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.
A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION.
A class of crystallins that provides refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Beta-crystallins are similar in structure to GAMMA-CRYSTALLINS in that they both contain Greek key motifs. Beta-crystallins exist as oligomers formed from acidic (BETA-CRYSTALLIN A CHAIN) and basic (BETA-CRYSTALLIN B CHAIN) subunits.
The basic subunit of beta-crystallins.
A subclass of crystallins that found in the lens (LENS, CRYSTALLINE) of VERTEBRATES. Gamma-crystallins are similar in structure to BETA-CRYSTALLINS in that they both form into a Greek key-like structure. They are composed of monomeric subunits.
The acidic subunit of beta-crystallins.
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.
Partial or complete opacity on or in the lens or capsule of one or both eyes, impairing vision or causing blindness. The many kinds of cataract are classified by their morphology (size, shape, location) or etiology (cause and time of occurrence). (Dorland, 27th ed)
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).
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.
The core of the crystalline lens, surrounded by the cortex.
A superorder in the class CEPHALOPODA, consisting of the orders Octopoda (octopus) with over 200 species and Vampyromorpha with a single species. The latter is a phylogenetic relic but holds the key to the origins of Octopoda.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
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.
One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.
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.
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.
The family of true toads belonging to the order Anura. The genera include Bufo, Ansonia, Nectophrynoides, and Atelopus.
Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.
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.
The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.
The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The determination of the concentration of a given component in solution (the analyte) by addition of a liquid reagent of known strength (the titrant) until an equivalence point is reached (when the reactants are present in stoichiometric proportions). Often an indicator is added to make the equivalence point visible (e.g., a change in color).
Kynurenine is a metabolic product of the amino acid tryptophan, formed via the kynurenine pathway, and serves as an important intermediate in the biosynthesis of nicotinamide adenine dinucleotide (NAD+) and other neuroactive compounds, while also playing a role in immune response regulation and potential involvement in various neurological disorders.
The removal of an amino group (NH2) from a chemical compound.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
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 superorder of CEPHALOPODS comprised of squid, cuttlefish, and their relatives. Their distinguishing feature is the modification of their fourth pair of arms into tentacles, resulting in 10 limbs.
Animals that have no spinal column.
'Eye proteins' are structural or functional proteins, such as crystallins, opsins, and collagens, located in various parts of the eye, including the cornea, lens, retina, and aqueous humor, that contribute to maintaining transparency, refractive power, phototransduction, and overall integrity of the visual system.
Maf proto-oncogene protein is the major cellular homolog of the V-MAF ONCOGENE PROTEIN. It was the first of the mammalian MAF TRANSCRIPTION FACTORS identified, and it is induced in activated T-LYMPHOCYTES and regulates GENETIC TRANSCRIPTION of INTERLEUKIN-4. c-maf is frequently translocated to an immunoglobulin locus in MULTIPLE MYELOMA.
A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric a7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen.
A genus of livebearing cyprinodont fish comprising the guppy and molly. Some species are virtually all female and depend on sperm from other species to stimulate egg development. Poecilia is used in carcinogenicity studies as well as neurologic and physiologic research.
One of a group of nonenzymatic reactions in which aldehydes, ketones, or reducing sugars react with amino acids, peptides, or proteins. Food browning reactions, such as those that occur with cooking of meats, and also food deterioration reactions, resulting in decreased nutritional value and color changes, are attributed to this reaction type. The Maillard reaction is studied by scientists in the agriculture, food, nutrition, and carbohydrate chemistry fields.
Measurement of the index of refraction (the ratio of the velocity of light or other radiation in the first of two media to its velocity in the second as it passes from one into the other).
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
The diversion of RADIATION (thermal, electromagnetic, or nuclear) from its original path as a result of interactions or collisions with atoms, molecules, or larger particles in the atmosphere or other media. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
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.
Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
An integrin alpha subunit that is unique in that it does not contain an I domain, and its proteolytic cleavage site is near the middle of the extracellular portion of the polypeptide rather than close to the membrane as in other integrin alpha subunits.
Proteins prepared by recombinant DNA technology.
An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.
An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.
The sum of the weight of all the atoms in a molecule.
The portion of the crystalline lens surrounding the nucleus and bound anteriorly by the epithelium and posteriorly by the capsule. It contains lens fibers and amorphous, intercellular substance.
Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.
An interleukin-1 subtype that occurs as a membrane-bound pro-protein form that is cleaved by proteases to form a secreted mature form. Unlike INTERLEUKIN-1BETA both membrane-bound and secreted forms of interleukin-1alpha are biologically active.
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.
An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A subclass of alpha-adrenergic receptors that mediate contraction of SMOOTH MUSCLE in a variety of tissues such as ARTERIOLES; VEINS; and the UTERUS. They are usually found on postsynaptic membranes and signal through GQ-G11 G-PROTEINS.
This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.
Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.
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.
Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.
A subclass of alpha-adrenergic receptors found on both presynaptic and postsynaptic membranes where they signal through Gi-Go G-PROTEINS. While postsynaptic alpha-2 receptors play a traditional role in mediating the effects of ADRENERGIC AGONISTS, the subset of alpha-2 receptors found on presynaptic membranes signal the feedback inhibition of NEUROTRANSMITTER release.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A cell surface receptor mediating cell adhesion to the EXTRACELLULAR MATRIX and to other cells via binding to LAMININ. It is involved in cell migration, embryonic development, leukocyte activation and tumor cell invasiveness. Integrin alpha6beta1 is the major laminin receptor on PLATELETS; LEUKOCYTES; and many EPITHELIAL CELLS, and ligand binding may activate a number of signal transduction pathways. Alternative splicing of the cytoplasmic domain of the alpha6 subunit (INTEGRIN ALPHA6) results in the formation of A and B isoforms of the heterodimer, which are expressed in a tissue-specific manner.
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 degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
This intrgrin is a key component of HEMIDESMOSOMES and is required for their formation and maintenance in epithelial cells. Integrin alpha6beta4 is also found on thymocytes, fibroblasts, and Schwann cells, where it functions as a laminin receptor (RECEPTORS, LAMININ) and is involved in wound healing, cell migration, and tumor invasiveness.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
The alpha subunits of integrin heterodimers (INTEGRINS), which mediate ligand specificity. There are approximately 18 different alpha chains, exhibiting great sequence diversity; several chains are also spliced into alternative isoforms. They possess a long extracellular portion (1200 amino acids) containing a MIDAS (metal ion-dependent adhesion site) motif, and seven 60-amino acid tandem repeats, the last 4 of which form EF HAND MOTIFS. The intracellular portion is short with the exception of INTEGRIN ALPHA4.
The family of true frogs of the order Anura. The family occurs worldwide except in Antarctica.
A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.
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 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 mass spectrometric technique that is used for the analysis of a wide range of biomolecules, such as glycoalkaloids, glycoproteins, polysaccharides, and peptides. Positive and negative fast atom bombardment spectra are recorded on a mass spectrometer fitted with an atom gun with xenon as the customary beam. The mass spectra obtained contain molecular weight recognition as well as sequence information.
An integrin alpha subunit that binds COLLAGEN and LAMININ though its I domain. It combines with INTEGRIN BETA1 to form the heterodimer INTEGRIN ALPHA1BETA1.
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.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
Brain waves characterized by a relatively high voltage or amplitude and a frequency of 8-13 Hz. They constitute the majority of waves recorded by EEG registering the activity of the parietal and occipital lobes when the individual is awake, but relaxed with the eyes closed.
"Ducks" is not a recognized medical term or condition in human health; it may refer to various anatomical structures in animals, such as the ducks of the heart valves, but it does not have a standalone medical definition.
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 transparent anterior portion of the fibrous coat of the eye consisting of five layers: stratified squamous CORNEAL EPITHELIUM; BOWMAN MEMBRANE; CORNEAL STROMA; DESCEMET MEMBRANE; and mesenchymal CORNEAL ENDOTHELIUM. It serves as the first refracting medium of the eye. It is structurally continuous with the SCLERA, avascular, receiving its nourishment by permeation through spaces between the lamellae, and is innervated by the ophthalmic division of the TRIGEMINAL NERVE via the ciliary nerves and those of the surrounding conjunctiva which together form plexuses. (Cline et al., Dictionary of Visual Science, 4th ed)
An integrin alpha subunit that occurs as alternatively spliced isoforms. The isoforms are differentially expressed in specific cell types and at specific developmental stages. Integrin alpha3 combines with INTEGRIN BETA1 to form INTEGRIN ALPHA3BETA1 which is a heterodimer found primarily in epithelial cells.
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.
Deficiency of the protease inhibitor ALPHA 1-ANTITRYPSIN that manifests primarily as PULMONARY EMPHYSEMA and LIVER CIRRHOSIS.
One of the two major classes of cholinergic receptors. Nicotinic receptors were originally distinguished by their preference for NICOTINE over MUSCARINE. They are generally divided into muscle-type and neuronal-type (previously ganglionic) based on pharmacology, and subunit composition of the receptors.
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.
Drugs that selectively bind to and activate alpha adrenergic receptors.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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).
Measurement of the intensity and quality of fluorescence.
A nuclear transcription factor. Heterodimerization with RETINOID X RECEPTOR GAMMA is important to metabolism of LIPIDS. It is the target of FIBRATES to control HYPERLIPIDEMIAS.
The most diversified of all fish orders and the largest vertebrate order. It includes many of the commonly known fish such as porgies, croakers, sunfishes, dolphin fish, mackerels, TUNA, etc.
A naturally occurring prostaglandin that has oxytocic, luteolytic, and abortifacient activities. Due to its vasocontractile properties, the compound has a variety of other biological actions.
Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.
Drugs that bind to but do not activate alpha-adrenergic receptors thereby blocking the actions of endogenous or exogenous adrenergic agonists. Adrenergic alpha-antagonists are used in the treatment of hypertension, vasospasm, peripheral vascular disease, shock, and pheochromocytoma.
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.
A form of fluorescent antibody technique commonly used to detect serum antibodies and immune complexes in tissues and microorganisms in specimens from patients with infectious diseases. The technique involves formation of an antigen-antibody complex which is labeled with fluorescein-conjugated anti-immunoglobulin antibody. (From Bennington, Saunders Dictionary & Encyclopedia of Laboratory Medicine and Technology, 1984)
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
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.
A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.
The continent lying around the South Pole and the southern waters of the Atlantic, Pacific, and Indian Oceans. It includes the Falkland Islands Dependencies. (From Webster's New Geographical Dictionary, 1988, p55)
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.
Hepatocyte nuclear factor 1-alpha is a transcription factor found in the LIVER; PANCREAS; and KIDNEY that regulates HOMEOSTASIS of GLUCOSE.
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.

