proteins from E. cuniculi as potential candidates. (hindawi.com)
  • Recently, heat shock proteins (HSPs) were found to be overexpressed in a wide range of malignancies have been considered as promising candidate biomarkers for GC. (waocp.org)
  • Induction of heat shock proteins (hsps) is considered as an important protective, ecophysiologically adaptive, and genetically conserved response to environmental stress in all organisms. (jifro.ir)
  • [4] [5] This was later described as the "Heat Shock Response" and the proteins were termed the "Heat Shock Proteins" (Hsps). (wikipedia.org)
  • It is known that up-regulation of the Hsps is a common cellular response to increased levels of non-native proteins that facilitates correct protein folding/refolding or degradation of non-functional proteins. (wiley.com)
  • In this review, we will focus on the ecological and evolutionary roles of stress-inducible heat shock proteins (Hsps), especially on Hsp70, one of the major heat shock proteins that has been intensively studied in model organisms and in naturally occurring populations. (wiley.com)
  • Indirect experimental evidence suggests that the major stress-inducible Hsp70 (also known as Hsp72 or Hsp70i) may be such a cancer-relevant antiapoptotic protein ( 2 ). (pnas.org)
  • Hsp70 is abundantly expressed in malignant human tumors of various origins, whereas in normal cells, its expression is mainly stress inducible. (pnas.org)
  • Under various stress conditions, the accumulation of the inducible Hsp70 enhances the ability of stressed cells to cope with increased concentrations of unfolded/denatured proteins ( 13 , 14 ). (pnas.org)
  • The ability to resolve protein members of the hsp70 multigene family by two-dimensional Western blotting permitted the characterization of antibodies which were specific in discriminating constitutively expressed hsc70 isoforms from stress-inducible hsp70 isoforms. (semanticscholar.org)
  • Finally, HSP70 inducible protein was significantly increased in chorionic villi of first trimester missed miscarriages concerning syncytiotrophoblasts, cytotrophoblasts, vessel and stroma cells compared to full-term placentas. (uth.gr)
  • Here, we review the recent evidence of the relationship between stress resistance and inducible Hsp expression, including a characterization of factors that induce the heat shock response and a discussion of the associated costs. (wiley.com)
  • Transgenic mice expressing the human inducible Hsp70 have hippocampal neurons resistant to ischemic injury. (ac.be)
  • Reference : Transgenic mice expressing the human inducible Hsp70 have hippocampal neurons resista. (ac.be)
  • en] Using transgenic mice constitutively expressing the human inducible Hsp70, we examined the role of Hsp70 on cell survival after focal cerebral ischemia. (ac.be)
  • This element specifically binds an inducible transcription factor, most probably heat shock factor, and a constitutive factor. (biochemj.org)
  • The main role of this domain is to stimulate the intrinsically slow ATPase activity of Hsp70 [25 26 and the key region required for this process is an invariant histidine-proline-aspartic acid (HPD) motif which resides in a loop between helix 2 and 3 of the J-domain [27-29]. (cancer-ecosystem.com)
  • [4] DnaJ heat-shock proteins play a role in regulating the ATPase activity of Hsp70 heat-shock proteins. (wikipedia.org)
  • However, the presence of a peptide in the binding domain stimulates the ATPase activity of Hsp70, increasing its normally slow rate of ATP hydrolysis. (wikipedia.org)
  • These cochaperones dramatically increase the ATPase activity of Hsp70 in the presence of interacting peptides. (wikipedia.org)
  • All cells constitutively express a 70-kDa heat shock cognate protein (Hsc70, also known as Hsp73), which is highly homologous to Hsp70 ( 7 , 8 ). (pnas.org)
  • Expression of HSP70 cognate protein was significantly increased in chorionic villi of first trimester missed miscarriages, concerning syncytiotrophoblastic cells only, compared to full-term placentas. (uth.gr)
  • Structure of the ATPase fragment of a 70K heat-shock cognate protein. (wikipedia.org)
  • Addition of ATP and other hydrolyzable nucleotides results in the dissociation of hsp70 from HSF while nonhydrolyzable nucleotide analogs do not disrupt the complex. (nih.gov)
  • Collectively these structural and biochemical research have started to reveal the powerful adjustments in Hsp70 that accompany nucleotide hydrolysis and substrate binding [21]. (cancer-ecosystem.com)
  • Once the entire protein is synthesized, a nucleotide exchange factor (prokaryotic GrpE , eukaryotic BAG1 and HspBP1 are among those which have been identified) stimulates the release of ADP and binding of fresh ATP, opening the binding pocket. (wikipedia.org)
  • The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). (novusbio.com)
  • Errors in protein folding result in a new homeostasis or inhibition of apoptosis and increasing cell proliferation that triggers carcinogenesis. (scirp.org)
