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 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.
A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.
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 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.
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.
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 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 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 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 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 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.
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.
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.
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.
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.
A subfamily of small heat-shock proteins found in a wide variety of organisms.
Proteins found in any species of bacterium.
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.
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.
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 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.
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.
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.
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.
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 broad-spectrum antibiotic that is being used as prophylaxis against disseminated Mycobacterium avium complex infection in HIV-positive patients.
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.
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.
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.
Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
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.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
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.
The sum of the weight of all the atoms in a molecule.
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 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.
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.
Proteins obtained from ESCHERICHIA COLI.
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.
Cellular proteins and peptides that are induced in response to cold stress. They are found in a broad variety of prokaryotic and eukaryotic organisms.
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.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
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.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Proteins prepared by recombinant DNA technology.
Elements of limited time intervals, contributing to particular results or situations.
A flavonol widely distributed in plants. It is an antioxidant, like many other phenolic heterocyclic compounds. Glycosylated forms include RUTIN and quercetrin.
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.
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.
A cell line derived from cultured tumor cells.
Inorganic compounds that contain sodium as an integral part of the molecule.
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.
Shock resulting from diminution of cardiac output in heart disease.
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 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.
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).
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 phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
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.
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 degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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).
The process by which chemical compounds provide protection to cells against harmful agents.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
(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.
Adaptation to a new environment or to a change in the old.
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 biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
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.
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.
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 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.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
The non-genetic biological changes of an organism in response to challenges in its ENVIRONMENT.
An absence of warmth or heat or a temperature notably below an accustomed norm.
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.
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 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.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
Shock produced as a result of trauma.
A species of fruit fly much used in genetics because of the large size of its chromosomes.
A protein which is a subunit of RNA polymerase. It effects initiation of specific RNA chains from DNA.
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.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
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.
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.
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.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
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.
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.
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.
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
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.
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.
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.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
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.
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.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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.
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).
The relationship between the dose of an administered drug and the response of the organism to the drug.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
The functional hereditary units of BACTERIA.
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 group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
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.
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 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)
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 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.
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.
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.
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)
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.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
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.
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.
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 pattern recognition receptor that interacts with LYMPHOCYTE ANTIGEN 96 and LIPOPOLYSACCHARIDES. It mediates cellular responses to GRAM-NEGATIVE BACTERIA.
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.
Proteins found in any species of fungus.
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.
The measure of the level of heat of a human or animal.
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.
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 species of CHLAMYDOPHILA that causes acute respiratory infection, especially atypical pneumonia, in humans, horses, and koalas.
Immunoglobulins produced in a response to BACTERIAL ANTIGENS.
Substances elaborated by bacteria that have antigenic activity.
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.
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)
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 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.
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 strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.
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 termination of the cell's ability to carry out vital functions such as metabolism, growth, reproduction, responsiveness, and adaptability.
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.
Type species of CHLAMYDIA causing a variety of ocular and urogenital diseases.
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.
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.
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.
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.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
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.
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.
The relationships of groups of organisms as reflected by their genetic makeup.
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.
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).
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
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).
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
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.
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.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
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.
Chemical substances, produced by microorganisms, inhibiting or preventing the proliferation of neoplasms.
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)
Substances that inhibit or prevent the proliferation of NEOPLASMS.
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.
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.
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)
Serological reactions in which an antiserum against one antigen reacts with a non-identical but closely related antigen.
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.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
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.
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.
A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
Disorders caused by imbalances in the protein homeostasis network - synthesis, folding, and transport of proteins; post-translational modifications; and degradation or clearance of misfolded proteins.
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.
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.
Twenty-carbon compounds derived from MEVALONIC ACID or deoxyxylulose phosphate.
Antibodies produced by a single clone of cells.

Mrj encodes a DnaJ-related co-chaperone that is essential for murine placental development. (1/8916)

We have identified a novel gene in a gene trap screen that encodes a protein related to the DnaJ co-chaperone in E. coli. The gene, named Mrj (mammalian relative of DnaJ) was expressed throughout development in both the embryo and placenta. Within the placenta, expression was particularly high in trophoblast giant cells but moderate levels were also observed in trophoblast cells of the chorion at embryonic day 8.5, and later in the labyrinth which arises from the attachment of the chorion to the allantois (a process called chorioallantoic fusion). Insertion of the ROSAbetageo gene trap vector into the Mrj gene created a null allele. Homozygous Mrj mutants died at mid-gestation due to a failure of chorioallantoic fusion at embryonic day 8.5, which precluded formation of the mature placenta. At embryonic day 8.5, the chorion in mutants was morphologically normal and expressed the cell adhesion molecule beta4 integrin that is known to be required for chorioallantoic fusion. However, expression of the chorionic trophoblast-specific transcription factor genes Err2 and Gcm1 was significantly reduced. The mutants showed no abnormal phenotypes in other trophoblast cell types or in the embryo proper. This study indicates a previously unsuspected role for chaperone proteins in placental development and represents the first genetic analysis of DnaJ-related protein function in higher eukaryotes. Based on a survey of EST databases representing different mouse tissues and embryonic stages, there are 40 or more DnaJ-related genes in mammals. In addition to Mrj, at least two of these genes are also expressed in the developing mouse placenta. The specificity of the developmental defect in Mrj mutants suggests that each of these genes may have unique tissue and cellular activities.  (+info)

Molecular chaperones: small heat shock proteins in the limelight. (2/8916)

Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.  (+info)

Cooperative binding of heat shock factor to the yeast HSP82 promoter in vivo and in vitro. (3/8916)

Previous work has shown that heat shock factor (HSF) plays a central role in remodeling the chromatin structure of the yeast HSP82 promoter via constitutive interactions with its high-affinity binding site, heat shock element 1 (HSE1). The HSF-HSE1 interaction is also critical for stimulating both basal (noninduced) and induced transcription. By contrast, the function of the adjacent, inducibly occupied HSE2 and -3 is unknown. In this study, we examined the consequences of mutations in HSE1, HSE2, and HSE3 on HSF binding and transactivation. We provide evidence that in vivo, HSF binds to these three sites cooperatively. This cooperativity is seen both before and after heat shock, is required for full inducibility, and can be recapitulated in vitro on both linear and supercoiled templates. Quantitative in vitro footprinting reveals that occupancy of HSE2 and -3 by Saccharomyces cerevisiae HSF (ScHSF) is enhanced approximately 100-fold through cooperative interactions with the HSF-HSE1 complex. HSE1 point mutants, whose basal transcription is virtually abolished, are functionally compensated by cooperative interactions with HSE2 and -3 following heat shock, resulting in robust inducibility. Using a competition binding assay, we show that the affinity of recombinant HSF for the full-length HSP82 promoter is reduced nearly an order of magnitude by a single-point mutation within HSE1, paralleling the effect of these mutations on noninduced transcript levels. We propose that the remodeled chromatin phenotype previously shown for HSE1 point mutants (and lost in HSE1 deletion mutants) stems from the retention of productive, cooperative interactions between HSF and its target binding sites.  (+info)

Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin. (4/8916)

This report demonstrates that Gadd45, a p53-responsive stress protein, can facilitate topoisomerase relaxing and cleavage activity in the presence of core histones. A correlation between reduced expression of Gadd45 and increased resistance to topoisomerase I and topoisomerase II inhibitors in a variety of human cell lines was also found. Gadd45 could potentially mediate this effect by destabilizing histone-DNA interactions since it was found to interact directly with the four core histones. To evaluate this possibility, we investigated the effect of Gadd45 on preassembled mononucleosomes. Our data indicate that Gadd45 directly associates with mononucleosomes that have been altered by histone acetylation or UV radiation. This interaction resulted in increased DNase I accessibility on hyperacetylated mononucleosomes and substantial reduction of T4 endonuclease V accessibility to cyclobutane pyrimidine dimers on UV-irradiated mononucleosomes but not on naked DNA. Both histone acetylation and UV radiation are thought to destabilize the nucleosomal structure. Hence, these results imply that Gadd45 can recognize an altered chromatin state and modulate DNA accessibility to cellular proteins.  (+info)

Role of nitric oxide in lipopolysaccharide-induced hepatic injury in D-galactosamine-sensitized mice as an experimental endotoxic shock model. (5/8916)

The role of nitric oxide (NO) in lipopolysaccharide (LPS)-induced hepatic injury was studied in D-galactosamine (D-GalN)-sensitized mice. The inducible isoform of NO synthase (iNOS) was immunohistochemically detected on hepatocytes around blood vessels in livers of mice injected with D-GalN and LPS not on hepatocytes in mice injected with D-GalN or LPS alone, although mRNA for iNOS was found in those mice. Nitrotyrosine (NT) was also found in livers of mice injected with D-GalN and LPS. The localization of NT was consistent with that of iNOS, and the time courses of NT and iNOS expression were almost the same. Expression of iNOS and NT was detected exclusively in the hepatic lesions of mice injected with D-GalN and LPS. Anti-tumor necrosis factor alpha neutralizing antibody inhibited iNOS and NT expression and hepatic injury. The results suggested that NO from iNOS may play a role in LPS-induced hepatic injury on D-GalN-sensitized mice as an experimental endotoxic shock model.  (+info)

Role of Listeria monocytogenes exotoxins listeriolysin and phosphatidylinositol-specific phospholipase C in activation of human neutrophils. (6/8916)

Polymorphonuclear leukocytes (PMN) are essential for resolution of infections with Listeria monocytogenes. The present study investigated the role of the listerial exotoxins listeriolysin (LLO) and phosphatidylinositol-specific phospholipase C (PlcA) in human neutrophil activation. Different Listeria strains, mutated in individual virulence genes, as well as purified LLO were used. Coincubation of human neutrophils with wild-type L. monocytogenes provoked PMN activation, occurring independently of phagocytosis events, with concomitant elastase secretion, leukotriene generation, platelet-activating factor (PAF) synthesis, respiratory burst, and enhanced phosphoinositide hydrolysis. Degranulation and leukotriene formation were noted to be solely dependent on LLO expression, as these features were absent when the LLO-defective mutant EGD- and the avirulent strain L. innocua were used. These effects were fully reproduced by a recombinant L. innocua strain expressing LLO (INN+) and by the purified LLO molecule. LLO secretion was also required for PAF synthesis. However, wild-type L. monocytogenes was more potent in eliciting PAF formation than mutants expressing LLO, suggesting the involvement of additional virulence factors. This was even more obvious for phosphoinositide hydrolysis and respiratory burst: these events were provoked not only by INN+ but also by the LLO-defective mutant EGD- and by a recombinant L. innocua strain producing listerial PlcA. We conclude that human neutrophils react to extracellularly provided listerial exotoxins by rapid cell activation. Listeriolysin is centrally involved in triggering degranulation and lipid mediator generation, and further virulence factors such as PlcA apparently contribute to trigger neutrophil phosphoinositide hydrolysis and respiratory burst. In this way, listerial exotoxins may influence the host defense against infections with L. monocytogenes.  (+info)

Chaperone activity with a redox switch. (7/8916)

Hsp33, a member of a newly discovered heat shock protein family, was found to be a very potent molecular chaperone. Hsp33 is distinguished from all other known molecular chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function. In vitro and in vivo experiments suggest that Hsp33 protects cells from oxidants, leading us to conclude that we have found a protein family that plays an important role in the bacterial defense system toward oxidative stress.  (+info)

Overexpression of human homologs of the bacterial DnaJ chaperone in the synovial tissue of patients with rheumatoid arthritis. (8/8916)

OBJECTIVE: To study the expression of the chaperone family of J proteins in the synovial tissue of patients with rheumatoid arthritis (RA) or osteoarthritis. METHODS: Rabbit antibodies specific for a synthetic peptide (pHSJ1: EAYEVLSDKHKREIYD), representing the most conserved part of all J domains thus far identified--among them the Drosophila tumor suppressor Tid56--were used in immunohistochemical analyses of frozen sections of synovial tissue and immunoblotting of protein extracts of adherent synovial cells. IgG specific for Tid56 was also used. RESULTS: Both antisera predominantly and intensely stained synovial lining cells from RA patients; other cells did not stain or stained only faintly. In immunoblots, anti-pHSJ1 specifically detected several bands with molecular weights of >74 kd (type I), 57-64 kd (type II), 41-48 kd (type III), and < or =36 kd (type IV). The strongest band detected in RA adherent synovial cells was the type II band, whereas in a B cell line, a type I band was prominent. CONCLUSION: Several potentially new members of the J family are described. The type II band represents the human homolog of the Drosophila Tid56 protein and is strongly expressed in RA synovial tissue.  (+info)