Alpha-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: implications for preventing irreversible thermal denaturation. (1/156)

Alpha-crystallin, the major eye-lens protein with sequence homology with heat-shock proteins (HSPs), acts like a molecular chaperone by suppressing the aggregation of damaged crystallins and proteins. To gain more insight into its chaperoning ability, we used a protease as the model system that is known to require a propeptide (intramolecular chaperone) for its proper folding. The protease ("N" state) from Conidiobolus macrosporus (NCIM 1298) unfolds at pH 2.0 ("U" state) through a partially unfolded "I" state at pH 3.5 that undergoes transition to a molten globule-(MG) like "I(A)" state in the presence of 0.5 M sodium sulfate. The thermally-stressed I(A) state showed complete loss of structure and was prone to aggregation. Alpha-crystallin was able to bind to this state and suppress its aggregation, thereby preventing irreversible denaturation of the enzyme. The alpha-crystallin-bound I(A) state exhibited native-like secondary and tertiary structure showing the interaction of alpha-crystallin with the MG state of the protease. 8-Anilinonaphthalene sulphonate (ANS) binding studies revealed the involvement of hydrophobic interactions in the formation of the complex of alpha-crystallin and protease. Refolding of acid-denatured protease by dilution to pH 7.5 resulted in aggregation of the protein. Unfolding of the protease in the presence of alpha-crystallin and its subsequent refolding resulted in the generation of a near-native intermediate with partial secondary and tertiary structure. Our studies represent the first report of involvement of a molecular chaperone-like alpha-crystallin in the unfolding and refolding of a protease. Alpha-crystallin blocks the unfavorable pathways that lead to irreversible denaturation of the alkaline protease and keeps it in a near-native, folding-competent intermediate state.  (+info)

Mass measurements of C-terminally truncated alpha-crystallins from two-dimensional gels identify Lp82 as a major endopeptidase in rat lens. (2/156)

Molecular chaperone activity of lens alpha-crystallins is reduced by loss of the C terminus. The purpose of this experiment was to 1) determine the cleavage sites produced in vitro by ubiquitous m-calpain and lens-specific Lp82 on alpha-crystallins, 2) identify alpha-crystallin cleavage sites produced in vivo during maturation and cataract formation in rat lens, and 3) estimate the relative activities of Lp82 and m-calpain by appearance of protease-specific cleavage products in vivo. Total soluble protein from young rat lens was incubated with recombinant m-calpain or Lp82 and 2 mM Ca2+. Resulting fragmented alpha-crystallins were separated by two-dimensional gel electrophoresis. Eluted alpha-crystallin spots were analyzed by mass spectrometry. Cleavage sites on insoluble alpha-crystallins were determined similarly in mature rat lens nucleus and in cataractous rat lens nucleus induced by selenite. In vitro proteolysis of alphaA-crystallin by Lp82 and m-calpain produced unique cleavage sites by removing 5 and 11 residues, respectively, from the C terminus. In vivo, the protease-specific truncations removing 5 and 11 residues from alphaA were both found in maturing lens, whereas only the truncation removing 5 residues was found in cataractous lens. Other truncation sites, common to both calpain isoforms, resulted from the removal of 8, 10, 16, 17, and 22 residues from the C terminus of alphaA. Using uniquely truncated alphaA-crystallins as in vivo markers, Lp82 and m-calpain were both found to be active during normal maturation of rat lens, whereas Lp82 seemed especially active during selenite cataract formation. These C-terminal truncations decrease chaperone activity of alpha-crystallins, possibly leading to the observed increases in insoluble proteins during aging and cataract. The methodology that allowed accurate mass measurements of proteins eluted from 2D gels should be useful to examine rapidly other post-translational modifications.  (+info)

Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. (3/156)

Hsp16.5, isolated from the hyperthermophilic Archaea Methanococcus jannaschii, is a member of the small heat-shock protein family. Small Hsps have 12- to 42-kDa subunit sizes and have sequences that are conserved among all organisms. The recently determined crystal structure of Hsp16.5 indicates that it consists discretely of 24 identical subunits. Using fluorescence resonance energy transfer, we show that at temperatures above 60 degrees C, the subunits of MjHsp16.5 freely and reversibly exchange with a rate constant of exchange at 68 degrees C of 0.067 min(-1). The subunit exchange reactions were strongly temperature-dependent, similar to the exchange reactions of the alpha-crystallins. The exchange reaction was specific to MjHsp16.5 subunits, as other sHsps such as alpha-crystallin were not structurally compatible and could not integrate into the MjHsp16.5 oligomer. In addition, we demonstrate that at temperatures as high as 70 degrees C, MjHsp16.5 retains its multimeric structure and subunit organization. Using insulin and alpha-lactalbumin as model target proteins, we also show that MjHsp16.5 at 37 degrees C is a markedly inefficient chaperone compared with other sHsps with these substrates. The results of this study support the hypothesis that MjHsp16.5 has a dynamic quaternary structure at temperatures that are physiologically relevant to M. jannaschii.  (+info)

Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle. (4/156)

The molecular events by which eccentric muscle contractions induce muscle damage and remodelling remain largely unknown. We assessed whether eccentric exercise modulates the expression of proteinases (calpains 1, 2 and 3, proteasome, cathepsin B+L), muscle structural proteins (alpha-sarcoglycan and desmin), and the expression of the heat shock proteins Hsp27 and alphaB-crystallin. Vastus lateralis muscle biopsies from twelve healthy male volunteers were obtained before, immediately after, and 1 and 14 days after a 30 min downhill treadmill running exercise. Eccentric exercise induced muscle damage as evidenced by the analysis of muscle pain and weakness, creatine kinase serum activity, myoglobinaemia and ultrastructural analysis of muscle biopsies. The calpain 3 mRNA level was decreased immediately after exercise whereas calpain 2 mRNA level was increased at day 1. Both mRNA levels returned to control values by day 14. By contrast, cathepsin B+L and proteasome enzyme activities were increased at day 14. The alpha-sarcoglycan protein level was decreased immediately after exercise and at day 1, whereas the desmin level peaked at day 14. alphaB-crystallin and Hsp27 protein levels were increased at days 1 and 14. Our results suggest that the differential expression of calpain 2 and 3 mRNA levels may be important in the process of exercise-induced muscle damage, whereas expression of alpha-sarcoglycan, desmin, alphaB-crystallin and Hsp27 may be essentially involved in the subsequent remodelling of myofibrillar structure. This remodelling response may limit the extent of muscle damage upon a subsequent mechanical stress.  (+info)

Enzyme activity after resealing within ghost erythrocyte cells, and protection by alpha-crystallin against fructose-induced inactivation. (5/156)

The role of alpha-crystallin as a molecular chaperone has been shown in many in vitro studies. In the present paper, we report on the chaperone function of alpha-crystallin within resealed erythrocyte ghosts. Eight enzymes were individually resealed within erythrocyte ghosts and assayed at zero time and at 24 h. The ghost cell suspension was separated into soluble and membrane fractions. Five of the enzymes had significantly greater enzyme activity after 24 h than the control within the soluble fractions. Fructation caused a decrease in enzyme activity (relative to the control). Resealing of alpha-crystallin within the ghost cell alongside the enzymes protected against inactivation by fructose within the soluble fraction.  (+info)

Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity. (6/156)

Several small heat shock proteins contain a well conserved alpha-crystallin domain, flanked by an N-terminal domain and a C-terminal extension, both of which vary in length and sequence. The structural and functional role of the C-terminal extension of small heat shock proteins, particularly of alphaA- and alphaB-crystallins, is not well understood. We have swapped the C-terminal extensions between alphaA- and alphaB-crystallins and generated two novel chimeric proteins, alphaABc and alphaBAc. We have investigated the domain-swapped chimeras for structural and functional alterations. We have used thermal and non-thermal models of protein aggregation and found that the chimeric alphaB with the C-terminal extension of alphaA-crystallin, alphaBAc, exhibits dramatically enhanced chaperone-like activity. Interestingly, however, the chimeric alphaA with the C-terminal extension of alphaB-crystallin, alphaABc, has almost lost its activity. Pyrene solubilization and bis-1-anilino-8-naphthalenesulfonate binding studies show that alphaBAc exhibits more solvent-exposed hydrophobic pockets than alphaA, alphaB, or alphaABc. Significant tertiary structural changes are revealed by tryptophan fluorescence and near-UV CD studies upon swapping the C-terminal extensions. The far-UV CD spectrum of alphaBAc differs from that of alphaB-crystallin whereas that of alphaABc overlaps with that of alphaA-crystallin. Gel filtration chromatography shows alteration in the size of the proteins upon swapping the C-terminal extensions. Our study demonstrates that the unstructured C-terminal extensions play a crucial role in the structure and chaperone activity, in addition to generally believed electrostatic "solubilizer" function.  (+info)

Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses. (7/156)

PURPOSE: To investigate the influence of diabetes on the cleavage of C-terminal amino acid residues of alphaA- and alphaB-crystallins in human and rat lenses. METHODS: The human lenses were diabetic or age-matched control lenses from donors 57, 59, 69, and 72 years of age. Lenses were also obtained from streptozotocin-induced diabetic rats. Individual lens crystallins in water-soluble fractions were separated by gel-permeation chromatography. The high (alphaH)- and low (alphaL)-molecular-weight fractions were analyzed by electrospray ionization mass spectrometry. RESULTS: A typical mass spectrum of alphaA-crystallin from human lenses showed intact unmodified alphaA-crystallin, truncated alphaA(1-172), and monophosphorylated alphaA-crystallin. Diabetic lenses showed nearly twofold higher levels of alphaA(1-172) than did the control lenses. Also, the alphaH fraction consistently showed significantly higher levels of alphaA(1-172) than the alphaL fraction. Human alphaB-crystallin showed no evidence of C-terminal truncation. Rat alphaA-crystallin had five C-terminal-truncated components, most of which showed substantial increases in diabetes. Truncated alphaA(1-162) appeared only in the diabetic rat lenses, suggesting specific activation of m-calpain in diabetes. alphaB-crystallin had only one C-terminal-truncated component, alphaB(1-170), which also showed increased levels in diabetes. CONCLUSIONS: These data suggest that diabetic stress causes either enzymatic or nonenzymatic cleavage of peptide bonds between specific C-terminal amino acid residues. Such truncated alpha-crystallins appear to contribute to an increased level of the alphaH fraction generally present in diabetic lenses. Loss of alphaA-crystallin chaperone activity seems to be related to truncation of the C-terminal amino acid residues.  (+info)

Small heat-shock proteins regulate membrane lipid polymorphism. (8/156)

Thermal stress in living cells produces multiple changes that ultimately affect membrane structure and function. We report that two members of the family of small heat-shock proteins (sHsp) (alpha-crystallin and Synechocystis HSP17) have stabilizing effects on model membranes formed of synthetic and cyanobacterial lipids. In anionic membranes of dimyristoylphosphatidylglycerol and dimyristoylphosphatidylserine, both HSP17 and alpha-crystallin strongly stabilize the liquid-crystalline state. Evidence from infrared spectroscopy indicates that lipid/sHsp interactions are mediated by the polar headgroup region and that the proteins strongly affect the hydrophobic core. In membranes composed of the nonbilayer lipid dielaidoylphosphatidylethanolamine, both HSP17 and alpha-crystallin inhibit the formation of inverted hexagonal structure and stabilize the bilayer liquid-crystalline state, suggesting that sHsps can modulate membrane lipid polymorphism. In membranes composed of monogalactosyldiacylglycerol and phosphatidylglycerol (both enriched with unsaturated fatty acids) isolated from Synechocystis thylakoids, HSP17 and alpha-crystallin increase the molecular order in the fluid-like state. The data show that the nature of sHsp/membrane interactions depends on the lipid composition and extent of lipid unsaturation, and that sHsps can regulate membrane fluidity. We infer from these results that the association between sHsps and membranes may constitute a general mechanism that preserves membrane integrity during thermal fluctuations.  (+info)

Crystallins are the major proteins found in the lens of the eye in vertebrates. They make up about 90% of the protein content in the lens and are responsible for maintaining the transparency and refractive properties of the lens, which are essential for clear vision. There are two main types of crystallins, alpha (α) and beta/gamma (β/γ), which are further divided into several subtypes. These proteins are highly stable and have a long half-life, which allows them to remain in the lens for an extended period of time. Mutations in crystallin genes have been associated with various eye disorders, including cataracts and certain types of glaucoma.

The crystalline lens is a biconvex transparent structure in the eye that helps to refract (bend) light rays and focus them onto the retina. It is located behind the iris and pupil and is suspended by small fibers called zonules that connect it to the ciliary body. The lens can change its shape to accommodate and focus on objects at different distances, a process known as accommodation. With age, the lens may become cloudy or opaque, leading to cataracts.

Beta-crystallins are proteins that make up a significant portion of the lens in our eyes. They are part of the crystallin family, which also includes alpha- and gamma-crystallins. These proteins are essential for maintaining the transparency and refractive properties of the eye's lens, allowing us to focus light onto the retina.

Beta-crystallins are organized into two subgroups: beta-A and beta-B. Each subgroup is made up of several different proteins called isoforms, which vary slightly in their amino acid sequences. These isoforms are produced by alternative splicing of the beta-crystallin genes during gene expression.

Mutations in the genes that encode beta-crystallins have been associated with various eye disorders, including cataracts and certain inherited forms of blindness. Cataracts are characterized by the clouding or opacification of the lens, which can lead to vision loss if not treated surgically. Inherited forms of blindness such as congenital nuclear cataracts and retinal degeneration have also been linked to mutations in beta-crystallin genes.

Overall, beta-crystallins play a crucial role in maintaining the health and function of our eyes, and their dysregulation can contribute to various eye disorders.

Beta-crystallin B chain is a protein that forms part of the beta-crystallin complex, which is a major structural component of the vertebrate eye lens. The beta-crystallins are organized into two subgroups, beta-A and beta-B, based on their structural and genetic characteristics.

The beta-B crystallin proteins are encoded by four genes (CRYBB1, CRYBB2, CRYBB3, and CRYBB4) that are located in a cluster on chromosome 22 in humans. These proteins have a molecular weight of approximately 25 kDa and are composed of four distinct domains: an N-terminal domain, two Greek key motifs, and a C-terminal domain.

The beta-crystallin B chain proteins play important roles in maintaining the transparency and refractive properties of the eye lens. Mutations in these genes have been associated with various forms of cataracts, which are clouding of the eye lens that can lead to vision loss.

Gamma-crystallins are a type of structural protein found in the lens of the eye. They are part of the crystallin family, which also includes alpha- and beta-crystallins. These proteins are responsible for maintaining the transparency and refractive properties of the lens, allowing light to pass through and focus on the retina. Mutations in the genes that encode gamma-crystallins have been associated with various forms of cataracts, which are clouding of the lens that can impair vision. Gamma-crystallins are primarily expressed during embryonic development and decrease in expression after birth.

Beta-crystallin A chain is a protein that is a component of the beta-crystallin complex, which is a major structural element of the vertebrate eye lens. The beta-crystallins are organized into two subfamilies, called beta-A and beta-B, based on their primary structures.

The beta-crystallin A chain is a polypeptide chain that contains approximately 100 amino acids and has a molecular weight of around 12 kilodaltons. It is encoded by the CRYBA1 gene in humans. The protein is characterized by four conserved domains, called Greek key motifs, which are involved in the formation of the quaternary structure of the beta-crystallin complex.

Mutations in the CRYBA1 gene have been associated with various forms of congenital cataracts, which are clouding of the eye lens that can lead to visual impairment or blindness. The precise function of beta-crystallins is not fully understood, but they are thought to play a role in maintaining the transparency and refractive properties of the eye lens.

Alpha-crystallins are small heat shock proteins found in the lens of the eye. They are composed of two subunits, alpha-A and alpha-B, which can form homo- or hetero-oligomers. Alpha-crystallins have chaperone-like activity, helping to prevent protein aggregation and maintain transparency of the lens. Additionally, they play a role in maintaining the structural integrity of the lens and protecting it from oxidative stress. Mutations in alpha-crystallin genes have been associated with certain forms of cataracts and other eye diseases.

A cataract is a clouding of the natural lens in the eye that affects vision. This clouding can cause vision to become blurry, faded, or dim, making it difficult to see clearly. Cataracts are a common age-related condition, but they can also be caused by injury, disease, or medication use. In most cases, cataracts develop gradually over time and can be treated with surgery to remove the cloudy lens and replace it with an artificial one.

Alpha-Crystallin A Chain is a protein that is part of the alpha-crystallin family, which are small heat shock proteins. These proteins play a role in protecting cells from stress and aggregation of other proteins. Alpha-Crystallin A Chain is found in various tissues, including the eye lens, where it helps maintain lens transparency and prevent cataracts. Mutations in the gene that encodes alpha-Crystallin A Chain have been associated with certain inherited forms of cataracts.

Alpha-Crystallin B chain is a protein that is a component of the eye lens. It is one of the two subunits of the alpha-crystallin protein, which is a major structural protein in the lens and helps to maintain the transparency and refractive properties of the lens. Alpha-Crystallin B chain is produced by the CRYAB gene and has chaperone-like properties, helping to prevent the aggregation of other proteins and contributing to the maintenance of lens clarity. Mutations in the CRYAB gene can lead to various eye disorders, including cataracts and certain types of glaucoma.

The lens nucleus, also known as the crystalline lens nucleus, is the central part of the crystalline lens in the eye. The crystalline lens is a biconvex structure located behind the iris and pupil, which helps to refract (bend) light rays and focus them onto the retina.

The lens nucleus is composed of densely packed lens fibers that have lost their nuclei and cytoplasm during differentiation. It is surrounded by the lens cortex, which consists of younger lens fiber cells that are still metabolically active. The lens nucleus is relatively avascular and receives its nutrients through diffusion from the aqueous humor in the anterior chamber of the eye.

The lens nucleus plays an important role in the accommodation process, which allows the eye to focus on objects at different distances. During accommodation, the ciliary muscles contract and release tension on the lens zonules, allowing the lens to become thicker and increase its curvature. This results in a decrease in the focal length of the lens and enables the eye to focus on nearby objects. The lens nucleus is more rigid than the cortex and helps maintain the shape of the lens during accommodation.