  • Neutralization of Hsp70 may open new possibilities for treatment of cancers that have acquired resistance to therapies activating the classical apoptosis pathway. (pnas.org)
  • Intensive apoptosis research during the last decade has resulted in the identification of several other proteins, which may similarly promote tumorigenesis by suppressing apoptosis ( 2 , 4 ). (pnas.org)
  • Moreover, Hsp70 effectively inhibits apoptosis induced by a wide range of stimuli ( 13 , 15 - 19 ). (pnas.org)
  • Interestingly, Hsp70 rescues cells from apoptosis induced by, e.g., tumor necrosis factor (TNF), without inhibiting the activation of effector caspases ( 19 ). (pnas.org)
  • These data suggest that Hsp70 functions either later in the apoptosis signaling cascade than any known survival-enhancing protein/drug or that Hsp70 suppresses another as yet unknown caspase-independent death pathway ( 19 ). (pnas.org)
  • In addition to its preferential expression in tumors and its ability to inhibit apoptosis, the role of Hsp70 in tumorigenesis is supported by data showing that its expression enhances the tumorigenic potential of rodent cells in vivo ( 20 - 22 ). (pnas.org)
  • Earlier results of a preliminary nature have suggested that the inhibition of Hsp70 synthesis in tumor cells may either sensitize them to chemotherapy or commit them to apoptosis ( 19 , 27 , 28 ). (pnas.org)
  • 2007). Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma. (springer.com)
  • 2016). The cytomegalovirus protein UL138 induces apoptosis of gastric cancer cells by binding to heat shock protein 70. (springer.com)
  • 70 AbstractObjective: To observe the effect of preventively used moxibustion on the expression of apoptosis-related factors in rats with acute gastric mucosal damage (GMD), and analyze the relationship between those factors and heat shock protein 70 (HSP70), for discovering the mechanism of moxibustion for protecting gastric mucosa from the aspect of mitochondria signal transduction of apoptosis. (scribd.com)
  • The GMD models were induced in groups except for A group, and the expression of cytochrome c (Cyt-c) in gastric mucosa was measured by Western-blot analysis, the expression of HSP70, cell apoptosis index (AI), apoptotic protease activating factor 1 (Apaf-1), Caspase-9, Caspase-3, Bcl-2 and Bax in gastric mucosal cells were studied by immunohistochemical detection. (scribd.com)
  • Conclusion: Moxibustion inhibits the apoptosis of rats gastric mucosal cells and protect them from damage, through up-regulating the expression of HSP70, and modulating the expressions of Cyt-c, Apaf-1, Caspase-9, Caspase-3, Bcl-2 and Bax which were related to the mitochondria signal transduction of apoptosis. (scribd.com)
  • Rats CLC NumberR2-03 Document CodeA Our previous studies have proved that preventively used moxibustion could induce high expression of HSP70 in gastric mucosa in rats with stress gastric ulcer, to inhibit cell apoptosis and protect gastric mucosa [1, 2]. (scribd.com)
  • Our present study aimed to observe the effect of moxibustion on the expression of Cyt-c, Apaf-1, and the apoptosisrelated factors in the gastric mucosal cells in rats with acute gastric mucosal damage (GMD), and to discover the relationship between the aforementioned factors with HSP70, for revealing the mechanism of moxibustion for inhibiting cell apoptosis and protecting gastric mucosa from the aspect of mitochondria signal transduction of apoptosis. (scribd.com)
  • Increased levels of heat shock proteins 70 (HSP70) in cancer cells are known to confer resistance to apoptosis. (bvsalud.org)
  • Since recent advances in the understanding of bacterial toxins have produced new strategies for the treatment of cancers, we investigated the effect of Pseudomonas aeruginosa exotoxin A (PEA) on HSP70 expression and induction of apoptosis in chemoresistant OSCC cell line (YD-9). (bvsalud.org)
  • On the other hand, PEA significantly decreased the viability of YD-9 cells by deteriorating the HSP70-relating protecting system through inhibition of HSP70 expression and inducing apoptosis in YD-9 cells. (bvsalud.org)
  • Therefore, these results indicate that PEA reduced the chemoresistance through inhibition of HSP70 expression and also induced apoptosis in chemoresistant YD-9 cells. (bvsalud.org)
  • To determine the mechanism of cell death, the levels of Bcl-cell lymphoma (Bcl)-2 proteins, Bcl-2-associated X (Bax) protein and anti-apoptosis heat-shock protein 70 were tested by applying reverse transcription polymerase chain reaction and Western blot. (dovepress.com)
  • The release of cytochrome c activated caspase-9, which consequently activated caspase-3/7 with the cleaved poly(ADP-ribose) polymerase protein, thereby resulting in apoptosis alteration. (dovepress.com)
  • Porcine reproductive and respiratory syndrome virus envelope (E) protein interacts with mitochondrial proteins and induces apoptosis. (sc.edu)
  • Constitutive expression of hsp70 caused protection from NO-induced cell lysis which was of the same extent as seen after heat stressing cells. (nih.gov)