Looking for online definition of heat-shock transcription factor family member 5 in the Medical Dictionary? heat-shock transcription factor family member 5 explanation free. What is heat-shock transcription factor family member 5? Meaning of heat-shock transcription factor family member 5 medical term. What does heat-shock transcription factor family member 5 mean?
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 ...
A single hyperthermic exposure can render cells transiently resistant to subsequent high temperature stresses. Treatment of rat embryonic fibroblasts with cycloheximide for 6 h after a 20-min interval at 45 degrees C inhibits protein synthesis, including heat shock protein (hsp) synthesis, and results in an accumulation of hsp 70 mRNA, but has no effect on subsequent survival responses to 45 degrees C hyperthermia. hsp 70 mRNA levels decreased within 1 h after removal of cycloheximide but then appeared to stabilize during the next 2 h (3 h after drug removal and 9 h after heat shock). hsp 70 mRNA accumulation could be further increased by a second heat shock at 45 degrees C for 20 min 6 h after the first hyperthermic exposure in cycloheximide-treated cells. Both normal protein and hsp synthesis appeared increased during the 6-h interval after hyperthermia in cultures which received two exposures to 45 degrees C for 20 min compared with those which received only one treatment. No increased hsp ...
TY - JOUR. T1 - Both near ultraviolet radiation and the oxidizing agent hydrogen peroxide induce a 32-kDa stress protein in normal human skin fibroblasts. AU - Keyse, Stephen M.. AU - Tyrrell, Rex M.. PY - 1987/10/25. Y1 - 1987/10/25. N2 - We have analyzed the pattern of protein synthesis in solar near ultraviolet (334 nm, 365 nm) and near visible (405 nm) irradiated normal human skin fibroblasts. Two hours after irradiation we find that one major stress protein of approximately 32 kDa is induced in irradiated cells. This protein is not induced by ultraviolet radiation at wavelengths shorter than 334 nm and is not inducible by heat shock treatment of these cells. Although sodium arsenite, diamide, and menadione all induced a 32-kDa protein, they also induced the major heat shock proteins. In contrast, the oxidizing agent, hydrogen peroxide, induced the low molecular weight stress protein without causing induction of the major heat shock proteins. A comparison of the 32-kDa proteins induced by ...
Elevated temperatures induce activation of the heat shock transcription factor 1 (HSF1) which in somatic cells leads to heat shock proteins synthesis and cytoprotection. However, in the male germ cells (spermatocytes) caspase-3 dependent apoptosis is induced upon HSF1 activation and spermatogenic cells are actively eliminated. To elucidate a mechanism of such diverse HSF1 activity we carried out genome-wide transcriptional analysis in control and heat-shocked cells, either spermatocytes or hepatocytes. Additionally, to identify direct molecular targets of active HSF1 we used chromatin immunoprecipitation assay (ChIP) combined with promoter microarrays (ChIP on chip). Genes that are differently regulated after HSF1 binding during hyperthermia in both types of cells have been identified. Despite HSF1 binding to promoter sequences in both types of cells, strong up-regulation of Hsps and other genes typically activated by the heat shock was observed only in hepatocytes. In spermatocytes HSF1 binding
The heat shock response is thought to be important for adaptation of organisms to their thermal environment (Feder and Hofmann, 1999; Hoffmann et al., 2003; Somero, 2005). A number of characteristics of the heat shock response could, in principle, respond to thermal selection, including: (1) the functional efficiency of the heat shock proteins themselves, (2) the onset temperature (Ton) at which hsp expression is induced, and (3) the magnitude of hsp expression under either basal or induced conditions. Although there is some evidence for each of these mechanisms in natural populations or following laboratory selection (Tomanek and Somero, 1999; Michalak et al., 2001; Feder et al., 2002; Sorensen et al., 2005) little is known about whether similar patterns are observed across multiple isoforms within a species, and few studies have assessed the relative roles and generality of these mechanisms.. We found no differences in the amino acid sequences of hsp70-1 or hsp70-2 within or between ...
The heat shock response is thought to be important for adaptation of organisms to their thermal environment (Feder and Hofmann, 1999; Hoffmann et al., 2003; Somero, 2005). A number of characteristics of the heat shock response could, in principle, respond to thermal selection, including: (1) the functional efficiency of the heat shock proteins themselves, (2) the onset temperature (Ton) at which hsp expression is induced, and (3) the magnitude of hsp expression under either basal or induced conditions. Although there is some evidence for each of these mechanisms in natural populations or following laboratory selection (Tomanek and Somero, 1999; Michalak et al., 2001; Feder et al., 2002; Sorensen et al., 2005) little is known about whether similar patterns are observed across multiple isoforms within a species, and few studies have assessed the relative roles and generality of these mechanisms.. We found no differences in the amino acid sequences of hsp70-1 or hsp70-2 within or between ...
Hepatitis C virus (HCV) infection has a worldwide prevalence of 3% and is the main entity responsible for liver transplantation in developed countries for treat...
The heat shock transcription factors (HSFs) are the major heat shock factors regulating the heat stress response. They participate in regulating the expression of heat shock proteins (HSPs), which are critical in the protection against stress damage and many other important biological processes. Study of the HSF gene family is important for understanding the mechanism by which plants respond to stress. The completed genome sequences of rice (Oryza sativa) and Arabidopsis (Arabidopsis thaliana) constitute a valuable resource for comparative genomic analysis, as they are representatives of the two major evolutionary lineages within the angiosperms: the monocotyledons and the dicotyledons. The identification of phylogenetic relationships among HSF proteins in these species is a fundamental step to unravel the functionality of new and yet uncharacterized genes belonging to this family. In this study, the full complement of HSF genes in rice and Arabidopsis has probably been identified through the ...
DNA-binding activity of a maize heat shock transcription factor (HSF) was induced by heat shock of a whole cell extract at 44°C. Addition of the calcium ion chelator EGTA reduced the binding of the HSF to heat shock element (HSE) in vitro. Re-addition of CaCl2 to the sample pretreated with EGTA restored the ability of the HSF to bind to DNA. DNA-binding activity of the HSF was also induced by directly adding CaCl2 to a whole cell extract at non-heat-shock temperature, but not by MgCl2. During HS at 44°C, calmodulin (CaM) antagonists chlorpromazine (CPZ) and N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W7) inhibited DNA-binding activity of the HSF in a concentration-dependent manner, but N-(6-aminohexyl)-1-naphthalenesulfonamide (W5), an inactive structural analogue of W7, did not. Addition of antiserum specific to CaM reduced the binding of the HSF to HSE. Re-addition of CaM to the sample pretreated with antiserum could restore the binding activity of the HSF. DNA-binding activity of ...
Heat shock response in eukaryotes is transcriptionally regulated by conserved heat shock transcription factors (Hsfs). Hsf genes are represented by a large multigene family in plants and investigation of the Hsf gene family will serve to elucidate the mechanisms by which plants respond to stress. In recent years, reports of genome-wide structural and evolutionary analysis of the entire Hsf gene family have been generated in two model plant systems, Arabidopsis and rice. Maize, an important cereal crop, has represented a model plant for genetics and evolutionary research. Although some Hsf genes have been characterized in maize, analysis of the entire Hsf gene family were not completed following Maize (B73) Genome Sequencing Project. A genome-wide analysis was carried out in the present study to identify all Hsfs maize genes. Due to the availability of complete maize genome sequences, 25 nonredundant Hsf genes, named ZmHsfs were identified. Chromosomal location, protein domain and motif organization of
In order to assess specific functional roles of plant heat shock transcription factors (HSF) we conducted a transcriptome analysis of Arabidopsis thaliana hsfA1a/hsfA1b double knock out mutants and wild-type plants. We used Affymetrix ATH1 microarrays (representing more than 24 000 genes) and conduc …
The HSPA5 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. Order western blots of the GRP-78 antibody from Abgent.
Induction of cell stress through gene transfer of an engineered heat shock transcription factor enhances tumor immunogenicity.s profile, publications, research topics, and co-authors
An overview of the mammalian heat shock factor (HSF) family members and their biological functions. HSFs contribute to multiple normal physiological processes and pathologies through direct regulation of their target genes. The HSF target genes that have been identified in vivo are shown. HSF1 was originally recognized as the principal stress-responsive regulator of the heat shock response, but now HSF2 is known to modulate HSF1-mediated expression of heat shock protein (HSP) genes through heterocomplex formation. On heat shock, HSF1 and HSF2 accumulate into nuclear stress bodies (NSBs), where they bind to satellite III repeats. HSF1 is also a regulator of immune responses and cancer. So far, the regulation of HSP genes in ageing has most intensively been examined in Caenorhabditis elegans. Both HSF1 and HSF2 have been ascribed regulatory functions in several developmental processes, such as oogenesis, spermatogenesis and corticogenesis. HSF4 is involved in the development of different sensory ...
Cell surface proteins major histocompatibility complex (MHC) class I-related chain A (MICA) and UL16-binding proteins (ULBP) 1, 2, and 3 are up-regulated upon infection or tumor transformation and can activate human natural killer (NK) cells. Patches of cross-linked raft resident ganglioside GM1 colocalized with ULBP1, 2, 3, or MICA, but not CD45. Thus, ULBPs and MICA are expressed in lipid rafts at the cell surface. Western blotting revealed that glycosylphosphatidylinositol (GPI)-anchored ULBP3 but not transmembrane MICA, MHC class I protein, or transferrin receptor, accumulated in detergent-resistant membranes containing GM1. Thus, MICA may have a weaker association with lipid rafts than ULBP3, yet both proteins accumulate at an activating human NK cell immune synapse. Target cell lipid rafts marked by green fluorescent protein-tagged GPI also accumulate with ULBP3 at some synapses. Electron microscopy reveals constitutive clusters of ULBP at the cell surface. Regarding a specific molecular basis for
Under changes in conditions as diverse as temperature, oxidation or pH, proteins in an organism may undergo harmful denaturation. Small Heat Shock proteins act as paramedics of the cell: during such events they quicky intervene by binding nascently unfolding proteins, leading them to refolding or denaturation pathways. Small heat shock proteins are ubiquitous in all kingdoms of life, but especially effective in plants: after all, plants cannot escape from harsh environmental conditions!. Collaborating with Benesch (University of Oxford) and Vierling (UMass) groups, we have contributed to shedding light into the mode of action of small Heat Shock Proteins in wheat and pea.. We describe a mechanism whereby dimers of these proteins are responsible for capturing their substrate, before assemblying into larger complexes. With our own integrative modelling methods using distance restraints and collision cross-section measurements, we demonstrate that small heat shock protein dimers assemble into ...
Lipoprotein NlpI of Escherichia coli is involved in the cell division, virulence, and bacterial interaction with eukaryotic host cells. To elucidate the functional mechanism of NlpI, we examined how NlpI affects cell division and found that induction of NlpI inhibits nucleoid division and halts cell growth. Consistent with these results, the cell division protein FtsZ failed to localize at the septum but diffused in the cytosol. Elevation of NlpI expression enhanced the transcription and the outer membrane localization of the heat shock protein IbpA and IbpB. Deletion of either ibpA or ibpB abolished the effects of NlpI induction, which could be restored by complementation. The C-terminus of NlpI is critical for the enhancement in IbpA and IbpB production, and the N-terminus of NlpI is required for the outer membrane localization of NlpI, IbpA, and IbpB. Furthermore, NlpI physically interacts with IbpB. These results indicate that over-expression of NlpI can interrupt the nucleoids division and the
The heat-inducible members of the Hsp100 (or Clp) family of proteins share a common function in helping organisms to survive extreme stress, but the basic mechanism through which these proteins function is not understood. Hsp104 protects cells against a variety of stresses, under many physiological …
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, ...
heat-shock protein (HSP) Any of various proteins that are synthesized by living cells in response to increased temperature. They occur in both eukaryotes and prokaryotes, and function mainly as molecular chaperones, protecting the cells proteins as they become unfolded due to heating and enabling them to refold correctly. Source for information on heat-shock protein: A Dictionary of Biology dictionary.
TY - JOUR. T1 - Heat-shock proteins as dendritic cell-targeting vaccines - getting warmer. AU - McNulty, Shaun. AU - Colaco, Camilo. AU - Blandford, Lucy. AU - Bailey, Christopher. AU - Baschieri, Selene. AU - Todryk, Stephen. PY - 2013. Y1 - 2013. N2 - Heat-shock proteins (hsp) provide a natural link between innate and adaptive immune responses by combining the ideal properties of antigen carriage (chaperoning), targeting and activation of antigen-presenting cells (APC), including dendritic cells (DC). Targeting is achieved through binding of hsp to distinct cell surface receptors and is followed by antigen internalization, processing and presentation. An improved understanding of the interaction of hsp with DC has driven the development of numerous hsp-containing vaccines, designed to deliver antigens directly to DC. Studies in mice have shown that for cancers, such vaccines generate impressive immune responses and protection from tumour challenge. However, translation to human use, as for ...
DNAJB5 (DnaJ heat shock protein family (Hsp40) member B5), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
DNAJA4 (DnaJ heat shock protein family (Hsp40) member A4), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
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
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, ...
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Complete information for CLPB gene (Protein Coding), ClpB Homolog, Mitochondrial AAA ATPase Chaperonin, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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 ...
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 ...
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Debio 0932, also known as CUDC-305, is a novel heat shock protein 90 (HSP90) inhibitor with strong affinity for HSP90 alpha/beta, high oral bioavailability and potent anti-proliferative activity against a broad range of cancer cell lines (with a mean IC50 of 220 nmol/L), including many non-small cell lung cancer (NSCLC) cell lines which are resistant to standard-of-care (SOC) agents.
Retinal diseases, such as hereditary retinitis pigmentosa and age-related macular degeneration, are characterized by the progressive loss of photoreceptors. Histone deacetylase 6 (HDAC6) is considered as a stress surveillance factor and a potential target for neuroprotection and regeneration. Overexpression of HDAC6 has been connected to neurodegenerative disorders, and its suppression may provide protection. Here we show that HDAC6 is constitutively present in the mouse retina, and in the cone-like mouse cell line 661W. In 661W cells HDAC6 inhibition by the specific inhibitor tubastatin A (TST) led to the acetylation of α-tubulin, which is a major substrate for HDAC6. After oxidative stress, exerted by hydrogen peroxide, TST promoted cell survival and the upregulation of heat-shock proteins HSP70 and HSP25 by activation of heat-shock transcription factor 1. Furthermore, in response to oxidative stress the redox regulatory protein peroxiredoxin 1 (Prx1) was modulated in 661W cells by HDAC6 inhibition.
Transcriptional Stability of Heat Shock Protein Genes and Cell Proliferation Rate Provides an Evidence of Superior Cellular Tolerance of Sahiwal (Bos indicus) Cow PBMCs to Summer Stress. Research & Reviews is a scientific organization that drives the progress of research through open access journals.
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., ...
Over the last few years, some of our experiments in which mycobacterial heat-shock protein HSP antigens were presented to the immune system as if they were viral antigens have had a significant impact on our understanding of protective immunity against tuberculosis. They have also markedly enhanced the prospects for new vaccines. We now know...
HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products…
Heat-shock protein 27 kinase (Science: enzyme) Phosphorylates hsp 26 on serine residues when stimulated by tumour necrosis factor or interleukin 1 registry number: EC 2.7.1.- Synonym: hsp 27 kinase, heat-shock protein 27 kinase, hsp27 kinase ...
Heat shock transcription factors (HSFs) are stress-responsive proteins that activate the expression of heat shock genes and are highly conserved from bakers yeast to humans. Under basal conditions, the human HSF1 protein is maintained as an inactive monomer through intramolecular interactions between two coiled-coil domains and interactions with heat shock proteins; upon environmental, pharmacological, or physiological stress, HSF1 is converted to a homotrimer that binds to its cognate DNA binding site with high affinity. To dissect regions of HSF1 that make important contributions to the stability of the monomer under unstressed conditions, we have used functional complementation in bakers yeast as a facile assay system. Whereas wild-type human HSF1 is restrained as an inactive monomer in yeast that is unable to substitute for the essential yeast HSF protein, mutations in the linker region between the DNA binding domain and the first coiled-coil allow HSF1 to homotrimerize and rescue the ...
An important goal of our work was to determine whether BiP induction occurs as a response to increased PR protein synthesis on the RER or whether plants anticipate the need for increased BiP levels via a more rapid mechanism. The fact that BiP expression is induced before β-1,3-glucanase expression does not exclude the possibility that other, unidentified PR proteins may be synthesized before BiP. However, most, if not all, abundant PR proteins have been discovered, and any unidentified PR proteins probably would not be abundant enough to impose significant ER stress. For this reason, we postulated that a feedback mechanism, such as the UPR (Shamu, 1997), is unlikely to be responsible for the rapid induction of BiP expression.. To substantiate this hypothesis, we tested whether a typical UPR, triggered by treatment with tunicamycin, would lead to systemic induction of BiP expression. The fact that this is not the case demonstrates that the UPR cannot be the systemic signal itself. However, it ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
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 ...
Heat shock proteins (HSPs) are important molecules required for ideal protein function. Extensive research on the functional properties of HSPs indicates that HSPs may be implicated in a wide range of physiological functions including immune function. In the immune system, HSPs are involved in cell proliferation, differentiation, cytokine release, and apoptosis. Therefore, the ability of the immune system, in particular immune cells, to function optimally and in unison with other physiological systems is in part dependent on signaling transduction processes, including bidirectional communication with HSPs. Regulatory T cells (Tregs) are important T cells with suppressive functions and impairments in their function have been associated with a number of autoimmune disorders. The purpose of this paper is to examine the relationship between HSPs and Tregs. The interrelationship between cells and proteins may be important in cellular functions necessary for cell survival and expansion during diseased state.
The highly conserved heat shock proteins (HSPs) are constitutively expressed and function as molecular chaperones which facilitate the synthesis and folding of proteins. They also participate in protein assembly, export, turn-over and regulation.
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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
TY - JOUR. T1 - αB-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. AU - Iwaki, T.. AU - Iwaki, A.. AU - Tateishi, J.. AU - Sakaki, Y.. AU - Goldman, J. E.. PY - 1993/12/1. Y1 - 1993/12/1. N2 - To understand the significance of the accumulation of αB-crystallin in Rosenthal fibers within astrocytes, the expression and metabolism of αB- crystallin in glioma cell lines were examined under the conditions of heat and oxidative stress, αB-crystallin mRNA was increased after both stresses, and αB-crystallin protein moved from a detergent-soluble form. In addition, Western blotting of Alexanders disease brain homogenates revealed that the 27-kd heat shock protein (HSP27), which is related to αB-crystallin, accumulates along with αB-crystallin. The presence of HSP27 in Rosenthal fibers was directly demonstrated by immunohistochemistry. Our results suggest that astrocytes in Alexanders disease may be ...