Changes in the lens nucleus are associated with several age-related eye conditions, including cataracts and presbyopia. Cataracts occur when the lens becomes cloudy or opaque, leading to a decrease in vision clarity. Presbyopia is a condition that affects the ability to focus on near objects and is caused by a hardening of the lens nucleus and a loss of elasticity in the lens fibers.

Octopodiformes is a taxonomic order that includes two main groups: octopuses (Octopoda) and vampire squids (Vampyroteuthis infernalis). This grouping is based on similarities in their fossil record and molecular data. Although they are commonly referred to as squids, vampire squids are not true squids, which belong to a different order called Teuthida.

Octopodiformes are characterized by several features, including:

1. A highly developed brain and complex nervous system.
2. Eight arms with suckers, but no tentacles.
3. The ability to change their skin color and texture for camouflage.
4. Three hearts that pump blood through their bodies.
5. Blue blood due to the copper-based protein hemocyanin.
6. A siphon used for jet propulsion and other functions, such as waste expulsion and mating.
7. Ink sacs for defense against predators.

Octopuses are known for their intelligence, problem-solving abilities, and short lifespans (usually less than two years). Vampire squids, on the other hand, live in deep ocean environments and have a unique feeding strategy that involves filtering organic matter from the water. They can also produce bioluminescent displays to confuse predators.

It is important to note that while Octopodiformes is a well-supported taxonomic group, there is still ongoing research and debate about the relationships among cephalopods (the class that includes octopuses, squids, cuttlefish, and nautiluses) and their classification.

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

Two-dimensional (2D) gel electrophoresis is a type of electrophoretic technique used in the separation and analysis of complex protein mixtures. This method combines two types of electrophoresis – isoelectric focusing (IEF) and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) – to separate proteins based on their unique physical and chemical properties in two dimensions.

In the first dimension, IEF separates proteins according to their isoelectric points (pI), which is the pH at which a protein carries no net electrical charge. The proteins are focused into narrow zones along a pH gradient established within a gel strip. In the second dimension, SDS-PAGE separates the proteins based on their molecular weights by applying an electric field perpendicular to the first dimension.

The separated proteins form distinct spots on the 2D gel, which can be visualized using various staining techniques. The resulting protein pattern provides valuable information about the composition and modifications of the protein mixture, enabling researchers to identify and compare different proteins in various samples. Two-dimensional gel electrophoresis is widely used in proteomics research, biomarker discovery, and quality control in protein production.

Adrenergic receptors are a type of G protein-coupled receptor that bind and respond to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Alpha adrenergic receptors (α-ARs) are a subtype of adrenergic receptors that are classified into two main categories: α1-ARs and α2-ARs.

The activation of α1-ARs leads to the activation of phospholipase C, which results in an increase in intracellular calcium levels and the activation of various signaling pathways that mediate diverse physiological responses such as vasoconstriction, smooth muscle contraction, and cell proliferation.

On the other hand, α2-ARs are primarily located on presynaptic nerve terminals where they function to inhibit the release of neurotransmitters, including norepinephrine. The activation of α2-ARs also leads to the inhibition of adenylyl cyclase and a decrease in intracellular cAMP levels, which can mediate various physiological responses such as sedation, analgesia, and hypotension.

Overall, α-ARs play important roles in regulating various physiological functions, including cardiovascular function, mood, and cognition, and are also involved in the pathophysiology of several diseases, such as hypertension, heart failure, and neurodegenerative disorders.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Bufonidae is a family of toads, characterized by the presence of parotoid glands that produce bufotoxins, a group of toxic secretions. These toads are found worldwide, except for Australia, New Zealand, Madagascar, and some isolated islands. They vary in size, shape, and coloration, depending on the species. Some notable members of this family include the common toad (Bufo bufo) and the Colorado River toad (Incilius alvarius). It is important to note that while these toads have toxic secretions, they are not typically harmful to humans unless ingested or if their secretions come into contact with mucous membranes or broken skin.

Hypoxia-Inducible Factor 1 (HIF-1) is a transcription factor that plays a crucial role in the body's response to low oxygen levels, also known as hypoxia. HIF-1 is a heterodimeric protein composed of two subunits: an alpha subunit (HIF-1α) and a beta subunit (HIF-1β).

The alpha subunit, HIF-1α, is the regulatory subunit that is subject to oxygen-dependent degradation. Under normal oxygen conditions (normoxia), HIF-1α is constantly produced in the cell but is rapidly degraded by proteasomes due to hydroxylation of specific proline residues by prolyl hydroxylase domain-containing proteins (PHDs). This hydroxylation reaction requires oxygen as a substrate, and under hypoxic conditions, the activity of PHDs is inhibited, leading to the stabilization and accumulation of HIF-1α.

Once stabilized, HIF-1α translocates to the nucleus, where it heterodimerizes with HIF-1β and binds to hypoxia-responsive elements (HREs) in the promoter regions of target genes. This binding results in the activation of gene transcription programs that promote cellular adaptation to low oxygen levels. These adaptive responses include increased erythropoiesis, angiogenesis, glucose metabolism, and pH regulation, among others.

Therefore, HIF-1α is a critical regulator of the body's response to hypoxia, and its dysregulation has been implicated in various pathological conditions, including cancer, cardiovascular disease, and neurodegenerative disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Aging is a complex, progressive and inevitable process of bodily changes over time, characterized by the accumulation of cellular damage and degenerative changes that eventually lead to increased vulnerability to disease and death. It involves various biological, genetic, environmental, and lifestyle factors that contribute to the decline in physical and mental functions. The medical field studies aging through the discipline of gerontology, which aims to understand the underlying mechanisms of aging and develop interventions to promote healthy aging and extend the human healthspan.

Solubility is a fundamental concept in pharmaceutical sciences and medicine, which refers to the maximum amount of a substance (solute) that can be dissolved in a given quantity of solvent (usually water) at a specific temperature and pressure. Solubility is typically expressed as mass of solute per volume or mass of solvent (e.g., grams per liter, milligrams per milliliter). The process of dissolving a solute in a solvent results in a homogeneous solution where the solute particles are dispersed uniformly throughout the solvent.

Understanding the solubility of drugs is crucial for their formulation, administration, and therapeutic effectiveness. Drugs with low solubility may not dissolve sufficiently to produce the desired pharmacological effect, while those with high solubility might lead to rapid absorption and short duration of action. Therefore, optimizing drug solubility through various techniques like particle size reduction, salt formation, or solubilization is an essential aspect of drug development and delivery.

Titrimetry is a type of analytical technique used in chemistry and medicine to determine the concentration of a substance (analyte) in a solution. It involves a controlled addition of a reagent, called a titrant, with a known concentration and volume, into the analyte solution until the reaction between them is complete. This point is commonly determined by a change in the physical or chemical properties of the solution, such as a color change, which is indicated by a visual endpoint or an electrical endpoint using a pH or redox electrode.

The volume of titrant added is then used to calculate the concentration of the analyte using the stoichiometry of the reaction and the concentration of the titrant. Titrimetry is widely used in medical laboratories for various applications, such as determining the amount of active ingredients in pharmaceuticals, measuring the strength of acid or base solutions, and assessing the hardness of water.

Kynurenine is an organic compound that is produced in the human body as part of the metabolism of the essential amino acid tryptophan. It is an intermediate in the kynurenine pathway, which leads to the production of several neuroactive compounds and NAD+, a coenzyme involved in redox reactions.

Kynurenine itself does not have any known physiological function, but some of its metabolites have been found to play important roles in various biological processes, including immune response, inflammation, and neurological function. For example, the kynurenine pathway produces several neuroactive metabolites that can act as agonists or antagonists at various receptors in the brain, affecting neuronal excitability, synaptic plasticity, and neurotransmission.

Abnormalities in the kynurenine pathway have been implicated in several neurological disorders, including depression, schizophrenia, Alzheimer's disease, and Huntington's disease. Therefore, understanding the regulation of this pathway and its metabolites has become an important area of research in neuroscience and neuropsychopharmacology.

Deamination is a biochemical process that refers to the removal of an amino group (-NH2) from a molecule, especially from an amino acid. This process typically results in the formation of a new functional group and the release of ammonia (NH3). Deamination plays a crucial role in the metabolism of amino acids, as it helps to convert them into forms that can be excreted or used for energy production. In some cases, deamination can also lead to the formation of toxic byproducts, which must be efficiently eliminated from the body to prevent harm.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

Molecular chaperones are a group of proteins that assist in the proper folding and assembly of other protein molecules, helping them achieve their native conformation. They play a crucial role in preventing protein misfolding and aggregation, which can lead to the formation of toxic species associated with various neurodegenerative diseases. Molecular chaperones are also involved in protein transport across membranes, degradation of misfolded proteins, and protection of cells under stress conditions. Their function is generally non-catalytic and ATP-dependent, and they often interact with their client proteins in a transient manner.

Decapodiformes is a taxonomic order of marine cephalopods, which includes squids, octopuses, and cuttlefish. The name "Decapodiformes" comes from the Greek words "deca," meaning ten, and "podos," meaning foot, referring to the fact that these animals have ten limbs.

However, it is worth noting that within Decapodiformes, octopuses are an exception as they only have eight arms. The other members of this order, such as squids and cuttlefish, have ten appendages, which are used for locomotion, feeding, and sensory perception.

Decapodiformes species are known for their complex behaviors, sophisticated communication systems, and remarkable adaptations that enable them to thrive in a variety of marine habitats. They play important ecological roles as both predators and prey in the ocean food chain.