  • L. Bhagat, V. P. Singh, R. K. Dawra, and A. K. Saluja, "Sodium arsenite induces heat shock protein 70 expression and protects against secretagogue-induced trypsinogen and NF- κ B activation," Journal of Cellular Physiology , vol. 215, no. 1, pp. 37-46, 2008. (hindawi.com)
  • A. Prayitno, E. Asnar, O. Astirin, D. Rosmala and S. Putra, "Heat Shock Protein 40 (Hsp40) and Hsp70 Protein Expression in Oral Squamous Cell Carcinoma (OSCC)," Journal of Cancer Therapy , Vol. 4 No. 3, 2013, pp. 734-741. (scirp.org)
  • These results show that tumorigenic breast cancer cells depend on the constitutive high expression of Hsp70 to suppress a transformation-associated death program. (pnas.org)
  • Furthermore, the expression of Hsp70 correlates with increased cell proliferation, poor differentiation, lymph node metastases, and poor therapeutic outcome in human breast cancer ( 23 - 26 ). (pnas.org)
  • For this purpose, we generated an adenoviral (Ad) vector carrying a fragment of human Hsp70 cDNA in antisense (as) orientation (Ad.asHsp70) capable of inhibiting the expression of Hsp70 without depleting the essential Hsc70. (pnas.org)
  • Inhibition of heat shock protein expression by Helicobacter pylori . (springer.com)
  • Our results suggest distinct strategies of Hsp70 expression in limpets occupying different heights and orientations in the rocky intertidal zone. (nih.gov)
  • Besides, there are a few information about HSP70 expression at the healing process. (usp.br)
  • OBJECTIVES: To determine the HSP70 expression at large bowel and intestinal anastomoses in normal and hypovolemic rats, as well as the amount of collagen and the quality of the inflammatory cells involved at this process, and correlate them. (usp.br)
  • The inflammatory cells were assessed by Hematoxilin-eosin, the amount of collagen was stained by red Picrossirius and the HSP70 expression was determined by immunohistochemical study. (usp.br)
  • The role of heat shock protein 70 (HSP70) expression has been investigated in various types of tumors. (ac.rs)
  • In this study we investigated expression of HSP70 in human colonic carcinoma and possible correlation with clinicopathology. (ac.rs)
  • To assess patterns (cytosolic and membrane) of HSP70 expression, the 48 surgically removed colorectal adenocarcinomas and 12 normal colonic and rectal mucosal samples were examined by immunohistochemistry and Western-blot. (ac.rs)
  • Densitometric analysis of blots of plasma membrane HSP70 expression has shown decrease in colorectal cancer cells compared to normal mucosa. (ac.rs)
  • Further research is necessary to clarify the mechanisms responsible for differential HSP70 expression as well as its definitive role in colorectal cancer. (ac.rs)
  • In future studies, the antibodies to the 'C1' Hsp70 will be used to delineate spore surface protein expression. (hindawi.com)
  • Immunohistochemistry was used to assess the level of expression of these proteins in archived tumor samples (N87) representing various pathological characteristics of GC. (waocp.org)
  • Our ndings indicate a role of HSP70 as a potential prognostic biomarker, patients harboring positive HSP70 expression displaying worse disease free survival than those with negative HSP70 expression. (waocp.org)
  • save Save Effect of moxibustion on expression of HSP70 and a. (scribd.com)
  • Cid C, Regidor I, Poveda PD, Alcazar A (2009) Expression of heat shock protein 90 at the cell surface in human neuroblastoma cells. (usp.br)
  • Conclusions: The results of the present study have sufficiently shown that there is an increase of HSP70 & 90 expression in chorionic villi of first trimester missed miscarriages compared to full-term placentas and this increase may have an important implication on the miscarriage process. (uth.gr)
  • Although in this study up expression of hsp70 was common to both the gill and the liver, it was significantly (p≤0.05) expressed more in the liver than the gill. (jifro.ir)
  • The aim of this study is to detect the expression of HSP70 in fluorosis patients and explore the role of Se in fluorosis protection. (fluoridealert.org)
  • Expression of HSP70 was evaluated by Western blotting and real-time PCR techniques. (fluoridealert.org)
  • The same results were found for expression of HSP70 protein to beta-actin ratio. (fluoridealert.org)
  • The gain of cytosolic DEDD enhances cyclin D1 expression by interacting with heat shock 71 kDa protein 8 (HSC70). (nature.com)
  • This suggests that constitutive expression of Hsp70 reduces the extent of damage following permanent middle cerebral artery occlusion. (ac.be)
  • In response to a 7°C temperature increase, expression of the transcripts encoding hsp70 and DnaJ-like protein increased as much as 18-fold and 3-fold, respectively, within a 8 h period. (int-res.com)
  • Tethered ZnF-PcG proteins repressed white and yellow expression at the majority of sites tested, with each fusion protein displaying a characteristic degree of silencing. (genetics.org)