Monoclonal antibodies to the human homologue of the bacterial 65 kD heat shock protein (hsp) were used to investigate the tissue distribution of endogenous hsp 65 in normal versus rheumatoid synovial tissue, in subcutaneous nodules of patients with rheumatoid arthritis (RA) and in several instances of non-rheumatoid inflammation. A strong reactivity of the anti-hsp antibody was found in the cartilage-pannus junction in rheumatoid joints and in rheumatoid nodules, but not in normal joints or in normal or inflamed kidney or liver (irreversible graft rejection, chronic glomerulonephritis or primary biliary cirrhosis). The findings provide a new hypothetical explanation for a role of T cells reactive with the 65 kD hsp in the generation of both articular and extra-articular lesions in chronic rheumatoid arthritis.
article{c39ed0c6-71b3-44bd-ae7d-1c63648fa85e, abstract = {,p,The small heat shock protein (sHsp) chaperones are crucial for cell survival and can prevent aggregation of client proteins that partially unfold under destabilizing conditions. Most investigations on the chaperone activity of sHsps are based on a limited set of thermosensitive model substrate client proteins since the endogenous targets are often not known. There is a high diversity among sHsps with a single conserved β-sandwich fold domain defining the family, the α-crystallin domain, whereas the N-terminal and C-terminal regions are highly variable in length and sequence among various sHsps and conserved only within orthologues. The endogenous targets are probably also varying among various sHsps, cellular compartments, cell type and organism. Here we have investigated Hsp21, a non-metazoan sHsp expressed in the chloroplasts in green plants which experience huge environmental fluctuations not least in temperature. We describe how ...
Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a member of the tumor necrosis factor α family of cytokines that preferentially induces apoptosis in transformed cells, making it a promising cancer therapy. However, many neoplasms are resistant to TRAIL-induced apoptosis by mechanisms that are poorly understood. We demonstrate that the expression of the small heat shock protein αB-crystallin (but not other heat shock proteins or apoptosis-regulating proteins) correlates with TRAIL resistance in a panel of human cancer cell lines. Stable expression of wild-type αB-crystallin, but not a pseudophosphorylation mutant impaired in its assembly and chaperone function, protects cancer cells from TRAIL-induced caspase-3 activation and apoptosis in vitro. Furthermore, selective inhibition of αB-crystallin expression by RNA interference sensitizes cancer cells to TRAIL. In addition, wild-type αB-crystallin promotes xenograft tumor growth and inhibits TRAIL-induced apoptosis in vivo in nude
78 kda Glucose Regulated Protein (Endoplasmic Reticulum Lumenal Ca(2+) Binding Protein Grp78 or Heat Shock 70 kDa Protein 5 or Immunoglobulin Heavy Chain Binding Protein or HSPA5) - Pipeline Review, H2 2018
Toll-like receptors (TLRs) represent the innate immune systems first line of defense against invading pathogens. TLRs are germline encoded type I transmembrane proteins that recognize pathogen associated molecular patterns (PAMPs) which tend to define broad classes of pathogens. TLRs exhibit both surface and intracellular localization. This global cellular distribution of receptors facilitates detection of PAMPs expressed on the surface of foreign organisms or encapsulated within them. In the case of nucleic acid-sensing TLRs, this distribution is also a regulatory mechanism, protecting the host from harmful response to self-nucleic acids. TLR9 primarily detects microbial DNA, however, when self-DNA is in complex with HMGB1, anti-nuclear antibodies, or an ant imicrobial peptide such as LL37, it is delivered to TLR9 in endosomes and can elicit inflammatory pathology. In this dissertation, I investigated the roles that the heat shock protein gp96 and proteolytic cleavage play in regulating TLR9 ...
This proposed research project seeks to understand environmental stress-responsive gene expression mediated through Heat Shock Transcription Factor (HSF). This project will involve the following three components: 1) a study of the DNA-binding properties of HSF to different stress-responsive promoters using the electrophoretic mobility shift assay to determine the relative binding affinity, and chemical cross linking reagents to determine the multimerization state of HSF; 2) map the sites of phosphorylation on HCF in response to different cellular stress; 3) determine the importance of the phosphorylation of HCF in regulating stress-responsive gene expression in vivo by constructing site directed mutations in the HCF phosphorylation sites and replacing the endogenous copy of HCF with each mutated HCF. Cells expressing the mutationally altered HCF molecules will be tested for their ability to activate CUP transcription in response to heat and oxidative stress. For the first research goal, DNA ...
Parallel experiments in living cells and in vitro were undertaken to characterize the mechanism by which misfolded and unassembled glycoproteins are retained in the ER. A thermoreversible folding mutant of vesicular stomatitis virus (VSV) G protein called ts045 was analyzed. At 39 degrees C, newly synthesized G failed to fold correctly according to several criteria: intrachain disulfide bonds were incomplete; the B2 epitope was absent; and the protein was associated with immunoglobulin heavy chain binding protein (BiP), a heat shock-related, ER protein. When the temperature was lowered to 32 degrees C, these properties were reversed, and the protein was transported to the cell surface. Upon the shift up from 32 degrees C back to 39 degrees C, G protein in the ER returned to the misfolded form and was retained, while the protein that had reached a pre-Golgi compartment or beyond was thermostable and remained transport competent. The misfolding reaction could be reconstituted in a cell free system ...
In the present study we demonstrated that arginine induced acute pancreatitis resulted in early disruption of the cytoskeleton with dramatic changes in both actin and intermediate filament organisation without a loss of total actin. Arginine pancreatitis was also accompanied by an increase in multiple stress heat shock proteins with large increases in HSP27 and HSP70 which were localised to acinar cells. We also observed an increase in HSP27 phosphorylation.. The histological alterations observed in response to 4.5 g/kg arginine were very similar to previous reports in which acute pancreatitis was induced by 5.0 g/kg6 or 4.5 g/kg19 arginine in male Wistar rats, while 2.5 g/kg arginine was reported to cause less severe pancreatic damage.6 Our results with 3.0 g/kg arginine also showed that general acinar structure was preserved at 24 hours, and that the majority of the pancreas contained normal appearing acini at 72 hours. Thus the extent of arginine induced pancreatitis depended on its dose. ...
Toward demonstrating functional significance for the transmembrane and/or cytoplasmic portions of MICA, we generated a transfectant of Daudi expressing a truncated form of MICA in which the cysteine at position 331 was replaced with a stop codon (Daudi/Class I+/MICA/C331*). The level of cell surface staining of this transfectant with a MICA mAb was similar to that of wild-type MICA in Daudi/Class I+/MICA (Fig. 4, b and c). We tested the susceptibility of these transfectants to NK cell cytotoxicity (Fig. 4 d). A peripheral blood NK cell line was efficiently able to kill untransfected Daudi, which lacks endogenous expression of MHC class I protein, but was inhibited from killing Daudi-expressing MHC class I protein (Daudi/Class I+). In agreement with previous data (5), Daudi-expressing MHC class I protein and MICA was efficiently killed, demonstrating how activation via NKG2D recognition can overcome inhibitory signaling. However, Daudi transfectants expressing MHC class I protein and the ...
Exposure of cells to environmental or chemical stressors will initiate the heat shock response, which is mediated by heat shock proteins. Heat shock proteins are molecular chaperones which are classified by size into six main families: HSP100, HSP90, HSP70, HSP60, HSP40 and the small heat shock proteins (sHsps). The sHsp family members bind to denatured proteins and maintain them in a folding competent state such that they may be refolded by other molecular chaperones. ,br /,,br /, The present study examined the expression and function of two amphibian sHsps, namely, ,em,Rana catesbeiana,/em, HSP30 and ,em,Xenopus laevis,/em, HSP27. Initially, an antisense riboprobe was produced to study the mRNA accumulation of ,em,Rana hsp30,/em, in cultured tongue fibroblast (FT) cells. Results showed that ,em,Rana hsp30,/em, mRNA was optimally induced when maintained at 35°C for 2 h. An antibody to the recombinant ,em,Rana,/em, HSP30 protein was also produced in order to study HSP30 protein accumulation ...
Molecular chaperones are required to maintain the proteome in a folded and functional state. When challenges to intracellular folding occur, the heat shock response is triggered, leading to increased synthesis of a class of inducible chaperones known as heat shock proteins (HSP). Although HSP synthesis is known to undergo a general decline with aging, the extent of this process varies quite markedly in some of the diseases associated with advanced age. In Alzheimers disease (AD), a prevalent protein folding disorder in the brain, the heat shock response of some critical classes of neurons becomes reduced. The resulting decline in HSP expression may be a consequence of the general enfeeblement of many aspects of cell physiology with aging and / or a response to the pathological changes in metabolism observed specifically in AD. Cancer cells, in contrast to normal aging cells, undergo de novo increases in HSP levels. This expansion in HSP expression has been attributed to increases in folding demand in
Cells are subjected to frequent assaults either from their environment or as a consequence of development or disease. Such stresses - which can be caused by a range of conditions, including changes in temperature and mechanical stresses - are damaging to proteins, so cells mount the so-called heat shock response. This response is an evolutionarily conserved transcriptional program that is orchestrated in eukaryotic cells by a protein called Hsf1 (short for heat shock factor 1; Morimoto, 1998). Three copies of this protein combine to form trimers that bind to the promoters of Hsf1-dependent genes, which leads to higher levels of heat shock proteins inside the cell. These proteins include the chaperones that refold misfolded proteins or target them for degradation. Once the effects of the stress have been dealt with, cells reduce the production of heat shock proteins to normal levels.. The heat shock response has been studied for more than 30 years, mainly in yeast and animal cells, and different ...
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 ...
TY - JOUR. T1 - Expression of heat shock protein 70 decreases with age in hepatocytes and splenocytes from female rats. AU - Gutsmann-Conrad, Astrid. AU - Pahlavani, Mohammad A.. AU - Heydari, Ahmad R.. AU - Richardson, Arlan. PY - 1999/3/15. Y1 - 1999/3/15. N2 - A decline in the induction of heat shock protein 70 (hsp70) expression with age has been shown to occur in a variety of tissues from male rodents. Because the age-related change in the expression of many genes often differ in male and female rodents, we have measured the induction of hsp70 expression in hepatocytes and splenocytes from young/adult (4-8 months) and old (20-22 months) female Fischer 344 rats. Hepatocytes and splenocytes isolated from old female rats showed a marked decrease in the induction of hsp70 mRNA and protein levels by heat shock when compared to hepatocytes and splenocytes isolated from young/adult female rats. Because the heat shock transcription factor HSF1 mediates the heat-induced transcription of hsp70, the ...
Effect of long term heat stress and dietary restriction on the expression of small heat shock protein sHSP genes in rat liver tissue ...
Recombinant Human Heat shock protein beta-7 is produced by our E.coli expression system and the target gene encoding Met1-Ile170 is expressed with a 6His tag at the C-terminus. Bon Opus Cat. #CG80
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 ...
In this study, we used co-IP and mass spectrometry to identify GEP binding partner from the membrane-enriched protein fraction of HCC cells. We have identified GRP78 as a binding partner of GEP in Hep3B (Table 1) and validated this interaction in another HCC cell line HepG2 (Fig. 2). GRP78 has been shown to present multifaceted subcellular positions and plays different physiological roles in different subcellular locations. Most GRP78 is retained in the ER, where it regulates unfolded protein response (UPR) by releasing ER stress transducers, PRKR-like ER kinase (PERK), inositol-requiring enzyme 1 (IRE1) and activating transcription factor 6 (ATF6), when unfolded proteins accumulate [26]. GRP78 is redistributed to mitochondria upon ER-stress, where it interacts with Raf-1 to maintain the mitochondrial permeability and inhibit ER-stress-induced apoptosis [27]. Accumulating evidence demonstrated the re-localization of GRP78 to plasma membrane, especially in the cancer cells that are under stress ...
The eusocial Hymenoptera have radiated across a wide range of thermal environments, exposing them to significant physiological stressors. We reconstructed the evolutionary history of three families of Heat Shock Proteins (Hsp90, Hsp70, Hsp40), the primary molecular chaperones protecting against thermal damage, across 12 Hymenopteran species and four other insect orders. We also predicted and tested for thermal inducibility of eight Hsps from the presence of cis-regulatory heat shock elements (HSEs). We tested whether Hsp induction patterns in ants were associated with different thermal environments. We found evidence for duplications, losses, and cis-regulatory changes in two of the three gene families. One member of the Hsp90 gene family, hsp83, duplicated basally in the Hymenoptera, with shifts in HSE motifs in the novel copy. Both copies were retained in bees, but ants retained only the novel HSE copy. For Hsp70, Hymenoptera lack the primary heat-inducible orthologue from Drosophila melanogaster and
TY - JOUR. T1 - Thermal preconditioning and heat-shock protein 72 preserve synaptic transmission during thermal stress.. AU - Kelty, Jonathan D.. AU - Noseworthy, Peter A.. AU - Feder, Martin E.. AU - Robertson, R. Meldrum. AU - Ramirez, Jan Marino. PY - 2002/1/1. Y1 - 2002/1/1. N2 - As with other tissues, exposing the mammalian CNS to nonlethal heat stress (i.e., thermal preconditioning) increases levels of heat-shock proteins (Hsps) such as Hsp70 and enhances the viability of neurons under subsequent stress. Using a medullary slice preparation from a neonatal mouse, including the site of the neural network that generates respiratory rhythm (the pre-Bötzinger complex), we show that thermal preconditioning has an additional fundamental effect, protection of synaptic function. Relative to 30 degrees C baseline, initial thermal stress (40 degrees C) greatly increased the frequency of synaptic currents recorded without pharmacological manipulation by approximately 17-fold (p , 0.01) and of ...
Any of a group of proteins in living cells that assist newly synthesized or denatured proteins to fold into their functional three-dimensional structures. The chaperones bind to the protein and prevent improper interactions within the polypeptide chain, so that it assumes the correct folded orientation. This process may require energy in the form of ATP. Other functions include assisting the translocation of proteins across the membranes of cell organelles and binding denatured proteins under stress conditions or in degenerative disease. There are several unrelated families of chaperones, including five classes of heat-shock proteins - HSP25 (small heat-shock proteins), HSP60, HSP70, HSP90, and HSP100 - chaperonins, calnexin, and calreticulin. ...
TY - JOUR. T1 - Heat shock-induced activation of stress MAP kinase is regulated by threonine-and tyrosine-specific phosphatases. AU - Nguyen, Aaron Ngocky. AU - Shiozaki, Kazuhiro. PY - 1999/7/1. Y1 - 1999/7/1. N2 - In eukaryotic species from yeast to human, stress-activated protein kinases (SAPKs), members of a MAP kinase (MAPK) subfamily, regulate the transcriptional response to various environmental stress. It is poorly understood how diverse forms of stress are sensed and transmitted to SAPKs. Here, we report the heat shock regulation of the fission yeast Spc1 SAPK, a homolog of human p38 and budding yeast Hog1p. Although osmostress and oxidative stress induce strong activation of the Wis1 MAPK kinase (MEK), which activates Spc1 through Thr-171/Tyr-173 phosphorylation, activation of Wis1 upon heat shock is relatively weak and transient. However, in heat- shocked cells, Pyp1, the major tyrosine phosphatase that dephosphorylates and inactivates Spc1, is inhibited for its interaction with Spc1, ...
In the present study, we demonstrated that stretch initiated the heat-shock response in rat hearts by activating HSF1, and this was followed by an increase in HSP72 mRNA. The intensity of HSF activation correlated with the amount of stretch, suggesting that the magnitude of stretch influences the degree of HSF1 activation. HSF1 activation was blocked by gadolinium, but not by diltiazem, which indicates that the stretch-induced heat-shock response was mediated by SACs. An alternative perfusion system, the working heart, was used to determine whether perfusion alone was sufficient to activate HSF. Perfusion in the working mode, which is closer to physiological perfusion and does not use an apical drain or ventricular balloon, did not activate HSF; however, HSF could be activated by increasing afterload (aortic stenosis), which effectively added an acute stretch.. Mechanical stresses, such as hemodynamic overload or mechanical stretch, alter the protein expression pattern in cardiac and skeletal ...
The sequence of heat shock-induced perturbations in protein synthesis and cytoskeletal organization was investigated in primary cultures of mouse mammary epithelial cells (MMEC). Exposure of the cells to 45 degrees C for 15 min caused a marked inhibition of protein synthesis through 2 h after heart. Resumption of protein synthesis began by 4 h, was complete by 8 h, and was accompanied by induction of four major heat shock proteins (HSPs) of 68, 70, 89, and 110 kD. Fluorescent cytochemistry studies indicated that heat shock elicited a reversible change in the organization of keratin filaments (KFs) and actin filaments but had a negligible effect on microtubules. Changes in the organization of KFs progressed gradually with maximal retraction and collapse into the perinuclear zone occurring at 1-2 h after heat followed by restoration to the fully extended state at 8 h. In contrast, actin filaments disappeared immediately after heat treatment and then rapidly returned within 30-60 min to their ...
Heat Shock Protein 22, human recombinant protein, HSPB8 H11 HMN2 CMT2L DHMN2, E2IG1, HMN2A, HSP22, Heat shock protein β-8, α-crystallin C chain, Smal validated in (PBV10440r-10), Abgent
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.. ...
Metabolic stress, characterized by a depletion of cellular ATP, has been proposed to be an important component of the trigger that induces stress protein synthesis. A reduction in ATP is thought to cause the HSF to bind to the heat shock element in the promoter region of the heat shock gene, thereby inducing the heat shock response (3, 28, 29). We have shown that heat shock alone has no significant effect on ATP concentrations but induces increased gene transcription of the major stress protein, HSP70, in rainbow trout red blood cells (Figs. 2 and3). Although HSP30 mRNA also increased after heat shock, the increase was not statistically significant, which may be attributed to the high variability associated with these data. Despite the maintenance of ATP levels after heat shock, however, there is a significant decline in ATP/ADP (Fig. 1 A). This decrease is indicative of an increase in ADP that accelerates energy turnover and equilibrates ATP production with ATP consumption. Therefore, a ...
TY - JOUR. T1 - Heat Shock Protein 90 Is Important for Sp1 Stability during Mitosis. AU - Wang, Shao An. AU - Chuang, Jian Ying. AU - Yeh, Shiu Hwa. AU - Wang, Yi Ting. AU - Liu, Yi Wen. AU - Chang, Wen Chang. AU - Hung, Jan Jong. PY - 2009/4/17. Y1 - 2009/4/17. N2 - Our previous study has revealed that heat shock protein (Hsp) 90 can interact with Sp1 to regulate the transcriptional activity of 12(S)-lipoxygenase. Herein, we further found that the interaction between Hsp90 and Sp1 occurred during mitosis. By geldanamycin (GA) treatment and knockdown of Hsp90, we found that this interaction during mitosis was involved in the maintenance of Sp1 stability, and that the phospho-c-Jun N-terminal kinase (JNK)-1 level also decreased. As the JNK-1 was knocked down by the shRNA of JNK-1, Sp1 was degraded through a ubiquitin-dependent proteasome pathway. In addition, for mutation of the JNK-1 phosphorylated residues of Sp1, namely, Sp1(T278/739A) and Sp1(T278/739D), the effect of GA on Sp1 stability was ...
There are many reports in the literature on the influence of oxidative stress during physical activity on the development of the inflammatory response and the resulting induction of HSP synthesis [5,18,19]. Under conditions of physical effort, the overexpression of genes encoding for HSP helps cells survive by protecting them from apoptosis. Morton et al. [22] claimed that the overexpression of HSP genes occurs after crossing a critical threshold, which is determined by individual difference in HSP expression propensity, training level, and also ROS levels. Evidence suggests that the level of HSP gene expression may indicate stress on the organism [5,18,19]; however, it is difficult to interpret changes in HSP gene expression. An increase in expression may indicate a high level of exposure to a stressor and that the critical threshold has been crossed. However, a decrease in the expression of these genes may reduce the organisms ability to tolerate stress [22].. Lui et al. [5], Tauler et al. ...