I'm sorry for any confusion, but "Invertebrates" is not a medical term. It is a term used in biology to describe a vast group of animals that do not have a vertebral column or spinal cord. This includes creatures such as insects, worms, starfish, and shellfish, among many others. They are classified as invertebrates because they lack a backbone, which is a characteristic of vertebrates, or animals that include humans and other mammals, birds, reptiles, amphibians, and fish.

Eye proteins, also known as ocular proteins, are specific proteins that are found within the eye and play crucial roles in maintaining proper eye function and health. These proteins can be found in various parts of the eye, including the cornea, iris, lens, retina, and other structures. They perform a wide range of functions, such as:

1. Structural support: Proteins like collagen and elastin provide strength and flexibility to the eye's tissues, enabling them to maintain their shape and withstand mechanical stress.
2. Light absorption and transmission: Proteins like opsins and crystallins are involved in capturing and transmitting light signals within the eye, which is essential for vision.
3. Protection against damage: Some eye proteins, such as antioxidant enzymes and heat shock proteins, help protect the eye from oxidative stress, UV radiation, and other environmental factors that can cause damage.
4. Regulation of eye growth and development: Various growth factors and signaling molecules, which are protein-based, contribute to the proper growth, differentiation, and maintenance of eye tissues during embryonic development and throughout adulthood.
5. Immune defense: Proteins involved in the immune response, such as complement components and immunoglobulins, help protect the eye from infection and inflammation.
6. Maintenance of transparency: Crystallin proteins in the lens maintain its transparency, allowing light to pass through unobstructed for clear vision.
7. Neuroprotection: Certain eye proteins, like brain-derived neurotrophic factor (BDNF), support the survival and function of neurons within the retina, helping to preserve vision.

Dysfunction or damage to these eye proteins can contribute to various eye disorders and diseases, such as cataracts, age-related macular degeneration, glaucoma, diabetic retinopathy, and others.

Proto-oncogene proteins, such as c-MAF, are normal cellular proteins that play crucial roles in various biological processes including cell growth, differentiation, and apoptosis (programmed cell death). When these genes undergo mutations or become overexpressed, they can transform into oncogenes, which contribute to the development of cancer.

The c-MAF protein is a transcription factor that regulates gene expression by binding to specific DNA sequences. It belongs to the basic region-leucine zipper (bZIP) family of transcription factors and plays essential roles in immune system function, cell cycle regulation, and tumorigenesis.

In cancer, c-MAF can contribute to tumor development and progression by promoting cell proliferation, survival, and angiogenesis (the formation of new blood vessels). Dysregulation of c-MAF has been implicated in various types of cancer, such as multiple myeloma, lung cancer, and breast cancer.

The alpha7 nicotinic acetylcholine receptor (α7nAChR) is a type of cholinergic receptor found in the nervous system that is activated by the neurotransmitter acetylcholine. It is a ligand-gated ion channel that is widely distributed throughout the central and peripheral nervous systems, including in the hippocampus, cortex, thalamus, and autonomic ganglia.

The α7nAChR is composed of five subunits arranged around a central pore, and it has a high permeability to calcium ions (Ca2+). When acetylcholine binds to the receptor, it triggers a conformational change that opens the ion channel, allowing Ca2+ to flow into the cell. This influx of Ca2+ can activate various intracellular signaling pathways and have excitatory or inhibitory effects on neuronal activity, depending on the location and function of the receptor.

The α7nAChR has been implicated in a variety of physiological processes, including learning and memory, attention, sensory perception, and motor control. It has also been studied as a potential therapeutic target for various neurological and psychiatric disorders, such as Alzheimer's disease, schizophrenia, and pain.

"Poecilia" is not a medical term, but a biological genus name. It belongs to the family Poeciliidae and includes several species of small freshwater fish commonly known as mollies, guppies, and swordtails. These fish are often kept in aquariums as pets. They are livebearers, which means they give birth to live young rather than laying eggs.

I'm sorry for any confusion, but the term "Maillard reaction" is not a medical definition, but rather a chemical one. It refers to a specific type of chemical reaction between amino acids and reducing sugars that gives browned food its distinctive flavor. This reaction is named after French chemist Louis-Camille Maillard, who first described it in the early 20th century.

In culinary terms, the Maillard reaction is responsible for the browning of many foods, such as the crust of bread, the surface of roasted meats, and the flavor of seared vegetables. The reaction occurs when food is cooked or heated at high temperatures, causing amino acids and sugars to react and form new compounds that contribute to the food's color, taste, and aroma.

While the Maillard reaction is not a medical term, it is worth noting that some of the compounds formed during this reaction have been linked to potential health effects. For example, acrylamide, a compound that can form during high-temperature cooking of certain foods, has been classified as a probable human carcinogen by the International Agency for Research on Cancer (IARC). However, more research is needed to fully understand the health implications of these compounds and their role in the diet.

Refractometry is a medical laboratory technique used to measure the refractive index of a substance, typically a liquid. The refractive index is the ratio of the speed of light in a vacuum to its speed in the substance being measured. In a clinical setting, refractometry is often used to determine the concentration of total solids in a fluid, such as urine or serum, by measuring the angle at which light passes through the sample. This information can be useful in the diagnosis and monitoring of various medical conditions, including dehydration, kidney disease, and diabetes. Refractometry is also used in the field of optometry to measure the refractive error of the eye, or the amount and type of correction needed to provide clear vision.

Protein denaturation is a process in which the native structure of a protein is altered, leading to loss of its biological activity. This can be caused by various factors such as changes in temperature, pH, or exposure to chemicals or radiation. The three-dimensional shape of a protein is crucial for its function, and denaturation causes the protein to lose this shape, resulting in impaired or complete loss of function. Denaturation is often irreversible and can lead to the aggregation of proteins, which can have negative effects on cellular function and can contribute to diseases such as Alzheimer's and Parkinson's.

Radiation scattering is a physical process in which radiation particles or waves deviate from their original direction due to interaction with matter. This phenomenon can occur through various mechanisms such as:

1. Elastic Scattering: Also known as Thomson scattering or Rayleigh scattering, it occurs when the energy of the scattered particle or wave remains unchanged after the collision. In the case of electromagnetic radiation (e.g., light), this results in a change of direction without any loss of energy.
2. Inelastic Scattering: This type of scattering involves an exchange of energy between the scattered particle and the target medium, leading to a change in both direction and energy of the scattered particle or wave. An example is Compton scattering, where high-energy photons (e.g., X-rays or gamma rays) interact with charged particles (usually electrons), resulting in a decrease in photon energy and an increase in electron kinetic energy.
3. Coherent Scattering: In this process, the scattered radiation maintains its phase relationship with the incident radiation, leading to constructive and destructive interference patterns. An example is Bragg scattering, which occurs when X-rays interact with a crystal lattice, resulting in diffraction patterns that reveal information about the crystal structure.

In medical contexts, radiation scattering can have both beneficial and harmful effects. For instance, in diagnostic imaging techniques like computed tomography (CT) scans, radiation scattering contributes to image noise and reduces contrast resolution. However, in radiation therapy for cancer treatment, controlled scattering of therapeutic radiation beams can help ensure that the tumor receives a uniform dose while minimizing exposure to healthy tissues.

Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry (MALDI-MS) is a type of mass spectrometry that is used to analyze large biomolecules such as proteins and peptides. In this technique, the sample is mixed with a matrix compound, which absorbs laser energy and helps to vaporize and ionize the analyte molecules.

The matrix-analyte mixture is then placed on a target plate and hit with a laser beam, causing the matrix and analyte molecules to desorb from the plate and become ionized. The ions are then accelerated through an electric field and into a mass analyzer, which separates them based on their mass-to-charge ratio.

The separated ions are then detected and recorded as a mass spectrum, which can be used to identify and quantify the analyte molecules present in the sample. MALDI-MS is particularly useful for the analysis of complex biological samples, such as tissue extracts or biological fluids, because it allows for the detection and identification of individual components within those mixtures.

Integrin α3β1 is a type of cell surface receptor that is widely expressed in various tissues, including epithelial and endothelial cells. It is composed of two subunits, α3 and β1, which form a heterodimeric complex that plays a crucial role in cell-matrix adhesion and signaling.

Integrin α3β1 binds to several extracellular matrix proteins, such as laminin, fibronectin, and collagen IV, and mediates various cellular functions, including cell migration, proliferation, differentiation, and survival. It also participates in intracellular signaling pathways that regulate cell behavior and tissue homeostasis.

Mutations in the genes encoding integrin α3β1 have been associated with several human diseases, including blistering skin disorders, kidney disease, and cancer. Therefore, understanding the structure, function, and regulation of integrin α3β1 is essential for developing new therapeutic strategies to treat these conditions.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Integrin α4 (also known as CD49d or ITGA4) is a subunit of integrin proteins, which are heterodimeric transmembrane receptors that mediate cell-cell and cell-extracellular matrix interactions. Integrin α4 typically pairs with β1 (CD29 or ITGB1) or β7 (ITGB7) subunits to form integrins α4β1 and α4β7, respectively.

Integrin α4β1, also known as very late antigen-4 (VLA-4), is widely expressed on various hematopoietic cells, including lymphocytes, monocytes, eosinophils, and basophils. It plays crucial roles in the adhesion, migration, and homing of these cells to secondary lymphoid organs, as well as in the recruitment of immune cells to inflammatory sites. Integrin α4β1 binds to its ligands, vascular cell adhesion molecule-1 (VCAM-1) and fibronectin, via the arginine-glycine-aspartic acid (RGD) motif.

Integrin α4β7, on the other hand, is primarily expressed on gut-homing lymphocytes and interacts with mucosal addressin cell adhesion molecule-1 (MAdCAM-1), a protein mainly found in the high endothelial venules of intestinal Peyer's patches and mesenteric lymph nodes. This interaction facilitates the trafficking of immune cells to the gastrointestinal tract, where they participate in immune responses against pathogens and maintain gut homeostasis.