  • Using transient expression experiments in carp EPC (epithelioma papulosum cyprini) cells and in microinjected zebrafish embryos, we show that a distal heat shock response element (HSE1) at approx. (biochemj.org)
  • The J domain of DnaJ interacts with Hsp70 heat shock proteins. (wikipedia.org)
  • The Hsp70 system interacts with extended peptide segments of proteins as well as partially folded proteins to prevent aggregation, remodel folding pathways, and regulate activity [7] When not interacting with a substrate peptide, Hsp70 is usually in an ATP bound state. (wikipedia.org)
  • As newly synthesized proteins emerge from the ribosomes , the substrate binding domain of Hsp70 recognizes sequences of hydrophobic amino acid residues, and interacts with them. (wikipedia.org)
  • Concurrently, DEDD interacts with Rb family proteins and promotes their proteasome-mediated degradation. (nature.com)
  • Antonoaea R, Fürst M, Nishiyama K, Muller M. The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon. (labome.org)
  • Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. (springer.com)
  • In freshly field-collected animals and in specimens acclimated at ambient temperature ( approximately 14 degrees C) for 14 days, the two high-intertidal species had higher constitutive levels of Hsp70 than the low- and mid-intertidal species. (nih.gov)
  • Our findings suggest that high-intertidal congeners of Lottia employ a "preparative defense" strategy involving maintenance of high constitutive levels of Hsp70 in their cells as a mechanism for protection against periods of extreme and unpredictable heat stress. (nih.gov)
  • The constitutive complex is not observed with the non-functional, proximal HSE3 sequence, suggesting that both factors are required for the heat shock response mediated by HSE1. (biochemj.org)
  • Intracellular protein homeostasis is largely controlled by Heat shock proteins (Hsp). (springer.com)
  • its DNA-binding activity increases rapidly, plateaus, and attenuates, during which the intracellular levels of hsp70 increase. (nih.gov)
  • Although initially α-synuclein was considered a purely intracellular protein, recent data suggest that it can be detected in the plasma and CSF of humans and in the culture media of neuronal cells. (jneurosci.org)
  • The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. (novusbio.com)
  • Heat shock protein 70 is an antiapoptotic chaperone protein highly expressed in human breast tumors and tumor cell lines. (pnas.org)
  • Despite the apoptotic morphology as judged by electron microscopy, the asHsp70-induced death was independent of known caspases and the p53 tumor suppressor protein. (pnas.org)
  • 2017). Downregulation of Sp1 by Minnelide leads to decrease in HSP70 and decrease in tumor burden of gastric cancer. (springer.com)
  • According to our results, overexpression of HSP72 in malignant tissues of patients with colorectal carcinoma is related to tumor progression, suggesting that these proteins could play an important role not only in tumorigenesis but also in the development of drug resistance. (ac.rs)
  • Following tumour resection protein was infused into tumor cavity. (springer.com)
  • Our results suggest that purified Hsp70 can induce specific effective anti-tumor immune response and warrants further investigation in randomised clinical trials. (springer.com)
  • Here, we report the efficient induction of tumor antigen-specific immune response by dendritic cells pulsed with recombinant fusion protein of Hsp70L1 and CEA 576-669 fragment of the carcinoembryonic antigen (CEA) containing CAP-1 (a HLA-A2-restricted CTL epitope). (aacrjournals.org)
  • Fusion protein CEA 576-669 -Hsp70L1 can promote dendritic cell maturation and activate dendritic cells to produce cytokines, such as interleukin-12, interleukin-1β, and tumor necrosis factor-α, and chemokines, such as macrophage inflammatory protein-1α, macrophage inflammatory protein-1β, and regulated on activation, normal T expressed and secreted, indicating the adjuvant ability of Hsp70L1 in the fusion protein. (aacrjournals.org)
  • HSP-peptide complexes isolated from intact tumor cells or virus-infected cells or reconstituted by covalent cross-link or fusion-protein strategies are all capable of eliciting potent CD8 + CTL responses to the antigenic peptides bound to the HSP ( 1 , 2 , 8 - 11 ). (aacrjournals.org)
  • For instance complementation studies concerning thirteen cytosolic J-domain protein exposed that at least four good examples (Sis1 Jjj1 Jjj3 Cwc23) fulfill exclusive functions in candida [34]. (cancer-ecosystem.com)
  • Using Western blot analyses, we noticed elevated levels of cytosolic HSP70 in colorectal cancer cells compared to normal. (ac.rs)
  • Hsp demonstrate specific affinity to particular classes of oncogenic peptides and client proteins in cancer cells, and are able to stabilize mutated oncogene proteins. (springer.com)
  • By expressing AliB-like ORF 1 and ORF 2 proteins, we have previously shown that they bind to peptides SETTFGRDFN (found in the 50S ribsosomal subunit protein L4 of Enterobacteriaceae) and FPPQSV (found in proteins of Prevotella species) respectively. (springer.com)