From NCBI Gene:. Heat-shock transcription factors (HSFs) activate heat-shock response genes under conditions of heat or other stresses. HSF4 lacks the carboxyl-terminal hydrophobic repeat which is shared among all vertebrate HSFs and has been suggested to be involved in the negative regulation of DNA binding activity. Two alternatively spliced transcripts encoding distinct isoforms and possessing different transcriptional activity have been described. [provided by RefSeq, Jul 2008]. From UniProt: ...
Exper Geront 2003; 38:1037-1040 Chaperone function plays a key role in sequestering damaged proteins and in repairing proteotoxic damage. Chaperones are induced by environmental stress and are called as stress or heat shock proteins. Here, we summarize the current knowledge about protein damage in aged organisms, about changes in proteolytic degradation, chaperone expression and function in the aging process, as well as the involvement of chaperones in longevity and cellular senescence. The role of chaperones in aging diseases, such as in Alzheimers disease, Parkinsons disease, Huntingtons disease and in other neurodegenerative diseases as well as in atherosclerosis and in cancer is discussed. We also describe how the balance between chaperone requirement and availability becomes disturbed in aged organisms, or in other words, how chaperone overload develops. The consequences of chaperone overload are also outlined together with several new research ...
OBJECTIVES: We examined the distribution of metallothionein (MT), a stress-inducible protein, and the cardiomyocyte diameter in human hearts after left-ventricular assist device (LVAD) support. BACKGROUND: Remodeling in end-stage heart failure is cha
A family of 10 thermoresistant cell lines cloned from Chinese hamster cells transfected with a plasmid containing the structural gene for the small human Mr 27,000 heat shock protein (HSP27) was used to assess the putative role of this heat shock protein in chemoresistance. These cells express varying amounts of human HSP27 in addition to the normal level of endogenous hamster HSP27. As previously observed in the case of thermoresistance, a significant positive linear correlation (P , 0.05) was found between cell survival in response to doxorubicin and the total amount of HSP27 expressed. Some clones were also examined for resistance to other drugs and chemicals. A statistically significant increased survival relative to the parental cells was observed following treatment with daunorubicin (three clones studied), colchicine, vincristine, actinomycin D, hydrogen peroxide, and sodium arsenite (one clone studied). However, the clone which expressed the highest level of HSP27 was as sensitive as ...
In biochemistry, heat shock is the effect of subjecting a cell to a temperature that is greater than the optimal temperature range of function of the cell. Heat shock refers to cellular exposure to rapid stress changes such as temperature, toxins, oxidative stress, heavy metals, and pathogenic infections. Specifically temperature induced heat shock, even of a few degrees, has the potential to disrupt proper protein folding. As a result, proteins can fold incorrectly, or become entangled which can results in nonspecific aggregation. Other cellular damages induced by heat shock include cytoskeletal rearrangement, changes in organelle localization, decrease in ATP production, unsafe drop in cellular pH levels, decreased translation of proteins, and changes in RNA splicing. Introduction of heat shock to cells elicits the molecular response, the heat shock response (HSR), which repairs damages caused by stressors such as protein misfolding and protein aggregation. The cellular response to heat shock ...
The major focus of this laboratory is on exercise-induced changes in cardiac and vascular function related to changes in molecular mechanisms regulating heat shock proteins and nitric oxide synthases. Physical inactivity (as with hypertension, smoking, and high cholesterol) is a major risk factor for coronary heart disease and the most prevalent of the four. Although exercise has been shown to provide a protective effect against high blood pressure and the development of atherosclerosis, the mechanism of this effect is unknown. In addition, while it is apparent that both nitric oxide synthases (NOS) and stress proteins play an important role in cardioprotection and vascular function, little is known about exercise-induced changes in NOS and/or stress protein expression in the vasculature. Using models of exercise and various disease states, this laboratory can evaluate exercise-induced changes in gene and protein expression in the cardiovascular system and examine their role in preventing ...
The heat shock protein response appears to be triggered primarily by nonnative proteins accumulating in a stressed cell and results in increased expression of heat shock proteins (HSPs). Many heat sho
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Several neuroinflammatory disorders are known or suspected to involve autoimmunity. Practically all proteomic studies of MP/exosomes detect substantial amounts of IgG, IgM, and complement (C) fragments on MP. It has long been known that MP-associated antibody-antigen (Ab:Ag) complexes (IC) are released on MP by the action of C. Recently, it was shown that MP-IC exert significant neuroinflammatory action [42]. The cause of shedding of IC from cell surfaces is often C-mediated attack on the opsonized cells, resulting in the release of Ab/Ag/C complex MP. A specific protein, mortalin, has been identified as instrumental in this process [71]. Mortalin belongs to the HSP family (stress chaperones) and has been implicated in Parkinsons disease (PD) [72]. Additional related references are given in the review by Robbins et al. [73], covering also cytokines on MP and their surface expression of PAMPs/DAMPs (pathogen-associated molecular patterns and danger-associated molecular patterns), which ...
αB-Crystallin (αB) and HSP27 belong to the class of small Heat Shock Proteins (sHSPs) whose levels of expression increase under conditions of cellular stress, viz., heat, pH, and ischemia. sHSPs form an integral part of the cellular chaperone network by maintaining aggregation-prone proteins in a soluble state. Due to their tendency to form large oligomeric structures, human small heat shock factors have been refractory to structural studies. We are using a combination of solution-state and solid-state NMR approaches to define the structures of dimeric constructs and of large oligomers. Although the full extent of the functions of αB-Crystallin (αB) and HSP27 remain to be determined, the proteins are each implicated in certain inherited forms of dystrophies and αB is also implicated in breast and other forms of cancer.. The PhoQ/PhoP two-component regulatory system plays a critical role in bacterial virulence. PhoQ is a sensor kinase that is capable of sensing the environment in which the ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
ATGen operates in the Commercial Physical Research sector. ATGen is a Korea-based company principally engaged in developing and manufacturing reagent used for experimentation . The Companys product portfolio consists of recombination proteins including binding immunoglobulin protein, carboxy terminus of HSP70 interacting protein, BCL2-associated athanogene 2; monoclonal antibodies including 14-3-3 beta antibody, A crystallin A antibody , alpha-crystallin B and NK Vue Kit used for physical examination and diagnosis. The Company distributes its products within domestic market and to overseas markets.
You searched for: Author Coleman, J.S. Remove constraint Author: Coleman, J.S. Journal Oecologia Remove constraint Journal: Oecologia Subject Zea mays Remove constraint Subject: Zea mays Subject heat shock proteins Remove constraint Subject: heat shock proteins Text Availability Citation in PubAg Remove constraint Text Availability: Citation in PubAg ...
Heat shock factor 1 (HSF1) is a protein that in humans is encoded by the HSF1 gene. HSF1 is highly conserved in eukaryotes and is the primary mediator of transcriptional responses to proteotoxic stress with important roles in non-stress regulation such as development and metabolism. Human HSF1 consists of several domains which regulate its binding and activity. This N-terminal domain of approximately 100 amino acids is the most highly conserved region in the HSF protein family and consists of a helix-turn-helix loop. The DBD of each HSF1 monomer recognizes the sequence nGAAn on target DNA. Repeated sequences of the nGAAn pentamer constitute heat shock elements (HSEs) for active HSF1 trimers to bind. The two regions responsible for oligomerization between HSF1 monomers are leucine zipper (LZ) domains 1-3 and 4 (these regions are also commonly referred to as HR-A/B and HR-C). LZ1-3 is situated just downstream of the DBD while LZ4 is located between the RD and the C-terminal TAD. Under non-stress ...
There are many similarities in the replication mechanisms employed by bacteriophage λ and its host E. coli(for reviews, see Bramhill and Kornberg, 1988, Keppel et al., 1988, and McMacken et al.,...
Tumor cell clones isolated from a rat 13762NF mammary adenocarcinoma and its spontaneous metastases were heterogeneous in their survival responses to continuous 42° heating. Clones MTLn3 and MTF7 had similar initial survival responses; they were significantly less sensitive than clone MTC. Following the first decrease in survival, different magnitudes of induced thermal resistance were observed. When ratios of the first and resistant slopes of survival curves were compared (the thermotolerance ratio), the order of induced thermal resistance was MTLn3 , MTF7 , MTC.. These clones were compared for the rates of synthesis of heat stress proteins (HSP). The same four major HSP at Mr 112,000, 90,000, 70,000, and 22,000 were induced or enhanced in all 3 clones. The rates of synthesis of these HSP were analyzed through a unique system of computer-assisted video densitometry and digitization. When all 4 HSP were analyzed as a group, the rates were significantly different (p , 0.017), and the rank order ...
Heat shock proteins[edit]. Secondary structures formed by the RBS can affect the translational efficiency of mRNA, generally ... At a higher-than-usual temperature (~42 °C), the RBS secondary structure of heat shock proteins becomes undone thus allowing ... The ribosomal protein S1 binds to adenine sequences upstream of the RBS. Increasing the concentration of adenine upstream of ... This is especially useful when multiple start codons are situated around the potential start site of the protein coding ...
Among his best-known work is his study of heat shock proteins, which he was the first to identify in vertebrate cells and on ... Schlesinger, MJ (25 July 1990). "Heat shock proteins". The Journal of Biological Chemistry. 265 (21): 12111-4. PMID 2197269. " ... known for his role in the study of heat shock proteins. Schlesinger attended Yale University as an undergraduate and received ... 1990). Stress Proteins : Induction and Function. Springer Berlin Heidelberg. ISBN 978-3-642-75817-1. Schlesinger, edited by ...
3.4) Heat shock factors. *HSF *1. *2. *4. (3.5) Tryptophan clusters. *ELF *2 ... SREB proteins are indirectly required for cholesterol biosynthesis and for uptake and fatty acid biosynthesis. These proteins ... proteins. However, in contrast to E-box-binding HLH proteins, an arginine residue is replaced with tyrosine making them capable ... SREBP precursors are retained in the ER membranes through a tight association with SCAP and a protein of the INSIG family. ...
The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a family of heat shock proteins. ... Recently, small heat shock proteins (sHSPs) were found in marine viruses (cyanophages). Hsp20, like all heat shock proteins, is ... to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins ( ... "Small heat shock protein 20 (Hsp20) facilitates nuclear import of protein kinase D 1 (PKD1) during cardiac hypertrophy". Cell ...
"Roles of Heat Shock Proteins". Scientific American. Retrieved 2018-10-28. "Wells named a fellow of National Academy of ... Hillary C.M. Nelson on the structure of Heat Shock Transcription Factor, which plays various roles as a molecular chaperone and ... and lead molecules against heat shock and multiple other cysteine proteases. Purportedly for this work, she was awarded tenure ... Her research focuses especially on caspases, apoptotic proteins involved in the regulation of cell death, and with impacts in ...
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 ... heat shock proteins protect cells when stressed by elevated temperatures. They account for 1-2% of total protein in unstressed ...
Heat shock protein beta-6 is a protein that in humans is encoded by the HSPB6 gene. HSPB6 also known as hsp20 is a 17-kDa ... "Entrez Gene: HSPB6 heat shock protein, alpha-crystallin-related, B6". Kato K, Goto S, Inaguma Y, Hasegawa K, Morishita R, Asano ... Chernik IS, Seit-Nebi AS, Marston SB, Gusev NB (2007). "Small heat shock protein Hsp20 (HspB6) as a partner of 14-3-3gamma". ... Overview of all the structural information available in the PDB for UniProt: O14558 (Heat shock protein beta-6) at the PDBe-KB ...
"Heat Shock Protein Vaccine". "HSPCC-96 Vaccine". "Acoustic Neuromas". "Pituitary Tumors". "Skull Base Tumors". Kacl, GM (1999 ...
... heat-shock proteins and regeneration in echinoderms". The Journal of Experimental Biology. 204 (Pt 5): 843-8. PMID 11171408.. ... Neural cells, for example, express growth-associated proteins, such as GAP-43, tubulin, actin, an array of novel neuropeptides ... as the venom volume is replaced before the active proteins are all replenished.[27] ...
About 65% of protein-coding genes currently lack functional assignment. Leishmania species produce several different heat shock ... revealing more than 8300 protein-coding and 900 RNA genes. Almost 40% of protein-coding genes fall into 662 families containing ... These proteins play a key role in meiosis. Thus, meiotic events provide the adaptive advantage of efficient recombinational ... L. infantum produces proteins BRCA1 and RAD51 that interact with each other to promote homologous recombinational repair. ...
"Heat Shock Proteins: How They Work (animated demonstration)". Archived from the original on January 9, 2008. Retrieved 2008-12- ... The treatment involved removing a patient's tumor cells, isolating and fortifying the cellular proteins that normally alert the ... immune system to disease, and re-injecting the proteins into the patient. In 1994, Armen co-founded Antigenics with Srivastava ...
... 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 ... Heat shock protein HSP 90-beta also called HSP90beta is a protein that in humans is encoded by the HSP90AB1 gene. HSP90AB1 is a ...
Lindquist pioneered the use of yeast as a model system to study how heat shock proteins regulate gene expression and protein ... particularly the protein folding problem[3][6] within a family of molecules known as heat-shock proteins,[7][8] and prions.[9] ... "The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins". Annual Review of ... She proposed that a heat shock protein, hsp90, may act in the same way, normally preventing phenotypic consequences of genetic ...
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). " ... Heat shock proteins Hsp70 Milner CM, Campbell RD (1990). "Structure and expression of the three MHC-linked HSP70 genes". ...
... and identified the tumor immunogenicity of heat shock proteins. Old is the author or co-author of more than 800 research ... of the p53 protein, the gene for which is mutated in approximately 50 percent of cancers (1979). Conducting of the most ...
The heat shock proteins HslV and HslU (HslVU complex; also known as ClpQ and ClpY respectively, or ClpQY) are expressed in many ... The hslV protein degrades unneeded or damaged proteins only when in complex with the hslU protein in the ATP-bound state. HslV ... "Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in ... The hslV protein is a protease and the hslU protein is an ATPase; the two form a symmetric assembly of four stacked rings, ...
Elevated expression of heat shock proteins is not correlated with chronic environmental stress and is thought to be due to the ... Heat shock proteins (HSPs) are a diverse class of molecular chaperones that assist in folding under stress. While originally ... Feder, ME; Hofmann, GE (1999). "Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological ... "The evolutionary and ecological role of heat shock proteins". Ecology Letters. 6 (11): 1025-1037. doi:10.1046/j.1461-0248.2003. ...
He specializes in the research on heat shock proteins. In 1999, he won Poland's highest scientific award, Prize of the ... Foundation for Polish Science for "research on regulatory proteins constituting part of the system protecting cells against ...
June 2002). "Nontoxic heat shock protein coinducer BRX-220 protects against acute pancreatitis in rats". Free Radic. Biol. Med ... Brown IR (October 2007). "Heat shock proteins and protection of the nervous system". Ann. N. Y. Acad. Sci. 1113: 147-58. doi: ... Kalmar B, Burnstock G, Vrbová G, Urbanics R, Csermely P, Greensmith L (July 2002). "Upregulation of heat shock proteins rescues ... a coinducer of heat shock proteins, delays disease progression in ALS mice". Nat. Med. 10 (4): 402-5. doi:10.1038/nm1021. PMID ...
As temperatures fall, production of antifreeze proteins and dehydrins increases. As temperatures rise, production of heat shock ... Heat transfer to the epidermis The rate of evaporation The rate of heat production The hypothalamus plays an important role in ... Heat stress is physiologically combated in four ways: radiation, conduction, convection, and evaporation. Cold stress is ... ISBN 978-0-521-88010-7. Long, S. P.; Ort, D. R. (2010). "More than taking the heat: Crops and global change". Current Opinion ...
The J domain interacts with Hsc70 heat-shock proteins. In many polyomavirus LTags, N-terminal to the J domain is a sequence ... The ATPase domain also contains regions responsible for protein-protein interactions with host cell proteins, most notably ... without affecting these protein-protein interaction sites. LTag is a large protein whose domains can be detected and annotated ... Polyomavirus LTag proteins contain four well-conserved, globular protein domains: from N- to C-terminus, these are the J domain ...
Before it binds with an androgen, the androgen receptor is bound to heat shock proteins. These heat shock proteins are released ... "Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, ... These misfolded AR proteins form aggregates in the cell cytoplasm and nucleus. Over the course of 30 to 50 years, these ... The human androgen receptor (AR) is a protein encoded by a gene located on the proximal long arm of the X chromosome (locus ...
Patruno M, Thorndyke MC, Candia Carnevali MD, Bonasoro F, Beesley PW (March 2001). "Growth factors, heat-shock proteins and ... Neural cells, for example, express growth-associated proteins, such as GAP-43, tubulin, actin, an array of novel neuropeptides ... as the venom volume is replaced before the active proteins are all replenished. Many annelids (segmented worms) are capable of ...
... is a heat-shock protein. It is known to reverse toxicity of mutant α-synuclein, TDP-43, FUS, and TAF15 in yeast cells. " ... "Yeast Chaperone Melts Protein Aggregates". Retrieved September 12, 2016. CS1 maint: discouraged parameter (link) ...
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 ... Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during ...
Heat shock proteins (HSPs) are present in some bacteria and serve as a "danger signal" to the immune system. However, some HSPs ... "Behçet's disease and antibody titers to various heat-shock protein 60s". Ocular Immunology and Inflammation. 7 (2): 69-74. ISSN ... "Innate and Adaptive Responses to Heat Shock Proteins in Behcet's Disease". Genetics Research International. 2013. doi:10.1155/ ... An association with the GIMAP ("GTPase of the immunity-associated protein") family of genes on the long arm of chromosome 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 ... When a cell is under stress, it naturally increases the production of stress proteins, including heat shock proteins such as ...
"Heat Shock Response" and the proteins were termed the "Heat Shock Proteins" (Hsps). The Hsp70 proteins have three major ... The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. ... "Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling". ... Giri B, Sethi V, Modi S, Garg B, Banerjee S, Saluja A, Dudeja V (July 2017). ""Heat shock protein 70 in pancreatic diseases: ...
They produce heat shock proteins (HSPs), but unlike other animals, they do this not in direct response to heat. Instead, they ... The Amazing Cataglyphis Ant, 2006-02-26, retrieved 2016-01-14 Moseley, Pope L. (1997-11-01). "Heat shock proteins and heat ... If they did not produce the proteins in anticipation of the extreme heat, they would die before the proteins could have their ... "the few minutes duration of the foraging frenzy is too short for synthesis of these protective proteins after exposure to heat ...
Kourtis N, Nikoletopoulou V, Tavernarakis N (2012). "Small heat-shock proteins protect from heat-stroke-associated ... "Small heat-shock proteins protect from heat-stroke-associated neurodegeneration". Nature. 490 (7419): 213-218. Bibcode: ... His group developed, for the first time, experimental heat stroke models; and identified mechanisms protecting against heat ... implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins". Trends in Biochemical ...
Homeobox protein Hox-D8 is a protein that in humans is encoded by the HOXD8 gene.[5][6][7] ... 3.4) Heat shock factors. *HSF *1. *2. *4. (3.5) Tryptophan clusters. *ELF *2 ... 1989). "Complementary homeo protein gradients in developing limb buds". Genes Dev. 3 (5): 641-50. doi:10.1101/gad.3.5.641. PMID ... HOXD8+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH) ...