In summary, Integrin α4 is a crucial subunit of integrins that mediates cell adhesion, migration, and homing to specific tissues through its interactions with various ligands. Dysregulation of integrin α4 has been implicated in several pathological conditions, including inflammatory diseases, autoimmune disorders, and cancer metastasis.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Integrin α6 (also known as CD49f) is a type of integrin, which is a heterodimeric transmembrane receptor that mediates cell-cell and cell-extracellular matrix (ECM) interactions. Integrins play crucial roles in various biological processes such as cell adhesion, migration, proliferation, differentiation, and survival.

Integrin α6 is a 130 kDa glycoprotein that pairs with integrin β1, β4 or β5 to form three distinct heterodimeric complexes: α6β1, α6β4, and α6β5. Among these, the α6β4 integrin is the most extensively studied. It specifically binds to laminins in the basement membrane and plays essential roles in maintaining epithelial tissue architecture and function.

The α6β4 integrin has a unique structure with an extended cytoplasmic domain of β4 that can interact with intracellular signaling molecules, cytoskeletal proteins, and other adhesion receptors. This interaction allows the formation of stable adhesion complexes called hemidesmosomes, which anchor epithelial cells to the basement membrane and provide mechanical stability to tissues.

Mutations in integrin α6 or its partners can lead to various human diseases, including epidermolysis bullosa, a group of inherited skin disorders characterized by fragile skin and mucous membranes that blister and tear easily.

Integrin α5β1, also known as very late antigen-5 (VLA-5) or fibronectin receptor, is a heterodimeric transmembrane receptor protein composed of two subunits: α5 and β1. This integrin is widely expressed in various cell types, including endothelial cells, smooth muscle cells, and fibroblasts.

Integrin α5β1 plays a crucial role in mediating cell-matrix adhesion by binding to the arginine-glycine-aspartic acid (RGD) sequence present in the extracellular matrix protein fibronectin. The interaction between integrin α5β1 and fibronectin is essential for various biological processes, such as cell migration, proliferation, differentiation, and survival. Additionally, this integrin has been implicated in several pathological conditions, including tumor progression, angiogenesis, and fibrosis.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

The crystalline lens in the eye is composed of three main parts: the capsule, the cortex, and the nucleus. The lens cortex is the outer layer of the lens, located between the capsule and the nucleus. It is made up of proteins and water, and its primary function is to help refract (bend) light rays as they pass through the eye, contributing to the focusing power of the eye.

The cortex is more flexible than the central nucleus, allowing it to change shape and adjust the focus of the eye for different distances. However, with age, the lens cortex can become less elastic, leading to presbyopia, a common age-related condition that affects the ability to focus on close objects. Additionally, changes in the lens cortex have been associated with cataracts, a clouding of the lens that can impair vision.

Integrin α4β1, also known as Very Late Antigen-4 (VLA-4), is a heterodimeric transmembrane receptor protein composed of two subunits, α4 and β1. It is involved in various cellular activities such as adhesion, migration, and signaling. This integrin plays a crucial role in the immune system by mediating the interaction between leukocytes (white blood cells) and the endothelial cells that line blood vessels. The activation of Integrin α4β1 allows leukocytes to roll along and then firmly adhere to the endothelium, followed by their migration into surrounding tissues, particularly during inflammation and immune responses. Additionally, Integrin α4β1 also interacts with extracellular matrix proteins such as fibronectin and helps regulate cell survival, proliferation, and differentiation in various cell types.

Interleukin-1 alpha (IL-1α) is a member of the interleukin-1 cytokine family, which plays a crucial role in the regulation of inflamation and immune responses. IL-1α is primarily produced by activated macrophages, epithelial cells, and fibroblasts. It is a potent proinflammatory cytokine that binds to the interleukin-1 receptor (IL-1R) and activates signaling pathways leading to the expression of genes involved in inflammation, fever, and cellular activation. IL-1α is involved in various physiological processes such as hematopoiesis, bone remodeling, and response to infection or injury. Dysregulation of IL-1α has been implicated in several pathological conditions including autoimmune diseases, atherosclerosis, and cancer.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

Integrin α2β1, also known as very late antigen-2 (VLA-2) or laminin receptor, is a heterodimeric transmembrane receptor protein composed of α2 and β1 subunits. It belongs to the integrin family of adhesion molecules that play crucial roles in cell-cell and cell-extracellular matrix (ECM) interactions.

Integrin α2β1 is widely expressed on various cell types, including fibroblasts, endothelial cells, smooth muscle cells, and some hematopoietic cells. It functions as a receptor for several ECM proteins, such as collagens (type I, II, III, and V), laminin, and fibronectin. The binding of integrin α2β1 to these ECM components mediates cell adhesion, migration, proliferation, differentiation, and survival, thereby regulating various physiological and pathological processes, such as tissue repair, angiogenesis, inflammation, and tumor progression.

In addition, integrin α2β1 has been implicated in several diseases, including fibrosis, atherosclerosis, and cancer. Therefore, targeting this integrin with therapeutic strategies may provide potential benefits for treating these conditions.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Alpha-1 adrenergic receptors (also known as α1-adrenoreceptors) are a type of G protein-coupled receptor that binds catecholamines, such as norepinephrine and epinephrine. These receptors are primarily found in the smooth muscle of various organs, including the vasculature, heart, liver, kidneys, gastrointestinal tract, and genitourinary system.

When an alpha-1 adrenergic receptor is activated by a catecholamine, it triggers a signaling cascade that leads to the activation of phospholipase C, which in turn activates protein kinase C and increases intracellular calcium levels. This ultimately results in smooth muscle contraction, increased heart rate and force of contraction, and vasoconstriction.

Alpha-1 adrenergic receptors are also found in the central nervous system, where they play a role in regulating wakefulness, attention, and anxiety. There are three subtypes of alpha-1 adrenergic receptors (α1A, α1B, and α1D), each with distinct physiological roles and pharmacological properties.

In summary, alpha-1 adrenergic receptors are a type of G protein-coupled receptor that binds catecholamines and mediates various physiological responses, including smooth muscle contraction, increased heart rate and force of contraction, vasoconstriction, and regulation of wakefulness and anxiety.

Integrin α5 (also known as CD49e) is a subunit of the heterodimeric integrin receptor called very late antigen-5 (VLA-5). Integrins are transmembrane adhesion receptors that play crucial roles in cell-cell and cell-extracellular matrix interactions. The α5β1 integrin, formed by the association of α5 and β1 subunits, specifically recognizes and binds to fibronectin, a major extracellular matrix protein. This binding event is essential for various biological processes such as cell migration, proliferation, differentiation, and survival.

In summary, Integrin alpha5 (α5) is an essential subunit of the α5β1 integrin receptor that mediates cell-fibronectin interactions and contributes to several vital cellular functions.

Integrin α1β1, also known as Very Late Antigen-1 (VLA-1) or CD49a/CD29, is a heterodimeric transmembrane receptor protein composed of α1 and β1 subunits. It belongs to the integrin family of adhesion molecules that play crucial roles in cell-cell and cell-extracellular matrix (ECM) interactions.

Integrin α1β1 is primarily expressed on various cell types, including fibroblasts, endothelial cells, smooth muscle cells, and some immune cells. This integrin binds to several ECM proteins, such as collagens (type I, II, III, IV), laminin, and fibronectin, mediating cell adhesion, migration, proliferation, differentiation, and survival. Additionally, α1β1 integrin has been implicated in various physiological and pathological processes, such as tissue repair, fibrosis, and tumor progression.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

Calpains are a family of calcium-dependent cysteine proteases that play important roles in various cellular processes, including signal transduction, cell death, and remodeling of the cytoskeleton. They are present in most tissues and can be activated by an increase in intracellular calcium levels. There are at least 15 different calpain isoforms identified in humans, which are categorized into two groups based on their calcium requirements for activation: classical calpains (calpain-1 and calpain-2) and non-classical calpains (calpain-3 to calpain-15). Dysregulation of calpain activity has been implicated in several pathological conditions, such as neurodegenerative diseases, muscular dystrophies, and cancer.

Alpha-2 adrenergic receptors are a type of G protein-coupled receptor that binds catecholamines, such as norepinephrine and epinephrine. These receptors are widely distributed in the central and peripheral nervous system, as well as in various organs and tissues throughout the body.

Activation of alpha-2 adrenergic receptors leads to a variety of physiological responses, including inhibition of neurotransmitter release, vasoconstriction, and reduced heart rate. These receptors play important roles in regulating blood pressure, pain perception, and various cognitive and emotional processes.

There are several subtypes of alpha-2 adrenergic receptors, including alpha-2A, alpha-2B, and alpha-2C, which may have distinct physiological functions and be targeted by different drugs. For example, certain medications used to treat hypertension or opioid withdrawal target alpha-2 adrenergic receptors to produce their therapeutic effects.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Integrin α6β1, also known as CD49f/CD29, is a heterodimeric transmembrane receptor protein composed of α6 and β1 subunits. It is widely expressed in various tissues, including epithelial cells, endothelial cells, fibroblasts, and hematopoietic cells. Integrin α6β1 plays a crucial role in cell-matrix adhesion, particularly to the laminin component of the extracellular matrix (ECM). This receptor is involved in various biological processes such as cell migration, proliferation, differentiation, and survival. Additionally, integrin α6β1 has been implicated in tumor progression, metastasis, and drug resistance in certain cancers.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Integrin α6β4 is a type of cell surface receptor that is composed of two subunits, α6 and β4. It is also known as CD49f/CD104. This integrin is primarily expressed in epithelial cells and plays important roles in cell adhesion, migration, and signal transduction.