  • Antigen presenting cells display on their surface MHC class II (MHC II) 4 molecules bound to peptides derived from proteins degraded in endosomal compartments (reviewed in Ref. 1 ). (jimmunol.org)
  • When an Hsp70 protein is ATP bound, the lid is open and peptides bind and release relatively rapidly. (wikipedia.org)
  • When Hsp70 proteins are ADP bound, the lid is closed, and peptides are tightly bound to the substrate binding domain. (wikipedia.org)
  • This spontaneous interaction is reversible, and in the ATP bound state Hsp70 may relatively freely bind and release peptides. (wikipedia.org)
  • Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). (novusbio.com)
  • The other pathway, activated by developmental signals or certain cytotoxic drugs, is regulated by the interplay of pro- and antiapoptotic members of the Bcl-2 protein family and involves mitochondrial release of apoptogenic molecules (e.g., cytochrome c ) for caspase activation and cell demolition ( 4 ). (pnas.org)
  • In summary, A 1 receptor-regulator of G protein signaling-K ATP signaling, arachidonic acid cascade, nitric oxide system, markers of neuronal damage, mitochondrial damage-related molecules, and the mitogen-activated protein kinase and nuclear factor-κB pathway are associated with the mechanisms of PF preconditioning. (aspetjournals.org)
  • Exposure to the HFD led to hyperacetylation of proteins involved in gluconeogenesis, mitochondrial oxidative metabolism, methionine metabolism, liver injury and the ER (endoplasmic reticulum) stress response. (biochemj.org)
  • Livers of mice fed on the HFD had reduced SIRT3 activity, a 3-fold decrease in hepatic NAD + levels and increased mitochondrial protein oxidation. (biochemj.org)
  • Our results suggest that SIRT3 is an integral regulator of mitochondrial function and its depletion results in hyperacetylation of critical mitochondrial proteins that protect against hepatic lipotoxicity under conditions of nutrient excess. (biochemj.org)
  • 3 ] reported that acetylation of up to 70 mitochondrial proteins in liver changed by at least 2.5-fold in response to caloric restriction, suggesting the importance of extranuclear acetylation in events influencing metabolic fuel utilization. (biochemj.org)
  • Mos-Hsp70 complexes could be immunoprecipitated with both Mos and Hsp70 antibodies. (biomedsearch.com)
  • We are using previously developed assays to evaluate the recombinant proteins and their corresponding antibodies as potential inhibitors of spore adherence and/or host cell infectivity. (hindawi.com)
  • An immunohistochemical investigation was carried out with which we marked the localization of heat shock proteins 70 and 90 on the syncytiotrophoblastic, cytotrophoblastic, stromal and blood vessel cells, using specific antibodies which can detect the presence of those proteins on light microscopy. (uth.gr)
  • Results obtained in a DNA repair pathways study have shown that the HSP70s induced by stress (HSP72 and HSP70-1) take part in these pathways after several stresses (Xray and UV, magnetic field, hydrogen peroxide, cis-platin). (archives-ouvertes.fr)
  • HSP72 et HSP70-1) sont impliquées dans ces voies cellulaires après différents stress (rayonnement X et UV, champ magnétique, péroxyde d'hydrogène, cis-platine). (archives-ouvertes.fr)
  • Here, we demonstrate that the mere inhibition of its synthesis by adenoviral transfer or classical transfection of antisense Hsp70 cDNA (asHsp70) results in massive death of human breast cancer cells (MDA-MB-468, MCF-7, BT-549, and SK-BR-3), whereas the survival of nontumorigenic breast epithelial cells (HBL-100) or fibroblasts (WI-38) is not affected. (pnas.org)
  • 103:2035, 1986), which has been shown to recognize the protein product of the full- length rat hsp70 cDNA (Longo et al: J Neurosci Res 36:325, 1993). (elsevier.com)
  • After the 3rd screening of this cDNA library with a human genomic DNA probe for HSP70 (pH2.3), 4 cDNA clones were isolated (named pGA 3 , pGB 1 , pGD 3 and pGE 4 , respectively). (elsevier.com)
  • In this study we therefore isolated and characterized a cDNA encoding the DnaJ-like protein from G. cydonium designated GCDNAJ. (int-res.com)
  • Moreover, human GATA4 recombinant protein could upregulate R-spondin1 in P. olivaceus ovary cells and FBCs (flounder brain cell line). (bireme.br)
  • As a chaperone, heat shock protein acts as central integrators of protein homeostasis in cell. (scirp.org)
  • T. J. Hubbard and C. Sander, "The Role of Heat-Shock and Chaperone Proteins in Protein Folding: Possible Molecular Mechanisms," Protein Engineering, Vol. 4, No. 7, 1991, pp. 711-717. (scirp.org)
  • Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. (genecards.org)
  • During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). (nih.gov)
  • The molecular chaperone heat shock protein 70 (Hsp70) acts at multiple steps in a protein's existence cycle including through the processes of foldable trafficking remodeling and degradation. (cancer-ecosystem.com)