Atromentin and leucomelone possess antibacterial activity, inhibiting the enzyme enoyl-acyl carrier protein reductase, ( ... of life turning harmless pneumococcus into a lethal form by co-inoculating the live pneumococci into a mouse along with heat- ... and Maclyn McCarty demonstrated that the transforming factor in Griffith's experiment was not protein, as was widely believed ... pneumoniae is associated with increased resistance to oxidative stress and increased expression of the RecA protein, a key ...
... which code for proteins with antiviral properties.[51] EBOV's V24 protein blocks the production of these antiviral proteins by ... Ebolaviruses can be eliminated with heat (heating for 30 to 60 minutes at 60 °C or boiling for five minutes). To disinfect ... The widespread bleeding that occurs in affected people causes swelling and shock due to loss of blood volume.[94] The ... which are then translated into structural and nonstructural proteins. The most abundant protein produced is the nucleoprotein, ...
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 ... Protein targeting and importEdit. See also: Protein targeting. The movement of so many chloroplast genes to the nucleus means ... A protein kinase drifting around on the outer chloroplast membrane can use ATP to add a phosphate group to the Toc34 protein, ...
Heat of vaporisation (kJ·mol−1) 136. 97.42. 79.1. 69. 66.1. ? Heat of formation of monatomic gas (kJ·mol−1) 162. 108. 89.6. ... The balance between potassium and sodium is maintained by ion transporter proteins in the cell membrane.[231] The cell membrane ... Nellis, W. J.; Weir, S. T.; Mitchell, A. C. (1999). "Metallization of fluid hydrogen at 140 GPa (1.4 Mbar) by shock compression ... Hence, all the alkali metals are soft and have low densities,[30] melting[30] and boiling points,[30] as well as heats of ...
Excess heat and energy production. An excess heat observation is based on an energy balance. Various sources of energy input ... It was adopted as a software product name Adobe ColdFusion and a brand of protein bars (Cold Fusion Foods).[182] It has also ... Neutron Emission from Cryogenically Cooled Metals Under Thermal Shock (self published). *^ ... There are also "heat-after-death" experiments, where the evolution of heat is monitored after the electric current is turned ...
The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins. Annual Review of ... The Heat-Shock Response. Annual Review of Biochemistry. 1986-06-01, 55 (1): 1151-1191 [2018-04-02]. ISSN 0066-4154. doi:10.1146 ...
Proteins related to the cytoskeleton components of other organisms exist in archaea,[89] and filaments form within their cells, ... 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 ... January 2002). "Introns in protein-coding genes in Archaea". FEBS Lett. 510 (1-2): 27-30. doi:10.1016/S0014-5793(01)03219-7. ...
The energy that is absorbed by the muscle will be dissipated as heat if the muscle is being used as a "damper or shock absorber ... muscle filaments or proteins) that overlaps to format a cross-bridge bond (attachment)".[1] ... If this energy is not used quickly it is dissipated as heat. The role of eccentric training is to use these principles of ... Eccentric contractions use less energy and actually absorb energy that will be used as heat or elastic recoil for the next ...
3.4)热休克因子(英语:Heat Shock Factor). HSF(1、2、4) ... Rb · RBL1(英语:Retinoblastoma-like protein 1) · RBL2(英语:Retinoblastoma-like protein 2) ... protein homodimerization activity. · sequence-specific DNA binding. · metal ion binding. · protein heterodimerization activity ... FOXP2(Forkhead box protein P2 (FOXP2))基因,即叉头框P2基因,是一个与言语功能的发育有关的基因
The FLP gene can then be induced selectively, commonly using either the heat shock promoter or the GAL4/UAS system. The ... The resulting BLM protein is defective. the defect in RecQ an helicase facilitates the defective unwinding of DNA during ... commonly the green fluorescent protein or GFP) and an allele of a gene to be studied (both on chromosomes bearing FRT sites). ...
... is upregulated by cellular stress and mediates heat shock response". Biochemical and Biophysical Research Communications. 360 ( ... positive regulation of protein kinase A signaling. • negative regulation of apoptotic process. • positive regulation of protein ... cellular response to heat. • regulation of DNA-templated transcription in response to stress. • regulation of hemopoiesis. • ... "TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer". Cancer Research. 64 (8): 2766-73. ...
ProteinEdit. Oats are the only cereal containing a globulin or legume-like protein, avenalin, as the major (80%) storage ... An early start is crucial to good fields, as oats go dormant in summer heat. In warmer areas, oats are sown in late summer or ... Oats were gathered into shocks, and then collected and run through a stationary threshing machine. ... Oat protein is nearly equivalent in quality to soy protein, which World Health Organization research has shown to be equal to ...
Known for his contributions to physics such as the Mach number and the study of shock waves.[211][212][213] ... R. L. Wysong (1976). "5: Origin of Proteins". The Creation-evolution Controversy (implications, Methodology and Survey of ... Sir John Leslie (1766-1832): Scottish mathematician and physicist best remembered for his research into heat; he was the first ... shock waves, nuclear physics, particle physics, astrophysics, physical cosmology, and general relativity.[363][364] ...
... heat shock, or oxidative damage - heat shock proteins that identify misfolded or unfolded proteins and target them for ... "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. ... The protein degradation processEdit. Ribbon diagram of ubiquitin, the highly conserved protein that serves as a molecular tag ...
Above the auger is a heat shield to disperse the direct heat before it reaches the heat box to allow the wood smoke to keep the ... Wood also contains small quantities of proteins, which contribute roasted flavors. Many of the odor compounds in wood smoke, ... The heat sensor inside the heat box relays the current temperature inside the box back to the temperature regulator which then ... The primary differences are the sources of heat and of the smoke. In a propane smoker, the heat is generated by a gas burner ...
The discovery was part of a continuing study on circulatory shock and proteolytic enzymes related to the toxicology of snake ... Bradykinin is a physiologically and pharmacologically active peptide of the kinin group of proteins, consisting of nine amino ... The kinin B1 and B2 receptors belong to G protein coupled receptor (GPCR) family. ... of bradykinin has led to a new understanding of many physiological and pathological phenomena including circulatory shock ...
protein binding. • protease binding. • tumor necrosis factor receptor binding. • cytokine activity. • identical protein binding ... Clark IA (July 1982). "Suggested importance of monokines in pathophysiology of endotoxin shock and malaria". Klin. Wochenschr. ... A local increase in concentration of TNF will cause the cardinal signs of Inflammation to occur: heat, swelling, redness, pain ... positive regulation of protein complex assembly. • protein kinase B signaling. • positive regulation of cytokine production. • ...
"Root shock: The consequences of African American dispossession" Journal of Urban Health. Springer, New York. Volume 78, Number ... some women prefer straightening of the hair through the application of heat or chemical processes.[70] Although this can be a ... and emphasizing the consumption of more fruits and vegetables than animal protein. There is some resistance to such changes, ...
These include the heat shock proteins (Hsp70s) and fatty acid binding proteins for anandamide (FABPs).[6][7] FABPs such as ... 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- ... protein transporters have been described that act as carriers to solubilize and transport the endocannabinoids through the ...
... proteins and their genes must be co-located for redox regulation according to the CoRR hypothesis for the function of DNA ... The word reduction originally referred to the loss in weight upon heating a metallic ore such as a metal oxide to extract the ... An abnormal redox state can develop in a variety of deleterious situations, such as hypoxia, shock, and sepsis. Redox mechanism ... and heat energy. Complete oxidation of materials containing carbon produces carbon dioxide. ...
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 ... Protein targeting and import[edit]. See also: Protein targeting. The movement of so many chloroplast genes to the nucleus means ... Protein synthesis[edit]. See also: Transcription and translation. Protein synthesis within chloroplasts relies on an RNA ...
... which result in either diminished levels of the C1-inhibitor protein (type I HAE) or dysfunctional forms of the same protein ( ... Heat syncope. Reduced. Hypothermia. Immersion foot syndromes Trench foot. Tropical immersion foot. Warm water immersion foot. ... activates other proteins of the complement system. Additionally, it inhibits various proteins of the coagulation cascade, ... type II HAE). Type III HAE has been linked with mutations in the F12 gene, which encodes the coagulation protein factor XII. ...
It reacts with proteins in the skin to give a dark brown color that may last as long as a month. ... Dry picric acid is relatively sensitive to shock and friction, so laboratories that use it store it in bottles under a layer of ... When glucose, picric acid and sodium carbonate are combined and heated, a characteristic red color forms. With a calibrating ... Picric acid was the first high explosive nitrated organic compound widely considered suitable to withstand the shock of firing ...
However, hypochlorite bleaches in low concentration were found to also attack bacteria by interfering with heat shock proteins ... They irreversibly denature or destroy many proteins, making them extremely versatile disinfectants. ... "Bleach Activates A Redox-Regulated Chaperone by Oxidative Protein Unfolding". Cell. 135 (4): 691-701. doi:10.1016/j.cell. ...
"Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate". The Journal of ... 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 ... Neupert W (1997). "Protein import into mitochondria". Annual Review of Biochemistry. 66: 863-917. doi:10.1146/annurev.biochem. ...
In Tamil Nadu and Andhra Pradesh, sesame oil is used as a preservative, as well as to temper the heat of their spicy foods, ... The byproduct that remains after oil extraction from sesame seeds, also called sesame oil meal, is rich in protein (35-50%) and ... shock with drop of blood pressure. In the systemic reactions can also be included severe reactions like dizziness, drowsiness, ... In most parts of the country, sesame seeds mixed with heated jaggery, sugar, or palm sugar is made into balls and bars similar ...
In order to aid in neurotransmission, GAD65 forms a complex with Heat Shock Cognate 70 (HSC70), cysteine string protein (CSP) ... Wei J, Davis KM, Wu H, Wu JY (May 2004). "Protein phosphorylation of human brain glutamic acid decarboxylase (GAD)65 and GAD67 ... protein kinase C (PKC). Both GAD67 and GAD65 are also regulated post-translationally by Pyridoxal 5'-phosphate (PLP); GAD is ... GAD67 is phosphorylated at threonine 91 by protein kinase A (PKA), while GAD65 is phosphorylated, and therefore regulated by, ...
heat shock protein binding. • receptor binding. Cellular component. • cytosol. • blood microparticle. • endoplasmic reticulum ... cellular protein metabolic process. • transport. • positive regulation of phagocytosis. • protein stabilization. Sources:Amigo ... protein binding. • protein heterodimerization activity. • phosphatidylcholine-sterol O-acyltransferase activator activity. • ... Click on genes, proteins and metabolites below to link to respective articles. [§ 1] ...
Heat-Shock Proteins, SmallHSP20 Heat-Shock ProteinsHSP27 Heat-Shock ProteinsHSP30 Heat-Shock ProteinsHSP40 Heat-Shock Proteins ... HSP47 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSC70 Heat-Shock ProteinsHSP110 Heat-Shock ProteinsHSP72 Heat-Shock Proteins ... and ProteinsProteinsMolecular ChaperonesHeat-Shock ProteinsChaperoninsGroup I Chaperonins +Group II Chaperonins + ... Heat-Shock Proteins. Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other ...
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 ... The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat ...
Heat shock proteins (HSPs) chaperone other cellular proteins, guarding them from going astray, folding improperly or ... Heat shock proteins, primarily members of the HSP90 and HSP70 families, participate in sounding the alarm and identifying the ... HSP90 receives folded proteins from other chaperones and helps to join them into a larger protein structure, such as a cellular ... When a cell is cancerous or infected by a pathogen, it generates proteins not found in normal cells. Fragments of such proteins ...
Source for information on heat-shock protein: A Dictionary of Biology dictionary. ... protecting the cells proteins as they become unfolded due to heating and enabling them to refold correctly. ... Any of various proteins that are synthesized by living cells in response to increased temperature. They occur in both ... is regarded as a heat-shock protein and acts as a marker for proteins destined for degradation. Many of the heat-shock proteins ...
Heat Shock Proteins and Chaperones RT2 Profiler PCR Array The Human Heat Shock Proteins & Chaperones RT² Profiler PCR Array ... Heat Shock Proteins and Chaperones RT2 Profiler PCR Array The Mouse Heat Shock Proteins & Chaperones RT² Profiler PCR Array ... Heat Shock Proteins and Chaperones RT2 Profiler PCR Array The Rat Heat Shock Proteins & Chaperones RT² Profiler PCR Array ... profiles the expression of 84 Heat Shock Protein genes that regulate protein folding. Heat shock proteins (HSPs, or molecular ...
... S. Tabibzadeh and J. Broome ... Human endometrium expresses a molecular repertoire which includes the heat shock proteins (Hsps) Hsp27, Hsp60, Hsp70, Hsp90, ... In view of known functions of the Hsps, it is likely that these proteins are involved in protection of the endometrial proteins ... against factors with the potential to lead to protein denaturation. Tumor necrosis factor-α (TNF-α) is a cytotoxic cytokine ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... found in heat shock protein beta-3 (HspB3) from vertebrates, also known as heat-shock protein 27-like protein (HSPL27, 17 kDa ... Small heat shock proteins (sHSP) are molecular chaperones that suppress protein aggregation and protect against cell stress, ...
This gives Hsp15 a very different functional role from all other heat shock proteins and points to a new aspect of translation. ... Hsp15: a ribosome-associated heat shock protein.. Korber P1, Stahl JM, Nierhaus KH, Bardwell JC. ... While only a part of the Hsp15 pool is found in the 50S peak before heat shock (for the extreme example of no binding at all ... We are analyzing highly conserved heat shock genes of unknown or unclear function with the aim of determining their cellular ...
Heat shock protein 60 and the regulation of autoimmunity. In: van Eden W, Young DB, eds. Stress Proteins in Medicine. New York ... Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. J ... Regulation of heat shock gene transcription by a family of heat shock factors. In: Morimoto RI, Tissières A, Georgopoulos C, ... Heat shock protein studies in type 1 and type 2 diabetes and human islet cell culture. Diabetic Med. 1995; 12: 595-599. ...
Jetzt Chaperokine Activity of Heat Shock Proteins versandkostenfrei online kaufen bei, Ihrem Bücher-Spezialisten! ... Heat Shock Proteins: Chaperokine Activity of Heat Shock Proteins (eBook / PDF)Download bestellen ... Chaperokine Activity of Heat Shock Proteins ". Klappentext zu „Chaperokine Activity of Heat Shock Proteins ". Chaperokine, is a ... Heat Shock Proteins provides the most comprehensive review on contemporary knowledge on the chaperokine activity of heat shock ...
Heat shock proteins and cytoprotection : ATP-deprived mammalian cells. [Alexander E Kabakov; Vladimir L Gabai] ... shock_proteins_physiology> # Heat-Shock Proteins--physiology. a schema:Intangible ;. schema:name "Heat-Shock Proteins-- ... 5. Heat Shock Proteins and Cardioresistance to Ischemia --. 6. Involvement of Heat Shock Proteins in Protection of Various ... Heat shock proteins--Physiological effect. a schema:Intangible ;. schema:name "Heat shock proteins--Physiological effect"@en ; ...
Molecular chaperones or heat shock proteins are involved in diverse biological processes and play an important role in ... Heat Shock Proteins as Targets for Novel Anti-Malarial Drugs. In: Shonhai A., Blatch G. (eds) Heat Shock Proteins of Malaria. ... Overall, heat shock protein inhibitors not only provide us with a new avenue to tackle malaria but also shed light on novel ... Hence, heat shock proteins serve as potential drug targets against malaria. The emergence of drug resistance in Plasmodium ...
Heat Shock Protein Inhibitors. Book Subtitle. Success Stories. Editors. * Shelli R. McAlpine ... Heat Shock Protein Inhibitors. Success Stories. Editors: McAlpine, Shelli R., Edkins, Adrienne Lesley (Eds.) ...
"The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones," Essays in Biochemistry, vol ... A. Nakai and R. I. Morimoto, "Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, ... A. Mathew and R. I. Morimoto, "Role of the heat-shock response in the life and death of proteins," Annals of the New York ... F. C. Neidhardt, R. A. VanBogelen, and V. Vaughn, "The genetics and regulation of heat-shock proteins," Annual Review of ...
Heat shock protein hsp90 regulates dioxin receptor function in vivo. M L Whitelaw, J McGuire, D Picard, J A Gustafsson, L ... Heat shock protein hsp90 regulates dioxin receptor function in vivo. M L Whitelaw, J McGuire, D Picard, J A Gustafsson, L ... Heat shock protein hsp90 regulates dioxin receptor function in vivo. M L Whitelaw, J McGuire, D Picard, J A Gustafsson, and L ... Heat shock protein hsp90 regulates dioxin receptor function in vivo Message Subject (Your Name) has sent you a message from ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Small heat shock proteins (sHsps) are molecular chaperones that suppress protein aggregation and protect against cell stress, ... Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy.. Nat. ...
It has been shown to self-assemble into oligomers upon heat shock or divalent cations treatment, but the functional role of the ... Background The human 90-kDa heat shock protein (HSP90) functions as a dimeric molecular chaperone. HSP90 identified on the cell ... Heat shock response Is the Subject Area "Heat shock response" applicable to this article? Yes. No. ... Protein structure Is the Subject Area "Protein structure" applicable to this article? Yes. No. ...
2004) Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes. J ... Small Heat Shock Proteins (sHSPs) are one of the least well understood classes of molecular chaperones, proteins which act to ... Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein aggregation by binding ... 2002) Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. Adv Protein Chem 59: ...
Heat shock proteins (HSPs) are primordial and abundant molecules expressed in all cells. Publications starting in 1984 have ... Immunotherapy for human cancer using heat shock protein-peptide complexes Curr Oncol Rep. 2005 Mar;7(2):104-8. doi: 10.1007/ ... Heat shock proteins (HSPs) are primordial and abundant molecules expressed in all cells. Publications starting in 1984 have ...
Heat shock protein HSP 90-alpha. A. 238. Homo sapiens. Mutation(s): 0 Gene Names: HSP90AA1, HSP90A, HSPC1, HSPCA. ... Structure of Heat Shock Protein 90 Bound to CS320. Kang, Y.N., Stuckey, J.A.. To be published. ...
Parsell, D.A. & Lindquist, S. (1994). Heat shock proteins and stress tolerance. In: The Biology of Heat Shock Proteins and ... The heat-shock response and expression of heat-shock proteins in wheat under diurnal heat stress and field conditions. Aust. J ... Heat shock proteins as antigens in immunity against infection and self. In: The Biology of Heat Shock Proteins and Molecular ... A purine-type heat shock protein 90 inhibitor promotes the heat shock response in Arabidopsis , Plant Biotechnology Reports, ...
RecName: Full=Heat shock protein 75 kDa, mitochondrial; Short=HSP 75; AltName: F... RecName: Full=Heat shock protein 75 kDa, ... RecName: Full=Heat shock protein 75 kDa, mitochondrial; Short=HSP 75; AltName: Full=TNFR-associated protein 1; AltName: Full= ... This gene encodes a mitochondrial chaperone protein that is member of the heat shock protein 90 (HSP90) family. The encoded ... and heat production by uncoupling proteins. Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat ...
Aim: Out of various members of heat shock protein (HSP) superfamily which act a molecular chaperon by binding to the denaturing ... protein thus stabilizing them and preserving their activity, HSP70 are of major importance in thermotolerance develop... ... Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle. *Bhat S ... Bhat, S., Kumar, P., Kashyap, N., Deshmukh, B., Dige, M. S., Bhushan, B., … Singh, G. (2016). Effect of heat shock protein 70 ...
Subcorneal colocalization of the small heat shock protein, hsp27, with keratins and proteins of the cornified cell envelope ... Background hsp27 is a member of the small heat shock protein family. Its expression in epidermal keratinocytes in situ and in ... Investigations of the molecular hsp27 interactions with the proteins of the cornified cell envelope are necessary to gain ... keratins and proteins of the cornified cell envelope (loricrin, filaggrin, transglutaminase 1). Results Actin staining did not ...
Heat shock proteins (HSPs) are by their nature upregulated in stressed cells and therefore abundantly present as potential ... Heat shock proteins (HSPs) are by their nature up-regulated in stressed cells and therefore abundantly present as potential ... Genetic evidence for a protective role for heat shock factor 1 and heat shock protein 70 against colitis. J Biol Chem (2007) ... A novel heat-shock protein coinducer boosts stress protein Hsp70 to activate T cell regulation of inflammation in autoimmune ...