Integrin α6β4 specifically binds to laminin-332 (also known as laminin-5), a component of the basement membrane, and forms a stable anchorage complex that links the cytoskeleton to the extracellular matrix. This interaction is critical for maintaining the integrity of epithelial tissues and regulating cell behavior during processes such as wound healing and tissue regeneration.

Mutations in the genes encoding integrin α6β4 have been associated with various human diseases, including epidermolysis bullosa, a group of inherited skin disorders characterized by fragile skin and blistering. Additionally, integrin α6β4 has been implicated in cancer progression and metastasis, as its expression is often upregulated in tumor cells and contributes to their invasive behavior.

Aldehyde dehydrogenase (ALDH) is a class of enzymes that play a crucial role in the metabolism of alcohol and other aldehydes in the body. These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using nicotinamide adenine dinucleotide (NAD+) as a cofactor.

There are several isoforms of ALDH found in different tissues throughout the body, with varying substrate specificities and kinetic properties. The most well-known function of ALDH is its role in alcohol metabolism, where it converts the toxic aldehyde intermediate acetaldehyde to acetate, which can then be further metabolized or excreted.

Deficiencies in ALDH activity have been linked to a number of clinical conditions, including alcohol flush reaction, alcohol-induced liver disease, and certain types of cancer. Additionally, increased ALDH activity has been associated with chemotherapy resistance in some cancer cells.

Integrins are a family of cell-surface receptors that play crucial roles in various biological processes, including cell adhesion, migration, and signaling. Integrin alpha chains are one of the two subunits that make up an integrin heterodimer, with the other subunit being an integrin beta chain.

Integrin alpha chains are transmembrane glycoproteins consisting of a large extracellular domain, a single transmembrane segment, and a short cytoplasmic tail. The extracellular domain contains several domains that mediate ligand binding, while the cytoplasmic tail interacts with various cytoskeletal proteins and signaling molecules to regulate intracellular signaling pathways.

There are 18 different integrin alpha chains known in humans, each of which can pair with one or more beta chains to form distinct integrin heterodimers. These heterodimers exhibit unique ligand specificities and functions, allowing them to mediate diverse cell-matrix and cell-cell interactions.

In summary, integrin alpha chains are essential subunits of integrin receptors that play crucial roles in regulating cell adhesion, migration, and signaling by mediating interactions between cells and their extracellular environment.

"Ranidae" is not a medical term. It is a biological term that refers to a family of frogs and toads, commonly known as "true frogs." These amphibians are characterized by their long legs, webbed feet, and the ability to live both in water and on land. Some examples of ranids include the American bullfrog and the green frog.

Integrins are a type of cell-adhesion molecule that play a crucial role in cell-cell and cell-extracellular matrix (ECM) interactions. They are heterodimeric transmembrane receptors composed of non-covalently associated α and β subunits, which form more than 24 distinct integrin heterodimers in humans.

Integrins bind to specific ligands, such as ECM proteins (e.g., collagen, fibronectin, laminin), cell surface molecules, and soluble factors, through their extracellular domains. The intracellular domains of integrins interact with the cytoskeleton and various signaling proteins, allowing them to transduce signals from the ECM into the cell (outside-in signaling) and vice versa (inside-out signaling).

These molecular interactions are essential for numerous biological processes, including cell adhesion, migration, proliferation, differentiation, survival, and angiogenesis. Dysregulation of integrin function has been implicated in various pathological conditions, such as cancer, fibrosis, inflammation, and autoimmune diseases.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Fast Atom Bombardment (FAB) Mass Spectrometry is a technique used for determining the mass of ions in a sample. In FAB-MS, the sample is mixed with a matrix material and then bombarded with a beam of fast atoms, usually xenon or cesium. This bombardment leads to the formation of ions from the sample which can then be detected and measured using a mass analyzer. The resulting mass spectrum provides information about the molecular weight and structure of the sample molecules. FAB-MS is particularly useful for the analysis of large, thermally labile, or polar molecules that may not ionize well by other methods.

Integrin α1 (also known as ITGA1 or CD49a) is a subunit of a heterodimeric integrin receptor, specifically the collagen receptor α1β1. Integrins are transmembrane proteins that play crucial roles in cell-cell and cell-extracellular matrix (ECM) adhesion, signaling, migration, proliferation, and differentiation. The α1β1 integrin binds to various collagen types, such as collagens I, II, III, and V, and mediates cellular responses upon binding to these ECM components.

The gene encoding Integrin α1 is located on chromosome 5 (5q31) in humans. Mutations in the ITGA1 gene can lead to various diseases, including leukocyte adhesion deficiency type II and some forms of epidermolysis bullosa.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.

Alpha rhythm is a type of brain wave that is typically observed in the electroencephalogram (EEG) of normal, awake individuals when they have their eyes closed. It is characterized by sinusoidal waves with a frequency range of 8-13 Hz and is most prominent over the occipital region of the head, which is located at the back of the skull above the brain's visual cortex.

Alpha rhythm is typically associated with relaxed wakefulness, and its presence may indicate that an individual is awake but not engaged in any mentally demanding tasks. It can be blocked or suppressed by various stimuli, such as opening one's eyes, hearing a loud noise, or engaging in mental activity.

Disruptions in alpha rhythm have been observed in various neurological and psychiatric conditions, including epilepsy, dementia, depression, and anxiety disorders. However, more research is needed to fully understand the clinical significance of these abnormalities.

"Ducks" is not a medical term. It is a common name used to refer to a group of birds that belong to the family Anatidae, which also includes swans and geese. Some ducks are hunted for their meat, feathers, or down, but they do not have any specific medical relevance. If you have any questions about a specific medical term or concept, I would be happy to help if you could provide more information!

Immunoblotting, also known as western blotting, is a laboratory technique used in molecular biology and immunogenetics to detect and quantify specific proteins in a complex mixture. This technique combines the electrophoretic separation of proteins by gel electrophoresis with their detection using antibodies that recognize specific epitopes (protein fragments) on the target protein.

The process involves several steps: first, the protein sample is separated based on size through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Next, the separated proteins are transferred onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric field. The membrane is then blocked with a blocking agent to prevent non-specific binding of antibodies.

After blocking, the membrane is incubated with a primary antibody that specifically recognizes the target protein. Following this, the membrane is washed to remove unbound primary antibodies and then incubated with a secondary antibody conjugated to an enzyme such as horseradish peroxidase (HRP) or alkaline phosphatase (AP). The enzyme catalyzes a colorimetric or chemiluminescent reaction that allows for the detection of the target protein.

Immunoblotting is widely used in research and clinical settings to study protein expression, post-translational modifications, protein-protein interactions, and disease biomarkers. It provides high specificity and sensitivity, making it a valuable tool for identifying and quantifying proteins in various biological samples.

The cornea is the clear, dome-shaped surface at the front of the eye. It plays a crucial role in focusing vision. The cornea protects the eye from harmful particles and microorganisms, and it also serves as a barrier against UV light. Its transparency allows light to pass through and get focused onto the retina. The cornea does not contain blood vessels, so it relies on tears and the fluid inside the eye (aqueous humor) for nutrition and oxygen. Any damage or disease that affects its clarity and shape can significantly impact vision and potentially lead to blindness if left untreated.

Integrin α3 (also known as ITGA3) is a subunit of a type of cell-surface receptor called an integrin. Integrins are involved in cell-cell and cell-extracellular matrix (ECM) interactions, and play important roles in various biological processes such as cell adhesion, migration, and survival.

Integrin α3 combines with the β1 subunit to form the integrin heterodimer α3β1, which is widely expressed in many tissues including epithelial cells, endothelial cells, and fibroblasts. Integrin α3β1 binds to various ECM proteins such as laminin-5, fibronectin, and collagen IV, and mediates cell adhesion and migration on these substrates.

Mutations in the ITGA3 gene have been associated with several human genetic disorders, including epidermolysis bullosa with pyloric atresia (EB-PA), a severe form of inherited skin fragility disorder, and Adams-Oliver syndrome, a rare genetic disorder characterized by scalp defects and limb abnormalities.

DNA primers are short single-stranded DNA molecules that serve as a starting point for DNA synthesis. They are typically used in laboratory techniques such as the polymerase chain reaction (PCR) and DNA sequencing. The primer binds to a complementary sequence on the DNA template through base pairing, providing a free 3'-hydroxyl group for the DNA polymerase enzyme to add nucleotides and synthesize a new strand of DNA. This allows for specific and targeted amplification or analysis of a particular region of interest within a larger DNA molecule.

Alpha 1-Antitrypsin (AAT) deficiency is a genetic disorder that results from insufficient levels of the protective protein AAT in the blood and lungs. This protein is produced by the liver and helps to protect the lungs from damage caused by inflammation and the action of enzymes, such as neutrophil elastase, that are released during the immune response.

In people with AAT deficiency, the lack of adequate AAT levels leads to an uncontrolled increase in neutrophil elastase activity, which can cause damage to lung tissue and result in emphysema, a condition characterized by shortness of breath, coughing, and wheezing. Additionally, some individuals with AAT deficiency may develop liver disease due to the accumulation of abnormal AAT proteins in liver cells.

There are different variants or genotypes associated with AAT deficiency, with the most common and severe form being the PiZZ genotype. This variant is caused by mutations in the SERPINA1 gene, which encodes for the AAT protein. Individuals who inherit two copies of this mutated gene (one from each parent) will have very low levels of AAT in their blood and are at increased risk of developing emphysema and liver disease.