  • May subsets of Hsp70 substrates be disrupted regardless of the wide activity of the chaperone preferentially? (cancer-ecosystem.com)
  • We provide evidence that mouse c-Mos binds to Hsp70, a molecular chaperone. (biomedsearch.com)
  • Molecular chaperone Hsp70 is well known for its ability to stimulate innate and adaptive anti-cancer immune response. (springer.com)
  • Only members of the Hsp70 family with general chaperone functions have such general holder activity. (springer.com)
  • Hsp70 chaperone systems assist non-native folding intermediates to fold to the native state ('folder' activity). (springer.com)
  • In molecular biology, chaperone DnaJ , also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein . (wikipedia.org)
  • The MHC II molecules assemble in the endoplasmic reticulum with invariant chain (Ii), a type II transmembrane protein that acts as a chaperone, and carries the information required to deliver the MHC II molecules to the endocytic route. (jimmunol.org)
  • The term 'chaperone' is adopted from one of their functions, namely to keep other proteins from getting involved in 'inappropriate' aggregations. (wiley.com)
  • Furthermore, the reactivation of photosystem II after photoinhibition was enhanced in the HSP70B -overexpressing strain when compared with the wild type, both in the presence or absence of synthesis of chloroplast-encoded proteins. (plantcell.org)
  • The Heat Shock Proteins (HSP) are expressed at stress situations, such as hypovolemia, also they are involved at the process of collagen synthesis. (usp.br)
  • The application of NSY50 up-regulated most of the identified proteins that were involved in carbohydrate metabolism and amino acid metabolism under normal conditions, which implied that both energy generation and the production of amino acids were enhanced, thereby ensuring an adequate supply of amino acids for the synthesis of new proteins in cucumber seedlings to promote plant growth. (frontiersin.org)
  • Members of the Hsp70 family are very strongly upregulated by heat stress and toxic chemicals, particularly heavy metals such as arsenic, cadmium, copper, mercury, etc. (wikipedia.org)
  • This assay has high sensitivity and excellent specificity for detection of Heat Shock Protein 70 (HSP70). (mybiosource.com)
  • 2 Structure and Function Mouse monoclonal to CIB1 of Hsp70 Domain architecture Hsp70 is a 70 kDa molecular machine that binds hydrophobic peptide sequences hydrolyzes ATP and directs its substrates into a variety of distinct fates. (cancer-ecosystem.com)
  • Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. (nih.gov)
  • In the cellular milieu, Hsp70s exert these activities in the quality control of misfolded proteins and the co- and posttranslational folding of newly synthesized proteins. (springer.com)
  • These proteins have the ability, as suggested by their name, to be over expressed in cells after heat shock but also following a huge variety of stresses and in several diseases and cellular disorders (Tavaria M et al, 1996). (archives-ouvertes.fr)
  • HSP70 measure ability to respond to cellular damage, and this study shows a significant decrease in this ability as dogs age. (medindia.net)
  • Heat shock proteins (HSP) are reported to act as an effective adjuvant to enhance the induction of antigen peptide-specific cellular immunity ( 1 , 2 ). (aacrjournals.org)
  • Acetylation has recently emerged as an important mechanism for controlling a broad array of proteins mediating cellular adaptation to metabolic fuels. (biochemj.org)
  • Download DNA or protein sequence, view genomic context and coordinates. (yeastgenome.org)
  • In addition to other activities, they assist in the correct folding of nascent polypeptide chains as they emerge from the ribosome, they participate in transmembrane protein transport, and they prevent aggregation of denatured proteins and allow the disassembly of multimolecular complexes. (plantcell.org)
  • Mechanistically related but less understood is the role of Hsp70s in the disassembly of protein complexes such as clathrin coats, viral capsids and the nucleoprotein complex, which initiates the replication of bacteriophage λ DNA. (springer.com)
  • Three PcG fusion proteins, ZnF-PC, ZnF-SCM, and ZnF-ESC, were studied, since biochemical analyses place these PcG proteins in distinct complexes. (genetics.org)
  • In Sirt3 −/− mice, exposure to the HFD further increased the acetylation status of liver proteins and reduced the activity of respiratory complexes III and IV. (biochemj.org)
  • Heat stress is known to render rat islet cells resistant against the toxic effects of nitric oxide, reactive oxygen intermediates and the islet cell toxin streptozotocin. (nih.gov)
  • The accumulation of faulty protein folding would harm cells and can result in death. (scirp.org)
  • The HSP70 heat shock protein is induced by acidosis in cultured cells and in ischemic brain and protects cells against many types of injury. (elsevier.com)
  • Hsp70 was found to associate with Mos ectopically expressed in COS-1 cells. (biomedsearch.com)