... general Heat shock proteins Genetic aspects Physiological aspects Research Structure ... Heat shock and the heat shock proteins: an overview.(Report) by International Journal of Medical Science and Public Health; ... heat+shock+proteins%3a+an+overview.-a0353321634,/a,. Citations: *MLA style: "Heat shock and the heat shock proteins: an ... heat+shock+proteins%3a+an+overview.-a0353321634. *APA style: Heat shock and the heat shock proteins: an overview.. (n.d.) >The ...
tr,O69287,O69287_CAMJU Heat shock protein OS=Campylobacter jejuni OX=197 GN=clpB PE=3 SV=1 ... to allow unambiguous identification of a protein.,p>,a href=/help/protein_names target=_top>More...,/a>,/p>Protein namesi. ... Pfam protein domain database. More...Pfami. View protein in Pfam. PF00004 AAA, 1 hit. PF07724 AAA_2, 1 hit. PF17871 AAA_lid_ ... PROSITE; a protein domain and family database. More...PROSITEi. View protein in PROSITE. PS00870 CLPAB_1, 1 hit. PS00871 CLPAB ...
... nounAny of a group of cellular proteins produced under physiological stress, such as high or low body temperature, that ... stabilize other cellular proteins and adjust cellular metabolism to cope with the stress.... ... heat shock protein. heat shock protein. noun. Any of a group of cellular proteins produced under physiological stress, such as ... How would you define heat shock protein? Add your definition here.. Please enable JavaScript to view the comments powered by ...
To understand the evolutionary mechanisms that led to the diversification of the various types of heat shock proteins(Hsps) and ... Secondary Structure Prediction Lateral Gene Transfer Small Heat Shock Protein Lateral Transfer Heat Shock Gene These keywords ... Lee GJ, Roseman AM, Saibil HR, Vierling E (1997) A small heat shock protein stably binds heat-denatured model substrates and ... gene encoding a oc32-like protein is part of a unique heat shock gene cluster together with groESL1 and three small heat shock ...
Pharmacological Actions : Apoptotic, Bcl-2 protein down-regulation, Caspase-3 Activation, Heat Shock Protein Down-Regulation ... 22 Abstracts with Heat Shock Protein Down-Regulation Research. Filter by Study Type. Animal Study. ... Pharmacological Actions : Heat Shock Protein Down-Regulation, Immunomodulatory, Interferon Gamma Reducer. Additional Keywords ... Pharmacological Actions : Heat Shock Protein Down-Regulation. Additional Keywords : Chemothapeutic Synergy: Paclitaxel, ...
  • For example, Hsp60 , Hsp70 and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70, and 90 kilodaltons in size, respectively. (
  • Beginning in the mid-1960s, investigators recognized that many HSPs function as molecular chaperones and thus play a critical role in protein folding, intracellular trafficking of proteins, and coping with proteins denatured by heat and other stresses. (
  • [15] However, some studies suggest that an increase in damaged or abnormal proteins brings HSPs into action. (
  • By helping to stabilize partially unfolded proteins, HSPs aid in transporting proteins across membranes within the cell. (
  • Heat shock proteins (HSPs) chaperone other cellular proteins, guarding them from going astray, folding improperly or misassembling while forming larger aggregates, as in the examples below. (
  • Heat shock proteins (HSPs) are important molecular chaperones that regulate protein folding. (
  • HSPs assist in the folding and maintenance of newly translated proteins, the refolding of denatured proteins, and the further unfolding of misfolded or destabilized proteins to assist in their degradation. (
  • Heat shock proteins (HSPs, or molecular. (
  • Human endometrium expresses a molecular repertoire which includes the heat shock proteins (Hsps) Hsp27, Hsp60, Hsp70, Hsp90, and alpha crystallin B chain. (
  • In view of known functions of the Hsps, it is likely that these proteins are involved in protection of the endometrial proteins against factors with the potential to lead to protein denaturation. (
  • Hsps or stress proteins are highly conserved molecules that fulfill a range of functions, including cytoprotection and the intracellular assembly, folding, and translocation of oligomeric proteins. (
  • Heat shock proteins (HSPs) are primordial and abundant molecules expressed in all cells. (
  • 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. (
  • 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. (
  • Heat shock proteins (HSPs) are by their nature upregulated in stressed cells and therefore abundantly present as potential targets for such regulation. (
  • Microbial heat shock proteins (HSPs) are antigens with a well-established tolerance promoting capacity. (
  • In some habitats, a stress from daily or seasonal fluctuation of environmental temperature causes an organism to respond by inducing sets of proteins including heat shock proteins (HSPs) and this process is known as a heat shock response or stress response In addition to heat stress, HSPs respond to other factors such as pathogen infection, oxidative stress, heavy metals and xenobiotic stresses. (
  • The objective of the present study is to investigate the role of heat shock proteins (Hsps) in preimplantation embryonic development and uterine receptivity during lipopolysaccharide (LPS)-induced pregnancy loss. (
  • Heat shock proteins (HSPs) have been implicated in the stimulation and generation of both innate and adaptive immunity. (
  • Heat shock proteins (HSPs) 4 are ubiquitous. (
  • The role of heat shock proteins (Hsps) in cellular quality control and degradation of pathogenic proteins is reviewed. (
  • Heat shock proteins (HSPs) play cytoprotective activities under pathological conditions through the initiation of protein folding, repair, refolding of misfolded peptides, and possible degradation of irreparable proteins. (
  • Intracellular residing heat shock proteins (HSPs) with a molecular weight of approximately 70 and 90 kDa function as molecular chaperones that assist folding/unfolding and transport. (
  • When the innate immune system is activated, heat shock proteins (HSPs) are produced to protect cells. (
  • Heat shock proteins (HSPs) are produced by cells in response to stress, such as a sudden spike in temperature. (
  • Dubbed 'molecular chaperones', HSPs may be best known for their stabilizing role inside cells where they help sort, separate and fold other proteins. (
  • Background- Heat shock proteins (HSPs) are a family of proteins with immunogenic and proinflammatory properties. (
  • Heat shock proteins (HSPs), a family of chaperone proteins with strong antigenic properties, may represent a plausible link between infection, inflammation, and acute coronary syndromes (ACS). (
  • The highly conserved heat shock proteins (HSPs) are constitutively expressed and function as molecular chaperones which facilitate the synthesis and folding of proteins. (
  • Under stressful conditions such as heat shock, pH shift or hypoxia, increased expression of HSPs protect the cell by stabilizing unfolded proteins, giving the cell time to repair or re-synthesize damaged proteins. (
  • The family of heat shock proteins (HSPs) was initially characterized as a highly conserved battery of genes whose expression could be induced by heat shock. (
  • Heat shock proteins (HSPs) are endogenous proteins whose function is to maintain the cell's tolerance to insult, and glutamine supplementation is known to increase HSP expression during intense exercise. (
  • Prevention of denaturation or refolding of already denatured proteins appears to be the principle function of the Hsps. (
  • In addition to their function during heat stress, Hsps can serve important functions under non-stress conditions. (
  • Heat shock proteins (Hsps) are a ubiquitous component of the cellular response to stress in both prokaryotic and eukaryotic organisms, but their role and function during desiccation stress in terrestrial arthropods has received limited attention. (
  • At the cellular level, the stress response involves the synthesis of a highly conserved family of heat shock proteins (Hsps). (
  • The biological consequence was an exceptional increase of transcriptional activity for a family of proteins that, for this particular reason, were generically named heat-shock proteins (HSPs). (
  • HSPs form oligomeric complexes constitutively expressed under normal conditions (ranging up 5-10% of the total protein). (
  • Heat shock proteins or HSPs are being synthesized under different kind of stress conditions and act as molecular chaperones for protein molecules. (
  • Usually HSPs are cytoplasmic proteins and they function in various intra-cellular processes. (
  • Together with other HSPs, HSP60 is participating in reactivation of heat-denatured proteins. (
  • 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). (
  • Heat shock proteins (HSPs) perform essential biological functions under both physiological and stressful conditions (13-19). (
  • Some bacterial heat shock proteins are upregulated via a mechanism involving RNA thermometers such as the FourU thermometer , ROSE element and the Hsp90 cis-regulatory element . (
  • HSP90 receives folded proteins from other chaperones and helps to join them into a larger protein structure, such as a cellular receptor. (
  • Heat shock proteins, primarily members of the HSP90 and HSP70 families, participate in sounding the alarm and identifying the culprits. (
  • Previously, our experiments indicated that the ligand-free dioxin receptor is stably associated with the 90-kDa heat shock protein, hsp90. (
  • To do so, in the present paper we start to obtain some experimental data of the proliferation curves of solid tumor cells, actually, A549 and HepG2, as well as the time-changes of proteins, especially HSP90 and HSP72, in them. (
  • An international research team has identified a new function of Hsp90, one of the most common and studied proteins in the human body. (
  • New research by teams at UNSW and VIB-KU Leuven in Belgium shows that that in addition to its well-known role as a protein chaperone, heat-shock protein Hsp90 also stimulates exosome release. (
  • Hsp90, short for heat-shock protein 90, is one of the most common proteins, making up one or two out of every hundred proteins in our cells. (
  • Hsp90 also helps degrade damaged or misfolded proteins that are beyond salvation. (
  • These functions make Hsp90 a crucial governor of protein homeostasis in the cell. (
  • As part of its role as a chaperone, Hsp90 is known to stabilise several proteins that affect tumor growth. (
  • We hypothesize that heat shock protein 90 (HSP90) plays a role in regulating intracellular iron accumulation upon ischemia and that inhibiting HSP90 rescues the brain from ischemic injury. (
  • Histone deacetylase (HDAC) inhibitors and the heat shock protein 90 (Hsp90) inhibitor 17-AAG have recently been shown to inhibit synovial sarcoma in preclinical models. (
  • Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins. (
  • 13 ) showed that KIT activation depends on protein stabilization by heat shock protein 90 (HSP90), with HSP90 inhibition causing degradation of wild-type KIT and an imatinib-resistant KIT D816V mutant. (
  • 17-Allylamino-18-demethoxy-geldanamycin (17-AAG) is a geldanamycin derivative ( 14 , 15 ) that binds a conserved pocket in the HSP90 NH 2 -terminal domain and prevents HSP90 from stabilizing client proteins. (
  • HSP90 client proteins are then increasingly directed towards the proteasome machinery for degradation ( 16 , 17 ). (
  • There are more than 100 known HSP90 client proteins, and many of these, such as KIT, serve oncogenic roles, making HSP90 an attractive therapeutic target in various human cancers ( 18 ). (
  • HSP90COCHAPERONES (Are Heat Shock Protein 90 (Hsp90) Co-Chaperones Virulence Factors in the Human Fungal Pathogen Candida albicans? (
  • Efforts aiming to identify new drug targets, demonstrated that the environmentally responsive chaperone heat shock protein 90 (Hsp90), which is a central regulator of the cell's protein balance, regulates C. albicans virulence and stress response pathways. (
  • When measuring protein levels in virulence-related conditions such as filamentous growth and biofilm formation, the student noticed that Hsp90-activating and inhibiting co-chaperones were co-regulated. (
  • Heat shock protein 90 (HSP90) is a key component of a multichaperone complex involved in the posttranslational folding of a number of client proteins, many of which play essential roles in tumorigenesis. (
  • The molecular chaperone, heat shock protein 90 (HSP90), plays an important role in the posttranslational maturation and activation of many critical oncogenic client proteins that are essential for facilitating malignant transformation and promoting the survival, growth, and invasive potential of cancer cells ( 5, 6 ). (
  • Enzo Life Sciences ELISA kits offer an easy and reproducible way to quantify various heat shock proteins including HSP70 and HSP90α. (
  • Heat shock protein 90 (HSP90) is an ATPase-dependent molecular chaperone ubiquitously expressed in eukaryotic cells. (
  • 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. (
  • Meanwhile, the mRNA level and protein expression of Hsp90 decreased significantly ( P (
  • Scientists at the Technische Universitaet Muenchen and the Cluster of Excellence Nanosystems Initiative Munich show what this kind of cooperation looks like in detail using a novel methodology applied to the heat shock protein Hsp90. (
  • A typical example for this kind of cooperation can be seen in the heat shock protein Hsp90, which controls the proper folding of other proteins. (
  • Using a sophisticated methodology, a team led by Professor Thorsten Hugel, head of the Department for Molecular Machines at the TU Muenchen and member of the Excellence Cluster Nanosystemns Initiative Munich (NIM), has now managed to observe this reaction in detail for the first time - step for step in an Hsp90 molecule, P23 protein and ATP. (
  • Hsp90 interacts with and is important for the folding of protein kinases and steroid hormone receptors in mammalian cells (for review, see Caplan, 1999 ). (
  • Constitutively expressed Hsp90 is downregulated during diapause yet remains responsive to both heat and cold stress ( Rinehart and Denlinger, 2000 ). (
  • 18 These proteins are present and can be induced in all species, and they are categorized into several families that are named on the basis of their approximate molecular weight (eg, the 70-kDa hsp70). (
  • Botha M, Chiang AN, Needham PG, Stephens LL, Hoppe HC et al (2011) Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock. (
  • Cockburn IL, Pesce ER, Pryzborski JM, Davies-Coleman MT, Clark PG et al (2011) Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1. (
  • Heat shock protein 70 (HSP70) are the molecular chaperones that assist in folding of newly synthesized polypeptides, refolding of misfolded proteins and translocation of proteins through biological membranes, and in addition have regulatory functions in signal transduction, cell cycle and apoptosis. (
  • Molecular chaperones of HSP70 family are also essential for the cell to survive environmental stress including heat shock. (
  • E. coli contains at least two different HSP70 proteins, Dnak and HSC66 and 14 different genes encoding HSP70 have been found in the genome of Saccharomyces cereviseae. (
  • The prokaryotic version shares about 80% sequence identity with the eukaryotic HSP70 protein which is found in the cytosol and in the organelles such as ER, mitochondria and chloroplast. (
  • Prototypical HSP70 proteins contain a nucleotide binding domain (NBD) and a peptide-binding domain (PBD) that are connected by a flexible linker region that contributes to allosteric regulation of NBD and PBD activity. (
  • Using a groove formed by the [beta] subdomain in the PBD, HSP70 binds to protein that have exposed hydrophobic regions with an extended conformation and the [alpha]-helical part serves as a lid on the peptide binding unit without direct contact to the substrate. (
  • T. R. Rieger, R. I. Morimoto and V. Hatzimanikatis, Mathematical modeling of the eukaryotic heat-shock response: Dynamics of the HSP70 promoter ,, Biophysical Journal , 88 (2005), 1646. (
  • sHsps bind denatured proteins and facilitate their refolding by the ATP-dependent molecular chaperones of the Hsp70 family (Haslbeck et al. (
  • However, in a paper published today , in the Journal of Clinical Investigation , Lisa Cunningham and her colleagues at the US National Institute on Deafness and Other Communication Disorders in Bethesda, Maryland, show that the protective effect of a heat shock protein, HSP70, may provide a new therapeutic option to prevent inner ear cells injury by these antibiotics. (
  • But more importantly, when the research team used utricle cultures that couldn't generate their own HSP70-and didn't heat shock them-but then added both an aminoglycoside and human HSP70 to those cultures, the hair cells remained unscathed. (
  • Although it still isn't clear how the hair cells are saved by HSP70, these tests show the presence of the protein outside the hair cells is enough to induce protection, says Cunningham. (
  • We show that stimulation of murine and human macrophages with the heat shock proteins gp96 and hsp70 results in induction of inducible NO synthase and the production of NO. The release of NO by monocytes exposed to hsp60 has been documented previously. (
  • stimulation of macrophages with mixtures of IFN-γ and gp96 or hsp70 leads to a synergistic production of NO. The present observations extend the roles of these heat shock proteins in innate immune responses to another potent and highly conserved function of APC. (
  • We examined protein levels in all samples using Dotblott with monoclonal antibody anti-Hsp40 and anti-Hsp70. (
  • OSCC patients have increased Hsp70 levels, so it is possible that something is going wrong in protein folding. (
  • 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. (
  • The dimerization of GRPEL2 may activate the folding machinery responsible for protein import into mitochondrial matrix or enhance the chaperone activity of mitochondrial HSP70, thus protecting mitochondrial proteostasis in oxidative stress. (
  • A range of proteins called heat shock transcription factors regulated the expression of HSP70 genes and were therefore potential regulators of the CPR. (
  • HSFA2 activity induced the expression of the HSP70 chaperones, probably through an interaction with a specific piece of deoxyribonucleic acid (DNA) known as the heat shock element, HSE. (
  • Many heat shock proteins function together in co-chaperone complexes, such as HSP70/HSP40 (bacterial DnaK/DnaJ) that along with GrpE acts as an ATP-regulated shuttle complex for newly synthesized proteins. (
  • We analyzed the effect of B-chromosome presence on expression level of heat shock protein 70 (Hsp70) in cerebral ganglion and gonad in both males and females of the grasshopper Eyprepocnemis plorans . (
  • It is clear that heat shock protein 70 (HSP70) is responsible for stressful conditions. (
  • Sequential interplay between BAG6 and HSP70 upon heat shock. (
  • BAG6/Scythe/Bat3 is a cochaperone of the heat shock protein HSP70 and is involved in various developmental processes, cellular stress and viability. (
  • BAG6 interferes with the protein-refolding activity of HSP70 but its precise involvement in proteotoxic stresses remains unknown. (
  • 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 the in vivo study, fish exposed to an acute heat shock (1h at 10°C above ambient temperature) exhibited a significant elevation in red blood cell Hsp70 levels over a 24 h period. (
  • There was also a significant increase in plasma Hsp70 levels at 4 h, but not at 24 h post-heat shock. (
  • The HSP70 family is a set of highly conserved proteins that are induced by a variety of biological stresses, including heat stress, in every organism in which the proteins have been examined. (
  • and mitochondrial HSP70 (mtHSP70, GRP75 or mortalin) a 75 kDa protein that is found within the mitochondria. (
  • 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. (
  • Heat shock protein 70 (HSP70) confers protection against various stressors and has the anti-inflammatory activity. (
  • It has been suggested that the lack of introns in inducible HSP70 genes could help to circumvent blocks in RNA splicing and enable preferential expression of heat shock proteins during periods of stress (Huang et al. (
  • Heat-shock proteins are named according to their molecular weight. (
  • They occur in both eukaryotes and prokaryotes, and function mainly as molecular chaperones , protecting the cell's proteins as they become unfolded due to heating and enabling them to refold correctly. (
  • Neal L. Millar and George A. C. Murrell, "Heat Shock Proteins in Tendinopathy: Novel Molecular Regulators," Mediators of Inflammation , vol. 2012, Article ID 436203, 7 pages, 2012. (
  • Small heat shock proteins (sHSP) are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits [ PMID: 16225851 ]. (
  • Molecular chaperones in vivo play a pivotal role in the maintenance of the proteome quality control and in the correct balance between protein folding and degradation. (
  • Molecular chaperones or heat shock proteins are involved in diverse biological processes and play an important role in maintaining cellular homeostasis. (
  • It is a molecular chaperone which interacts with a large number of different proteins. (
  • Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein aggregation by binding clients destabilized during cellular stress. (
  • Small Heat Shock Proteins (sHSPs) are one of the least well understood classes of molecular chaperones, proteins which act to prevent or reverse improper protein associations ( 1 ). (
  • Most heat shock proteins (Hsp) function as molecular chaperones that help organisms to cope with stress of both an internal and external nature. (
  • 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. (
  • 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 ). (