  • It is known that c-Mos protein kinase activity in cell extracts of transfected COS-1 or NIH3T3 cells is labile. (biomedsearch.com)
  • While YD-9 cells showed high resistance to chemotherapeutic agents such as etoposide and 5-fluorouraci (5-FU), HSP70 antisense oligonucelotides sensitized chemoresistant YD-9 cells to etoposide and 5-FU. (bvsalud.org)
  • cells and to compare the concentration of placental HSP70 & 90 in term deliveries and in missed miscarriages. (uth.gr)
  • The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. (wikipedia.org)
  • Heat shock proteins (HSP) have been revealed to interact with antigen-presenting cells and have potent adjuvant capability to induce antigen-specific CD8 + CTL and Th1 responses. (aacrjournals.org)
  • Surprisingly, in both COS-7 cells and hippocampal neurons, GKAP forms insoluble aggregates with Shank that colocalize with heat shock protein 70 and neurofilaments, two markers of the aggresomes in which misfolded proteins accumulate. (jneurosci.org)
  • However, the two proteins are organized in clusters in COS cells and synaptic clusters in neurons when both are overexpressed and associated with wild-type PSD-95, but not with palmitoylation-deficient PSD-95. (jneurosci.org)
  • Heat shock protein 70 (Hsp70) mediates Zika virus entry, replication, and egress from host cells. (sc.edu)
  • The human heat-shock protein multigene family comprises several highly conserved proteins with structural and functional properties in common, but which vary in the extent of their inducibility in response to metabolic stress. (nus.edu.sg)
  • G. Banumathy, V. Singh, S. R. Pavithra, and U. Tatu, "Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes," Journal of Biological Chemistry , vol. 278, no. 20, pp. 18336-18345, 2003. (hindawi.com)
  • Human Heat Shock Protein 70 (GenBank Accession No. NM_005345), a.a. 2-641 with C-terminal His-tag, MW = 71 kDa, expressed in E. coli . (bpsbioscience.com)
  • Burnie JP, Carter TL, Hodgetts SJ, Matthews RC (2006) Fungal heat-shock proteins in human disease. (usp.br)
  • Purpose: To investigate the role of heat shock protein (HSP) on the chorionic villi of human placenta! (uth.gr)
  • HSP22 and HSP70 are human proteins belonging to Heat Shock Proteins family. (archives-ouvertes.fr)
  • These results suggest that the bacteria-like vesicles and refringent particles observed in human blood represent non-living membrane vesicles and protein aggregates derived from blood. (nature.com)
  • Synthetic peptide corresponding to aa 574-591 of human HSP70. (novusbio.com)
  • Synthetic peptide within Human Hsp70 aa 600-700 (C terminal). (abcam.com)
  • Orthologous to human HSPA1B (heat shock protein family A (Hsp70) member 1B). (jax.org)
  • Using western blot analysis of levels of heat-shock protein 70 (Hsp70), we examined the heat-shock responses of four Lottia congeners: Lottia scabra and L. austrodigitalis, which occur in the high-intertidal zone, and L. pelta and L. scutum, which are restricted to the low- and mid-intertidal zones. (nih.gov)
  • In the absence of ATP from cell extracts, protein kinase activity of Mos was lost within 6 h on ice even though the Mos protein was not degraded and remained bound to Hsp70. (biomedsearch.com)
  • To provide further evidence for the functional significance of Hsp70 interaction to Mos function, we show that the residue serine 3 in Mos, which is important for the regulation of protein kinase activity of Mos is also important for Hsp70 association. (biomedsearch.com)
  • We investigated the molecular mechanisms of Shank1 targeting and synapse assembly by looking at the function of guanylate kinase-associated protein (GKAP) and PSD-95 interactions. (jneurosci.org)
  • Shank and GKAP (guanylate kinase-associated protein) are probably two of the major scaffold proteins organizing the PSD. (jneurosci.org)
  • Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIA(Ntr) in Escherichia coli. (labome.org)
  • They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. (springer.com)
  • All of these activities appear to be based on the property of Hsp70 to interact with hydrophobic peptide segments of proteins in an ATP-controlled fashion. (springer.com)
  • Based on lipid analysis and Western blotting, we show that the bacteria-like entities consist of membrane vesicles containing serum and exosome proteins, including albumin, fetuin-A, apolipoprotein-A1, alkaline phosphatase, TNFR1 and CD63. (nature.com)
  • Postsynaptic density (PSD) proteins include scaffold, cytoskeletal, and signaling proteins that structurally and functionally interact with glutamate receptors and other postsynaptic membrane proteins. (jneurosci.org)
  • The postsynaptic density (PSD) consists of a network of interacting proteins that form an electron-dense organelle right beneath the postsynaptic membrane. (jneurosci.org)
  • We show that activated HSF associates with hsp70 and that the interaction is detected as the levels of hsp70 increase in the cell. (nih.gov)
  • A. L. Edkins, M. H. Ludewig, and G. L. Blatch, "A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40," International Journal of Biochemistry and Cell Biology , vol. 36, no. 8, pp. 1585-1598, 2004. (hindawi.com)
  • However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. (genecards.org)
  • Hsp70 by itself is characterized by a very weak ATPase activity, such that spontaneous hydrolysis will not occur for many minutes. (wikipedia.org)
  • The best known of these cochaperones are the bacterial DnaJ and GrpE proteins and their eukaryotic homologs. (plantcell.org)
  • Arrhenius analysis of the relationship between hyperthermia and Hsp70 promoter activation: a comparison between ex vivo and in vivo data. (semanticscholar.org)
  • In in vivo studies we proved the efficacy of the intratumoral delivery of Hsp70 in the model of intracranial glioma C6 in animals. (springer.com)
  • Based on our preclinical in vivo data we conducted for the first time pilot study for assessment of anti-tumour activity of Hsp70 in patients with brain tumours. (springer.com)
  • Gentaur Molecular :Prosci \ HSPA4 (Hsp70) belongs to the heat shock protein 70 family. (antibody-antibodies.com)
  • Product Detail : 26-101 HSPA4 (Hsp70) belongs to the heat shock protein 70 family. (antibody-antibodies.com)
  • We have also other products like : HSPA4 (Hsp70) belongs to the heat shock protein 70 family. (antibody-antibodies.com)
  • The Bcl-2 protein family contains three major subgroups. (pnas.org)
  • This family of proteins contain a 70 amino acid consensus sequence known as the J domain. (wikipedia.org)
  • Proteins in this family consist of three domains . (wikipedia.org)
  • To date, investigations have focused primarily on the Hsp70 family. (wiley.com)
  • In most species, there are many proteins that belong to the Hsp70 family. (embl.de)
  • X.-Q. Bao and G.-T. Liu, "Induction of overexpression of the 27- and 70-kDa heat shock proteins by bicyclol attenuates concanavalin A-induced liver injury through suppression of nuclear factor- κ B in mice," Molecular Pharmacology , vol. 75, no. 5, pp. 1180-1188, 2009. (hindawi.com)
  • no induction of Hsp70 occurred in L. scabra. (nih.gov)
  • Therefore, this study determined whether induction of heat shock proteins protects cultured astrocytes against acidosis. (elsevier.com)
  • Since heat shock did not protect against acidosis at 24 h when HSP70 induction was maximal but did protect at 48 h when HSP70 was markedly diminished, the protective effect of heat shock at 48 h may be related to stress proteins present at 48 h. (elsevier.com)
  • It is concluded that induction of HSP70 and other heat shock proteins by heat shock protects astrocytes against subsequent lethal heat shock. (elsevier.com)
  • However, heat shock and acid treatment increase the vulnerability of astrocytes to acidosis 24 h later in spite of the induction of HSP70 heat shock proteins. (elsevier.com)
  • The finding that heat shock protected astrocytes against acidosis 2 days later may suggest that delayed induction of stress proteins partially protects the astrocytes against damage produced by high concentrations of hydrogen ions. (elsevier.com)
  • Hsp70-like protein 1 (Hsp70L1) is structurally and functionally similar to Hsp70 and has the ability to promote dendritic cell maturation and activation as described previously by us ( 13 ). (aacrjournals.org)
  • In the ATP-bound form, it has a low affinity for substrate proteins. (genecards.org)
  • Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. (genecards.org)
  • Inoculation with FOC inhibited most of the proteins related to carbohydrate and energy metabolism and to protein metabolism. (frontiersin.org)
  • The combined inoculation treatment (NSY50+FOC) accumulated abundant proteins involved in defense mechanisms against oxidation and detoxification as well as carbohydrate metabolism, which might play important roles in preventing pathogens from attacking. (frontiersin.org)
  • Taken together, these results suggest that P. polymyxa NSY50 may promote plant growth and alleviate FOC-induced damage by improving the metabolism and activation of defense-related proteins in cucumber roots. (frontiersin.org)
  • It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. (nih.gov)
  • Evidence of an interaction between Mos and Hsp70: a role of the Mos residue serine 3 in mediating Hsp70 association. (biomedsearch.com)
  • Interaction of heat shock protein 70 (HSP70) polymorphisms and occupational hazards increases the risk of hypertension in coke oven workers. (cdc.gov)
  • We therefore explore the possible role of HSP70 polymorphisms and their interaction with occupational environment in hypertension risk. (cdc.gov)
  • Further analysis of the interaction of HSP70 polymorphisms with occupational environment indicated a strong positive interaction between HSP70 genotype (HSP70-1 GC+CC, HSP70-2 AA and HSP70-hom TC+CC) and oven top workplace. (cdc.gov)
  • Repression by ZnF-SCM required a protein interaction domain, the SPM domain, which suggests that this domain is not primarily used to direct SCM to chromosomal loci. (genetics.org)

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