  • Investigations of the molecular hsp27 interactions with the proteins of the cornified cell envelope are necessary to gain further insight into terminal keratinocyte differentiation and disorders of keratinization. (
  • A subfamily of small heat-shock proteins that function as molecular chaperones that aid in refolding of non-native proteins. (
  • Penke B, Bogár F, Crul T, Sántha M, Tóth ME, Vígh L. Heat Shock Proteins and Autophagy Pathways in Neuroprotection: From Molecular Bases to Pharmacological Interventions. (
  • The form of these functions is to help setting up a complex protein molecular fold (folded protein) in many important settings, such as growth, differentiation, and the ability to live. (
  • 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. (
  • The study evaluated the involvement of molecular structures called damage-associated molecular patterns (DAMPs), such as hyaluronan (HA) and heat shock proteins (Hsp) on NLRP1 and NLRP3 inflammasomes activation in peripheral blood monocytes. (
  • By comparing microarray analyses for arabidopsis plants treated with heat, AZC and tunicamycin we hoped to identify the molecular pathways involved in the CPR. (
  • Many heat shock protein family members are now known to function constitutively as molecular chaperones, stabilizing and assisting in the trafficking of nascent peptides during normal growth. (
  • The generation of a new proteostasis network implies an immediate role in protein synthesis, folding, disaggregation, or degradation, processes that encompass the translational machinery, molecular chaperones and their associated cochaperones, the ubiquitin-proteasome machinery, and the autophagy system. (
  • Because these proteins were first found in cells that were exposed to high temperatures, they are called "heat shock proteins" and have been named according to their molecular weights. (
  • Heat Shock protein 70 is one of those molecular chaperons which are highly concerned, involved in DE novo folding of proteins also in stressful conditions prevent the aggregation of unfolding proteins and even refold [ 3 ]. (
  • Several heat shock proteins function as intra-cellular chaperones for other proteins. (
  • The Human Heat Shock Proteins & Chaperones RT² Profiler PCR Array profiles the expression of 84 Heat Shock Protein genes that regulate protein folding. (
  • Protein chaperones assist several proteins in the folding to their native conformation. (
  • Protein chaperones contribute to maintain the correct balance between protein synthesis and degradation. (
  • Chaperones are ubiquitous proteins and are present in all the cells and in all the cellular compartments. (
  • Chaperones prevent protein misfolding and aggregation that may be associated to several degenerative diseases. (
  • Proteins of this class of chaperones have been found in nearly all organisms. (
  • They function mainly as CHAPERONES , permitting the correct refolding of proteins that have been unfolded during stress. (
  • Indeed, certain co-chaperones are important for survival of oxidative stress and heat shock, for biofilm formation, and the survival of an invertebrate model of fungal virulence. (
  • Both of these examples are associated with the accumulation of misfolded proteins, which is managed by the plant through the induction of protein chaperones to assist with protein refolding. (
  • We firstly observed this in plant cells infected with viruses which accumulated large amounts of viral proteins in the cell cytoplasms and induced a specific range of chaperones called cytosolic HSP70s1. (
  • These genes, which potentially identified the CPR subcomponent of the heat shock response included transcription factors, various chaperones, splicing factors and components of the protein degradation machinery. (
  • Enzo Life Sciences is your exclusive source for the comprehensive portfolio of Stressgen® products specific to the analysis of Heat Shock Proteins (HSP) and chaperones. (
  • The latter factor, CtsR, controls the expression of genes encoding the HSP100/Clp chaperones and the protease ClpP ( 6 , 8 ) that constitute the core of the bacterial protein quality control system ( 9 , 10 ). (
  • In this article we review the basics of the stress response, summarize current controversies over the role of extracellular chaperones in inflammatory reactions and autoimmunity, and discuss the cytoprotective and immunoregulatory roles of heat-shock proteins, a challenging subject that may open a new avenue for the drug discovery and treatment of diseases related to autoimmune disturbs. (
  • Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay. (
  • The small heat shock protein Hsp27: Present understanding and future prospects. (
  • Background hsp27 is a member of the small heat shock protein family. (
  • We analysed the colocalization of hsp27 with actin, keratins and proteins of the cornified cell envelope (loricrin, filaggrin, transglutaminase 1). (
  • Small heat shock proteins including HSP27 and the crystallins form large oligomeric complexes that function to prevent protein aggregation. (
  • peptides in heat-shock protein Hsp20 (G71HFSVLLDVKHFSPEEIAVK91) and Hsp27 (D93RWRVSLDVNHFAPDELTVK113) with sequence homology to alpha-crystallin also have robust chaperone and anti-apoptotic activities. (
  • [7] The small 8-kilodalton protein ubiquitin , which marks proteins for degradation, also has features of a heat shock protein. (
  • Another protein, ubiquitin , is regarded as a heat-shock protein and acts as a marker for proteins destined for degradation. (
  • The unbalance of the equilibrium between protein synthesis, protein folding and protein degradation may contribute to protein misfolding and aggregation which may lead to the onset of several degenerative diseases associated with protein aggregation, such as Alzheimer's and Huntington's disease. (
  • The current view of their chaperone action is that they bind unfolding "client" proteins, thereby preventing their irreversible aggregation ( 9 - 12 ). (
  • Hsp demonstrate specific affinity to particular classes of oncogenic peptides and client proteins in cancer cells, and are able to stabilize mutated oncogene proteins. (
  • Therefore, it has been proposed that immunization with heat-shock protein peptides could prevent the development of certain diseases. (
  • Increased synthesis of selected proteins in Drosophila cells following stresses such as heat shock was first reported in 1974. (
  • In addition to being constitutively expressed (making up 5% to 10% of the total protein content under normal growth conditions), the synthesis of these proteins can be markedly induced (up to 15% of the total cellular protein content) by a range of cellular insults that cause protein unfolding, misfolding, or aggregation and a flux of newly synthesized non-native proteins, the function of which is to stabilize and refold proteins. (
  • Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat production by uncoupling proteins. (
  • The name of these proteins however was derived from the first trigger i.e. heat that was identified as increasing their synthesis. (
  • Activity of taraxasteryl acetate on inflammation and heat shock protein synthesis. (
  • S.v. Activity of taraxasteryl acetate on inflammation and heat shock protein synthesis. (
  • It also showed inhibitory effect on heat shock protein 72 (hsp72) synthesis in stimulated neutrophils, while it had opposite effects on unstimulated cells. (
  • We have recently shown that protein synthesis is required for the stabilization. (
  • According to two-dimensional gel electrophoresis the synthesis of heat shock protein 90 was also increased in a chondrocytic cell line and in HeLa cells, and mass spectrometric analysis suggested that the induction was rather due to increase in heat shock protein 90beta than in heat shock protein 90alpha. (
  • Aspects of the response to heat stress have been highly conserved from bacteria to humans, including the induction of heat stress protein (Hsp) synthesis. (
  • Heat stress results in the production of mis-folded proteins during their synthesis and the denaturation of existing proteins. (
  • HSP60 attracts a new amino acid chain or a protein that has lost its structure and internalizes it. (
  • This observation raises the interesting question of how Hsp60, which is typically an intracellular protein, gets in contact with the immune system. (
  • 8 Therefore, we investigated whether this high prevalence of Cp-HSP60 IgG antibody titers was related to the presence of coronary artery disease, myocardial necrosis, and levels of high-sensitivity C-reactive protein (hs-CRP) and whether it decreases during follow-up, which would suggest a specific link with the acute phase of instability. (
  • The HSP60/HSP10 complex (bacterial GroEL/GroES) forms an alternative protein folding mechanism in the mitochondria. (
  • HSP protein 60 (HSP60) also plays an important role in mitochondrial function and in immune system activation. (
  • The chaperonin human heat shock protein 60 (HSP60) occurs in mitochondria and in bacteria, is highly conserved, antigenic and a major autoantigen. (
  • Thus, the 62K urease-associated protein of H. pylori belongs to the HSP60 family of stress proteins known as chaperonins. (
  • In muscle tissues HSP60 facilitates the folding and assembly of proteins as they enter the mitochondria, and stabilizes preexisting proteins under stress conditions. (
  • It has also been suggested that heat shock protein 60 (Hsp60) belonging to a class of highly conserved proteins may play a role in the pathogenesis of chlamydial infections. (
  • The involvement of the heat shock protein 60 (Hsp60) of C. trachomatis in the immunopathogenesis of trachoma 2 , pelvic inflammatory disease 3 , tubal infertility 4 and ectopic pregnancy 5 is well known. (
  • It is also known that persistent C. trachomatis infection in cell culture leads to increased expression of Hsp60 proteins in chlamydia particles 6 . (
  • An enzyme immunoassay (EIA) method for the measurement of immunoglobulin-(Ig)A and IgG antibodies against C. pneumoniae and human Hsp60 proteins was developed. (
  • However, because of their occasional unsatisfactory performance, researchers used heat shock protein 60 (Hsp60) as a receptor for Listeria adhesion protein LAP. (
  • Search, Find and Buy Antibodies, ELISA Kits and Proteins. (
  • Additionally we are shipping Heat Shock 70kDa Protein 4 Antibodies (99) and Heat Shock 70kDa Protein 4 Proteins (6) and many more products for this protein. (
  • Serum levels of anti-heat shock protein 27 antibodies in patients with chronic liver disease. (
  • By showing an association of Chlamydia pneumoniae heat shock protein 60 immunoglobulin A antibodies with asthma, the results support the hypothesis of an association between Chlamydia pneumoniae infection and asthma and support the need for further investigations on the role of heat shock protein 60 in the pathogenesis of asthma. (
  • The new biosensor uses heat shock proteins instead of the antibodies used in other tests, and tests indicate that the sensor is faster and more sensitive at detecting the bacterium than antibody-based tests, with a microbe capture rate up to 83% greater than possible with the antibody-based tests. (
  • [4] Many members of this group perform chaperone function by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. (
  • [10] [11] This discovery eventually led to the identification of the heat-shock proteins (HSP) or stress proteins whose expression this puffing represented. (
  • Since that time, the study of stress proteins has undergone explosive growth. (
  • As a consequence, the heat shock proteins are also referred to as stress proteins and their upregulation is sometimes described more generally as part of the stress response . (
  • During heat stress, outer membrane proteins (OMPs) do not fold and cannot insert correctly into the outer membrane. (
  • Many of the heat-shock proteins are also induced by other stresses, both natural and unnatural, including reduced oxygen concentration, changes in osmotic potential, ionizing radiation , and toxins, and hence are also called stress proteins . (
  • However, HSP expression also increases due to other sources of cellular stress, including osmotic stress, oxidative stress, and the unfolded protein response, mediated by the ATF family of transcription factors. (
  • The importance of the sHSPs is evidenced by their almost ubiquitous expression ( 2 ), the presence of multiple sHSP genes in most organisms ( 3 ), and their dramatic up-regulation under stress conditions making them among the most abundant of cellular proteins ( 4 ). (
  • The heat-inducible members of the Hsp100 (or Clp) family of proteins share a common function in helping organisms to survive extreme stress, but the basic mechanism through which these proteins function is not understood. (
  • Homology with the Escherichia coli ClpA protein suggests that Hsp104 may provide stress tolerance by helping to rid the cell of heat-denatured proteins through proteolysis. (
  • 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. (
  • 4,5] Many of the morphological and phenotypic effects of heat stress can be explained by the aggregation of proteins and an imbalance of protein homeostasis. (
  • Any of a group of cellular proteins produced under physiological stress, such as high or low body temperature, that stabilize other cellular proteins and adjust cellular metabolism to cope with the stress. (
  • Section II, addresses the role heat shock proteins play in psychological disorders including post traumatic stress disorders and learning (Heat Shock Proteins and Psychological Stress). (
  • an intracellular protein that increases in concentration during metabolic stress, such as exposure to heat. (
  • In PROKARYOTES heat shock proteins may account for about 15% of the cellular protein under stress conditions. (
  • Then, if you have thermal stress, conditions might shift, whereby proteins that already require folding QC will need more of it, and those that didn't require any will suddenly need it (or vice versa). (
  • Their name dates back to the 1980s, when they were first described as a group of proteins upregulated upon sudden heat stress. (
  • As a protein chaperone, it assists in the proper folding of other proteins and stabilizes them in case of cellular stress. (
  • Heat shock proteins often function as chaperons in the refolding of proteins damaged by heat stress. (
  • Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model? (
  • The aim of this study was to investigate the role of heat-shock proteins after heat-shock stress on the post-ischemic recovery of cardiac mechanical and endothelial function following a prolonged cardiac arrest. (
  • Both postischemic myocardial and endothelial function were improved by heat stress. (
  • Various signals modulate HspB1 phosphorylation: growth factors, tumor necrosis factor , differentiating agents, heat and oxidative stress (Arrigo et al. (
  • If the induction of HSFA2-AZC were a signature of the CPR and one consequence of heat stress was protein misfolding, then heat stress should also induce HSFA2-AZC. (
  • The stress response was rather intense in HeLa cells, therefore, we investigated the effect of continuous 30 MPa hydrostatic pressure on the expression of the two heat shock protein 90 genes in HeLa cells using Northern and Western blot analyses. (
  • These results show a specific regulation of stress proteins in cells exposed to high hydrostatic pressure. (
  • The results point to an interesting interaction between B-chromosome and stress protein expression in reproductive tissue. (
  • These results strongly suggest a functional redundancy between FkpA and SurA for OMP biogenesis under heat shock stress conditions. (
  • Editor's Comment: Heat shock proteins (HSP) prevent cellular damage when an organism is exposed to elevated temperatures or other stress. (
  • The aim of this study was to investigate the effects of cold stress on the expression levels of heat shock proteins (Hsps90, 70, 60, 40, and 27) and inflammatory factors (iNOS, COX-2, NF-κB, TNF-α, and PTGEs) and oxidative indexes in hearts of chickens. (
  • Vulnerability of experimentally induced fatty liver to heat stress in rats. (
  • The aim of this study was to confirm the vulnerability of fatty liver to heat stress using fatty liver rats from the viewpoint of the induction of apoptosis. (
  • The plant heat stress protein, Hsp101, and the yeast ortholog, Hsp104, are required to confer thermotolerance in plants and yeast ( Saccharomyces cerevisiae ), respectively. (
  • In contrast, the level of Hsp101 transcript increased in the tassel at anthesis following a heat stress without an increase in Hsp101 protein. (
  • However, anthers at anthesis, mature pollen, developing endosperm, and embryos largely failed to mount a heat stress response at the level of Hsp101 protein or mRNA, indicating that Hsp101 expression is not heat inducible in these organs. (
  • These data suggest an organ-specific control of Hsp101 expression during development and following a heat stress through mechanisms that may include posttranscriptional regulation. (
  • To eliminate damaged proteins, cells developed highly efficient stress response and protein quality control systems. (
  • One of the most intensely studied stress-response pathways is the bacterial heat-shock response. (
  • However, when bacteria are exposed to stress situations, the ClpC chaperone preferentially interacts with misfolded proteins. (
  • To clarify and delineate the precise function of CtsR and McsB in the bacterial stress response, we screened the respective proteins from various Gram-positive bacteria for recombinant production and succeeded in reconstituting the Bacillus stearothermophilus CtsR/McsB system in vitro. (
  • These proteins are essential for maintenance of cellular homeostasis, both in times of stress and in normal cell functioning. (
  • Further work on the effects of eHsp70 on target tissues effects, and the mechanisms involved, may have important implications in our understanding of the role of this stress protein in cell signaling and stress adaptation in fish. (
  • The stress response to heat-shock was originally described in the early '60s by the Italian researcher Ferruccio Ritossa [ 4 ]. (
  • In normal conditions HSP20 is diffusely disturbed in cytosol but under the heat stress it undergoes translocation to membrane fraction. (
  • Heat stress shifts the equilibrium towards oligomers, whereas phosphorylation induces dissociation of large oligomers and decrease of its chaperone activity. (
  • Conclusion: Salivary and circulatory Heat Shock protein 70 showed significant increase in Individuals undergoing renal dialysis .Thus, Circulatory and salivary Heat Shock Protein 70 is an efficient stress marker in chronic renal disease condition. (
  • As a response to stress ancient signalling pathway leads to expression of heat shock proteins, they have an efficient protective mechanism, preventing a non -specific protein aggregate [ 2 ]. (
  • Heat shock proteins 70 protects cells against oxidative stress inhibits stress kinase and apoptosis [ 4 ]. (
  • Heat shock proteins (Hsp) are a common focus in assays used to establish conditions of physiological and environmental stress (Downs et al. (
  • These heat shock proteins are really important in a lot of stress responses. (
  • Seventy international academics and researchers contribute 25 chapters on new research in the field of heat shock proteins (HSP), groups of proteins whose expression is increased when the cells of living organisms are exposed to elevated temperatures or other stress. (
  • Both chlamydial and human heat shock protein 60s (HSP 60), which colocalize in human atheroma, may contribute to inflammation during atherogenesis. (
  • 2006). Increased expression of HspB1 in response to the aggregation of proteins specific for conformational diseases have been reported by several authors (Outeiro et al. (
  • All living organisms face a variety of environmental stresses that cause the misfolding and aggregation of proteins. (
  • Their name comes from their original discovery as genes and proteins that increase their expression under elevated temperatures, mediated by transcription factors known as the heat shock factors. (
  • From these, 425 genes were also differentially expressed after heat shock. (
  • The crystal structure of the CtsR repressor, in complex with DNA, pinpointed key residues important for high-affinity binding to the promoter regions of heat-shock genes. (
  • In B. subtilis , CtsR represses transcription of the clpC heat shock operon and the clpE and clpP genes by binding specifically to a seven-nucleotide direct repeat sequence located upstream of the transcriptional start sites ( 7 ). (
  • It is assumed that the released McsB can now form a complex with CtsR, thereby displacing it from DNA and inducing the expression of heat-shock genes ( 14 ). (
  • The inducible 72 kDa heat shock protein (HSP72) has been shown to be protective in non-neuronal cells and neurons in culture, but its function and the control of its expression in the CNS are poorly understood. (
  • Chaperone proteins and folding catalysts may contribute to successful folding into the native and active protein conformation in the crowded cellular environment, thus avoiding aggregation of non‐native protein forms. (
  • In addition to numerous components in immune responses, chaperone proteins are also detected in the extracellular fluids and have been implicated in autoimmune and inflammatory diseases acting as pro- and anti-inflammatory factors. (
  • sHSPs independently express not only in heat shock response but also have developmental roles in embryonic or juvenile stages of mammals, teleost fish and some lower vertebral genomes. (
  • Ali Khan H and Mutus B (2014) Protein disulfide isomerase a multifunctional protein with multiple physiological roles. (
  • Oligomeric proteins assemble with exceptional selectivity, even in the presence of closely related proteins, to perform their cellular roles. (
  • This initial biochemical finding gave rise to a large number of studies on the induction of heat shock and its biological role. (
  • Induction of heat-shock proteins enhances myocardial and endothelial functional recovery after prolonged cardioplegic arrest. (
  • The total gene expression profile of heat-shocked plants showed the induction of HSFA2 and HSFA2-AZC, confirming that the heat shock response involved the CPR. (
  • Specific induction of heat shock protein 90beta by high hydrostatic pressure. (
  • Heat shock mediated induction of [pSer326]HSF1 Protein (Prod. (
  • Induction is expressed as the fold change relative to non heat‐shocked control samples. (
  • Background: Exposure of Leishmania promastigotes to the temperature of their mammalian hosts results in the induction of a typical heat shock response. (
  • Heat shock protein induction in rat hearts. (
  • Given that Fast Track designation is not typically discussed until Phase 2 data is produced, we view the FDA's position as very encouraging for our technology and strategy of targeting heat shock protein induction as a potential treatment for ALS. (
  • Any of a large group of proteins that protect cells from injury caused by increased temperatures or other physical stresses. (
  • A special group of proteins, the so-called chaperons, helps other proteins to obtain their correct conformation. (
  • The presence of a specific group of proteins in the fruitfly Drosophilia melanogaster as a response to high temperature first identified by Ritossa in 1962 then termed as heat shock protein, have been an area of interest with context to their biochemical and functional role, change in cellular changes during disease, aging and infectious process [ 1 ]. (
  • Any of a group of proteins that are synthesized in the cytoplasm of cells as part of the heat shock response and act to protect the chromosomes from damage. (
  • Isolation and characterization of a human heart cDNA encoding a new member of the small heat shock protein family--HSPL27. (
  • Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. (
  • The authors experimentally investigated how two oligomeric small heat-shock protein paralogs avoid coassembly and found that flexibility at regions outside of the interaction interfaces played a key role. (
  • αB-Crystallin, a member of the small heat shock protein (HSP) family, accumulates in reactive astrocytes in a variety of pathological conditions. (
  • This extends the paradigm that intrinsic dynamics are crucial to protein function to include equilibrium fluctuations in quaternary structure, and suggests they are integral to the sHSPs' role in the cellular protein homeostasis network. (
  • The ubiquitous presence of amyloids in NDDs suggests the involvement of disturbed protein homeostasis (proteostasis) in the underlying pathomechanisms. (
  • As a chaperone, heat shock protein acts as central integrators of protein homeostasis in cell. (
  • Errors in protein folding result in a new homeostasis or inhibition of apoptosis and increasing cell proliferation that triggers carcinogenesis. (
  • With the purpose to protect proteins from misfolding, denaturation and/or aggregation, cells trigger a fast response characterized by a number of events able to protect them from the hostile environment, and restore a balanced and safe new steady-state of protein homeostasis commonly referred to as 'proteostasis' [ 1 , 2 ]. (
  • Intracellular protein homeostasis is largely controlled by Heat shock proteins (Hsp). (
  • HspB1 is a protein of 205 amino acids (22783 Da), which can be phosphorylated at serines 15, 78 and 82 by mitogen- activated protein kinases associated protein kinases ( MAPKAP kinase 2 , MAPKAP kinase 3 ). (
  • The activity of heat shock proteins is relatively unaffected by an antagonist of LPS, and is abrogated by heat denaturation. (
  • Expression of the hspb4 gene, which codes for alpha crystallin , increases considerably in the lens in response to heat shock. (
  • QIAGEN provides a broad range of assay technologies for heat shock protein and chaperone research that enables analysis of gene expression and regulation, epigenetic modification, genotyping, and signal transduction pathway activation. (
  • See 3 reference sequence protein isoforms for the TRAP1 gene. (
  • 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. (
  • section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. (
  • Petersen and Mitchell found that in D. melanogaster a mild heat shock pretreatment which induces heat shock gene expression (and greatly enhances survival after a subsequent higher temperature heat shock) primarily affects translation of messenger RNA rather than transcription of RNA. (
  • The choices of species and reviewed settings are considered only if you query protein names, protein description or gene names. (
  • When the gene for a self-assembling protein duplicates, it might be expected that the related proteins (paralogs) would retain interfaces that would allow coassembly. (
  • We show that most proteins related by gene duplication of an oligomeric ancestor have evolved to avoid hetero-oligomerization and that this correlates with their acquisition of distinct functions. (
  • Death-associated protein 6 also known as Daxx is a protein that in humans is encoded by the DAXX gene. (
  • This gene encodes a multifunctional protein that resides in multiple locations in the nucleus and in the cytoplasm. (
  • Recombinant fragment, corresponding to a region within amino acids 1 -219 of the Human Heat Shock Factor 2 Binding Protein (O75031). (
  • Chaperokine, is a term that describes the unique function of extracellular heat shock protein (eHsp) as both chaperone and cytokine. (
  • Banumathy G, Singh V, Pavithra SR, Tatu U (2003) Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. (
  • Some like it hot: the structure and function of small heat-shock proteins. (
  • They are expressed in all organisms and in different subcellular compartments, their predominant function being the folding and unfolding of protein substrates ( 1 ). (
  • Also, if the cell is under a high demand for protein production, then it might adaptively upregular HSP function simply to deal with the increased load - regardless of thermal conditions. (
  • Heat shock proteins have been found in all species examined, from bacteria to humans, suggesting that they evolved very early and have an important function. (
  • Many proteins form complexes to function. (
  • In the cytoplasm, the encoded protein may function to regulate apoptosis. (
  • The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination. (
  • Several additional interacting proteins are known, but not always is there an understanding of the specific function and relevance of this interaction. (
  • While at first Daxx was said to be a "death protein", it is suggested that associating with centromeric components leads to another function of Daxx. (
  • The genetics and regulation of heat-shock proteins. (
  • Taken together, this project has found a new method for measuring ferrous iron levels and a possible link among heat shock proteins in cellular iron regulation. (
  • They also participate in protein assembly, export, turn-over and regulation. (
  • Identification of the CtsR/McsB arginine phospho-switch expands the repertoire of possible protein modifications involved in prokaryotic and eukaryotic transcriptional regulation. (
  • however, the relevance of this protein in intercellular signaling, especially in regards to immune regulation, is gaining increasing importance in mammalian models. (
  • It has been well established that elaborate involvement of heat shock proteins is required during the process of malaria pathogenesis. (
  • Acharya P, Chaubey S, Grover M, Tatu U (2012) An exported heat shock protein associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytes. (
  • This book is a must read for heat shock protein researchers, graduate and postgraduate fellows in the field of Medicine in general and specialities in Excersie Physiology, Neuroscience, Immunology, Aging and Pathology. (
  • Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. (
  • Some members of the HSP family are expressed at low to moderate levels in all organisms because of their essential role in protein maintenance. (
  • a class of PROTEINS synthesized in organisms in response to various stresses, such as elevated temperature, reduced oxygen concentration and ionizing radiation. (
  • They play an important role in protein-protein interactions such as folding and assisting in the establishment of proper protein conformation (shape) and prevention of unwanted protein aggregation. (
  • Here we investigate the role of Hsp104 in vivo using a temperature-sensitive Vibrio harveyi luciferase-fusion protein as a test substrate. (
  • Heat Shock Proteins and Whole Body Physiology is an exciting new book in the Heat Shock Proteins series which provides the most up-to-date review on novel mechanisms insights into the important role played by heat shock proteins in human physiology. (
  • Section I, introduces the readers to the role played by heat shock proteins in various diseases and disorders (Heat Shock Proteins and Disease). (
  • Section III, present a detailed review of the role played by heat shock proteins in exercise physiology (Heat Shock Proteins and Exercise Physiology). (
  • Tonight I decided to dedicate a few minutes tonight to look into the possible role of heat shock proteins in hair growth. (
  • But scientists continue to discover the protective role that heat shock proteins can play outside of cells-from activating the body's defense system to helping repair injured muscle . (
  • It has been suggested that heat shock proteins play an important role in parasite survival and differentiation. (
  • Also, while trout hepatocytes secrete eHsp70 in response to endotoxin shock, a role for eHsp70 in eliciting an immune response is not clear in lower vertebrates. (
  • Heat shock proteins play an important role in protein-protein interactions, including folding and assisting in establishing of proper protein conformation, and prevention of inappropriate protein aggregation. (
  • Background and Objective: Heat shock protein 70 usually located in the cytoplasm, it plays an important role has a chaperone. (
  • The role of heat shock proteins in chronic renal damage, their protective and deleterious effect is of prime importance for the future perspectives of optimizing renal therapy the aim of this study was to evaluate the circulatory and salivary heat shock protein level 70 in healthy individuals and individuals undergoing renal dialysis with chronic renal disease. (
  • Heat shock protein 70 usually located in the cytoplasm, it plays an important role has a chaperone. (
  • The aim of the study was (i) to investigate DNA polymorphisms of the obtained bacterial strains isolated from avian feathers (ii) obtaining recombinant Hsp55 protein and defining its role as a potential component of vaccines used in poultry diseases. (
  • After Fas stimulation, Daxx is activated and plays its role of pro-apoptotic protein in activating the c-JUN-N-Terminal Kinase (JNK) pathway. (
  • 2007). Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma. (
  • 2016). The cytomegalovirus protein UL138 induces apoptosis of gastric cancer cells by binding to heat shock protein 70. (
  • It interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1 (ETS1). (
  • The Cignal Heat Shock Element (HSE) Reporter Assay Kit is designed to monitor the activity of heat shock response through measuring transcriptional activity of heat shock transcription factors. (
  • DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. (
  • Sensitive, ELISA kit for this key transcription factor for heat shock protein (chaperone) research. (
  • In the nucleus, the encoded protein functions as a potent transcription repressor that binds to sumoylated transcription factors. (
  • High pressure increases cellular heat shock protein 70 level in a number of cell types on account of increased stabilisation of the heat shock protein 70 mRNA. (
  • Heat shock protein 90beta mRNA level increased within 6 hours of exposure to 30 MPa hydrostatic pressure, while hsp90alpha level remained stable. (
  • In expanding foliar leaves, husk leaves, the tassel at the premeiosis stage of development, or pre-anthesis anthers, however, the heat-mediated increase in protein was not accompanied by an equivalent increase in mRNA. (
  • In situ RNA localization analysis revealed that Hsp101 mRNA accumulated in the subaleurone and aleurone of developing kernels and was highest in the root cap meristem and quiescent center of heat-stressed roots. (
  • Overall, heat shock protein inhibitors not only provide us with a new avenue to tackle malaria but also shed light on novel features of parasite's biology. (
  • This protein is a member of the serpin superfamily of serine proteinase inhibitors. (
  • Synergism of heat shock protein 90 and histone deacetylase inhibitors in synovial sarcoma. (
  • In muscle cells HspB3 forms an oligomeric 150 kDa complex with myotonic dystrophy protein kinase-binding protein (MKBP/ HspB2), this complex may comprise one of two independent muscle-cell specific chaperone systems. (
  • In 1974, Tissieres, Mitchell and Tracy discovered that heat-shock induces the production of a small number of proteins and inhibits the production of most others. (
  • Without P23 the heat shock enzyme effectively runs on idle. (
  • However, while normal enzyme reactions often are easy to follow because the involved proteins alter their conformations clearly, the interaction between P23 and ATP involves significantly less conspicuous changes in state. (
  • Without P23 the heat shock enzyme effectively runs on idle," explains Bjoern Hellenkamp their results. (
  • this protein can be removed from the urease by ion-exchange chromatography without inactivating the enzyme. (
  • Saliva and serum samples were evaluated for Heat shock protein 70 by ELIZA Method (Enzyme -linked immunoassay for heat shock protein 70) and statistical analysis was done with independent student't' test. (
  • HSP18.1 represents the family of class I cytosolic plant sHSPs which accumulate at heat-shock temperatures (≥38 °C) to ≈1% of the total cellular protein ( 19 ). (
  • HspB1 belongs to the ubiquitous family of small heat shock proteins (sHsps). (
  • Daxx interacts with the TGF-β type II receptor by binding of C-terminal domain of the protein. (
  • The protein folding of a nascent polypeptide is the decoding of the linear information contained in the primary sequence into the native and functionally active three‐dimensional conformation. (
  • The native protein conformation is the active and functional form of the protein in vivo . (
  • Therefore the energy of stabilization of a folded protein is relatively low (30-65 KJ/mol) and a slight increase in temperature may cause labile proteins to lose their distinct native conformation. (
  • HSP47 Heat-Shock Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (
  • This graph shows the total number of publications written about "HSP47 Heat-Shock Proteins" by people in Harvard Catalyst Profiles by year, and whether "HSP47 Heat-Shock Proteins" was a major or minor topic of these publication. (
  • Below are the most recent publications written about "HSP47 Heat-Shock Proteins" by people in Profiles. (
  • Interactome Screening Identifies the ER Luminal Chaperone Hsp47 as a Regulator of the Unfolded Protein Response Transducer IRE1a. (
  • [8] A conserved protein binding domain of approximately 80 amino-acid alpha crystallins are known as small heat shock proteins (sHSP). (
  • Botha M, Pesce ER, Blatch GL (2007) The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. (
  • Expression of heat shock proteins 70 and 47 in tissues following short-pulse laser irradiation: assessment of thermal damage and healing. (
  • Mechanisms of Protein Folding, 2nd edn, pp. 212-249. (
  • 7. What Are the Mechanisms of Heat Shock Protein-Mediated Cytoprotection Under ATP Deprivation? (
  • Written by leaders in the field of heat shock protein exercise physiology, neuroscience and aging, the chapters systematically and in a step wise fashion takes the reader through the fascinating mechanisms by which heat shock proteins modulate human disease and pathophysiology and provides answers as to its biological significance to the host. (
  • We named this new phenomenon the cytosolic protein response (CPR) and compared the underlying mechanisms with those for the UPR. (
  • Neuroinflammation is a hallmark of ALS pathology characterized by activation of glial cells, which respond by upregulating small heat shock proteins (HSPBs), but the exact underlying pathological mechanisms are still largely unknown. (
  • p>This section provides any useful information about the protein, mostly biological knowledge. (
  • Plant and animal responses to misfolded protein in a specific subcompartment of cells, the endoplasmic reticulum (ER), were studied extensively before, but responses to the accumulation of misfolded protein in the soluble cytosol, i.e. outside of the ER, was a novel area of research. (
  • A number of molecules have been proposed, including members of the heat shock protein (hsp) families. (
  • Heat Shock Proteins seem to be a broad category for molecules that are produced during temperature, UV, or other stresses and assist in folding proteins. (
  • They can contain signaling molecules but also potentially toxic proteins. (
  • A mild heat shock pretreatment of the same kind that protects against death from subsequent heat shock also prevents death from exposure to cold. (
  • Heat-shock proteins also occur under non-stressful conditions, simply "monitoring" the cell's proteins. (
  • Finally, putative therapeutic strategies for efficient removal of cytotoxic proteins from neurons and design of new therapeutic targets against the progression of NDDs are discussed. (
  • Heat shock proteins ( HSP ) are a family of proteins that are produced by cells in response to exposure to stressful conditions. (
  • The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). (
  • Fragments of such proteins can then potentially act as antigens, substances that provoke an immune response. (
  • heat-shock protein ( HSP ) Any of various proteins that are synthesized by living cells in response to increased temperature. (
  • Is the Subject Area "Heat shock response" applicable to this article? (
  • One of the most amazing aspects of heat shock response is that it is triggered by a temperature increase of just a few degrees. (
  • The former process was called the unfolded protein response (UPR). (
  • We expected that responses to heat-treatment and AZC treatment would both include the CPR and UPR and that response to tunicamycin would be restricted to the UPR. (
  • High-sensitivity ELISA kit for quantifying both normal and upregulated levels of Grp78/BiP for unfolded protein response, cancer and neurodegenerative disease research. (
  • Neither heat (45°C) nor cold (-10°C) treatment further enhances this response. (
  • In the Gram-positive model organism Bacillus subtilis , the heat-shock response is mediated by a complex regulatory network ( 1 , 2 ) that is under control of at least four major transcriptional regulators, including the alternative sigma factor σB ( 3 ), the two-component response regulator CssR ( 4 ), and the repressors HrcA ( 5 ) and CtsR ( 6 , 7 ). (
  • Here, we report results of laboratory experiments to establish the upper thermal tolerance and heat shock protein response of juvenile American shad exposed to gradually increasing temperatures. (
  • p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later. (
  • If you enter a valid Uniprot ID, UniProt accession number or RefSeq protein ID, the system will not consider the species and reviewed settings of your query. (
  • Heat treatment abolished all these effects, but did not alter the ability of E. coli LPS to induce these functions. (
  • To consistently induce the CPR, the accumulation of misfolded proteins was induced by treatment with a chemical azetidine-2-carboxylic acid (AZC). (
  • It is also a subunit of AUF1-containing protein complexes [ PMID: 18573886 ]. (
  • Here we capitalize on these unique advantages to study the complexes formed between pea HSP18.1 and a model client protein, firefly luciferase (Luc). (
  • In ECs, either HSP 60 triggered activation of NF-κB complexes containing p65 and p50 Rel proteins. (
  • It is known that rapid heat hardening can be elicited by a brief exposure of cells to sub-lethal high temperature, which in turn provides protection from subsequent and more severe temperature. (
  • When a cell is cancerous or infected by a pathogen, it generates proteins not found in normal cells. (
  • We consider a relation between proliferation of solid tumor cells and time-changes of the quantities of heat shock proteins in them. (
  • Finally, we discuss a problem which exists between mitosis of solid tumor cells and time-changes of the quantities of heat shock proteins, from the viewpoint of biotechnology. (
  • Exosomes are important for signal transduction across cells, but these vesicles are often hijacked by toxic proteins such as prions, alpha-synuclein or tau, thus contributing to the spread of diseases across the brain," he says. (
  • The accumulation of faulty protein folding would harm cells and can result in death. (
  • The outer membrane proteins (OMPs) of Gram-negative bacterial cells, as well as the mitochondrion and chloroplast organelles, possess unique and highly stable β-barrel structures. (
  • We also demonstrated that the deletion of fkpA from the Δ surA cells resulted in only a mild decrease in the levels of folded OMPs at the normal temperature but a severe decrease as well as lethality at the heat shock temperature, whereas the deletion of fkpA from the Δ skp cells had no detectable effect on OMP biogenesis at either temperature. (
  • Heat-shock protein 60-reactive CD4+CD28null T cells in patients with acute coronary syndromes. (
  • however, the effect of this protein remains to be tested using other cell systems, including immune cells in fish. (
  • Heat Shock Factor 2 Is Involved in the Upregulation of αB-Crystallin by High Extracellular Potassium1. (
  • Evidently this protein, HSP62, participates in the extracellular assembly and/or protection of the urease against inactivation in the hostile environment of the stomach. (