Diagnosis of AAT deficiency typically involves measuring AAT levels in the blood and performing genetic testing to identify specific variants of the SERPINA1 gene. Treatment may include lifestyle modifications, such as smoking cessation, bronchodilators, and corticosteroids to manage lung symptoms, as well as augmentation therapy with intravenous infusions of AAT protein to help slow disease progression in individuals with severe deficiency. Liver transplantation may be considered for those with advanced liver disease.

Nicotinic receptors are a type of ligand-gated ion channel receptor that are activated by the neurotransmitter acetylcholine and the alkaloid nicotine. They are widely distributed throughout the nervous system and play important roles in various physiological processes, including neuronal excitability, neurotransmitter release, and cognitive functions such as learning and memory. Nicotinic receptors are composed of five subunits that form a ion channel pore, which opens to allow the flow of cations (positively charged ions) when the receptor is activated by acetylcholine or nicotine. There are several subtypes of nicotinic receptors, which differ in their subunit composition and functional properties. These receptors have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and schizophrenia.

Species specificity is a term used in the field of biology, including medicine, to refer to the characteristic of a biological entity (such as a virus, bacterium, or other microorganism) that allows it to interact exclusively or preferentially with a particular species. This means that the biological entity has a strong affinity for, or is only able to infect, a specific host species.

For example, HIV is specifically adapted to infect human cells and does not typically infect other animal species. Similarly, some bacterial toxins are species-specific and can only affect certain types of animals or humans. This concept is important in understanding the transmission dynamics and host range of various pathogens, as well as in developing targeted therapies and vaccines.

Adrenergic alpha-agonists are a type of medication that binds to and activates adrenergic alpha receptors, which are found in the nervous system and other tissues throughout the body. These receptors are activated naturally by chemicals called catecholamines, such as norepinephrine and epinephrine (also known as adrenaline), that are released in response to stress or excitement.

When adrenergic alpha-agonists bind to these receptors, they mimic the effects of catecholamines and cause various physiological responses, such as vasoconstriction (constriction of blood vessels), increased heart rate and force of heart contractions, and relaxation of smooth muscle in the airways.

Adrenergic alpha-agonists are used to treat a variety of medical conditions, including hypertension (high blood pressure), glaucoma, nasal congestion, and attention deficit hyperactivity disorder (ADHD). Examples of adrenergic alpha-agonists include phenylephrine, clonidine, and guanfacine.

It's important to note that adrenergic alpha-agonists can have both beneficial and harmful effects, depending on the specific medication, dosage, and individual patient factors. Therefore, they should only be used under the guidance of a healthcare professional.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

PPAR-alpha (Peroxisome Proliferator-Activated Receptor alpha) is a type of nuclear receptor protein that functions as a transcription factor, regulating the expression of specific genes involved in lipid metabolism. It plays a crucial role in the breakdown of fatty acids and the synthesis of high-density lipoproteins (HDL or "good" cholesterol) in the liver. PPAR-alpha activation also has anti-inflammatory effects, making it a potential therapeutic target for metabolic disorders such as diabetes, hyperlipidemia, and non-alcoholic fatty liver disease (NAFLD).

I'm sorry for any confusion, but "Perciformes" is not a medical term. It is a term used in the field of biology, specifically in taxonomy and ichthyology (the study of fish). Perciformes is an order of ray-finned bony fishes that includes over 10,000 species, making it the largest order of vertebrates. Examples of fish within this order include perch, sea bass, sunfish, and tuna.

Dinoprost is a synthetic form of prostaglandin F2α, which is a naturally occurring hormone-like substance in the body. It is used in veterinary medicine as a uterotonic agent to induce labor and abortion in various animals such as cows and pigs. In human medicine, it may be used off-label for similar purposes, but its use must be under the close supervision of a healthcare provider due to potential side effects and risks.

It is important to note that Dinoprost is not approved by the FDA for use in humans, and its availability may vary depending on the country or region. Always consult with a licensed healthcare professional before using any medication, including Dinoprost.

Isoelectric focusing (IEF) is a technique used in electrophoresis, which is a method for separating proteins or other molecules based on their electrical charges. In IEF, a mixture of ampholytes (molecules that can carry both positive and negative charges) is used to create a pH gradient within a gel matrix. When an electric field is applied, the proteins or molecules migrate through the gel until they reach the point in the gradient where their net charge is zero, known as their isoelectric point (pI). At this point, they focus into a sharp band and stop moving, resulting in a highly resolved separation of the different components based on their pI. This technique is widely used in protein research for applications such as protein identification, characterization, and purification.

Adrenergic alpha-antagonists, also known as alpha-blockers, are a class of medications that block the effects of adrenaline and noradrenaline at alpha-adrenergic receptors. These receptors are found in various tissues throughout the body, including the smooth muscle of blood vessels, the heart, the genitourinary system, and the eyes.

When alpha-blockers bind to these receptors, they prevent the activation of the sympathetic nervous system, which is responsible for the "fight or flight" response. This results in a relaxation of the smooth muscle, leading to vasodilation (widening of blood vessels), decreased blood pressure, and increased blood flow.

Alpha-blockers are used to treat various medical conditions, such as hypertension (high blood pressure), benign prostatic hyperplasia (enlarged prostate), pheochromocytoma (a rare tumor of the adrenal gland), and certain types of glaucoma.

Examples of alpha-blockers include doxazosin, prazosin, terazosin, and tamsulosin. Side effects of alpha-blockers may include dizziness, lightheadedness, headache, weakness, and orthostatic hypotension (a sudden drop in blood pressure upon standing).

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

The Fluorescent Antibody Technique (FAT), Indirect is a type of immunofluorescence assay used to detect the presence of specific antigens in a sample. In this method, the sample is first incubated with a primary antibody that binds to the target antigen. After washing to remove unbound primary antibodies, a secondary fluorescently labeled antibody is added, which recognizes and binds to the primary antibody. This indirect labeling approach allows for amplification of the signal, making it more sensitive than direct methods. The sample is then examined under a fluorescence microscope to visualize the location and amount of antigen based on the emitted light from the fluorescent secondary antibody. It's commonly used in diagnostic laboratories for detection of various bacteria, viruses, and other antigens in clinical specimens.

Proteomics is the large-scale study and analysis of proteins, including their structures, functions, interactions, modifications, and abundance, in a given cell, tissue, or organism. It involves the identification and quantification of all expressed proteins in a biological sample, as well as the characterization of post-translational modifications, protein-protein interactions, and functional pathways. Proteomics can provide valuable insights into various biological processes, diseases, and drug responses, and has applications in basic research, biomedicine, and clinical diagnostics. The field combines various techniques from molecular biology, chemistry, physics, and bioinformatics to study proteins at a systems level.

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

Sequence analysis in the context of molecular biology and genetics refers to the systematic examination and interpretation of DNA or protein sequences to understand their features, structures, functions, and evolutionary relationships. It involves using various computational methods and bioinformatics tools to compare, align, and analyze sequences to identify patterns, conserved regions, motifs, or mutations that can provide insights into molecular mechanisms, disease associations, or taxonomic classifications.

In a medical context, sequence analysis can be applied to diagnose genetic disorders, predict disease susceptibility, inform treatment decisions, and guide research in personalized medicine. For example, analyzing the sequence of a gene associated with a particular inherited condition can help identify the specific mutation responsible for the disorder, providing valuable information for genetic counseling and family planning. Similarly, comparing the sequences of pathogens from different patients can reveal drug resistance patterns or transmission dynamics, informing infection control strategies and therapeutic interventions.

The Antarctic regions typically refer to the geographical areas surrounding the continent of Antarctica, including the Southern Ocean and various subantarctic islands. These regions are known for their extreme cold, ice-covered landscapes, and unique wildlife adapted to survive in harsh conditions. The Antarctic region is also home to important scientific research stations focused on topics such as climate change, marine life, and space exploration. It's worth noting that the Antarctic Treaty System governs these regions, which prohibits military activity, mineral mining, nuclear testing, and nuclear waste disposal, and promotes scientific research and cooperation among nations.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

Hepatocyte Nuclear Factor 1-alpha (HNF1A) is a transcription factor that plays a crucial role in the development and function of the liver. It belongs to the family of winged helix transcription factors and is primarily expressed in the hepatocytes, which are the major cell type in the liver.

HNF1A regulates the expression of various genes involved in glucose and lipid metabolism, bile acid synthesis, and drug metabolism. Mutations in the HNF1A gene have been associated with maturity-onset diabetes of the young (MODY), a form of diabetes that is typically inherited in an autosomal dominant manner and often diagnosed in early adulthood. These mutations can lead to impaired insulin secretion and decreased glucose tolerance, resulting in the development of diabetes.

In addition to its role in diabetes, HNF1A has also been implicated in liver diseases such as nonalcoholic fatty liver disease (NAFLD) and alcoholic liver disease (ALD). Dysregulation of HNF1A has been shown to contribute to the development and progression of these conditions by altering the expression of genes involved in lipid metabolism, inflammation, and fibrosis.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

... and iota-crystallins. For example, alpha, beta, and delta crystallins are found in avian and reptilian lenses, and the alpha, ... alpha-crystallin being found in small amounts in tissues outside the lens. Alpha-crystallin has chaperone-like properties ... Crystallins at the U.S. National Library of Medicine Medical Subject Headings (MeSH) alpha-Crystallins at the U.S. National ... Crystallins from a vertebrate eye lens are classified into three main types: alpha, beta and gamma crystallins. These ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Gamma-crystallin D is a protein that in humans is encoded by the CRYGD gene. Crystallins are separated into two classes: taxon- ... "Entrez Gene: CRYGD crystallin, gamma D". Graw J (1998). "The crystallins: genes, proteins and diseases". Biol. Chem. 378 (11): ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Beta-crystallin A3 is a protein that in humans is encoded by the CRYBA1 gene. Crystallins are separated into two classes: taxon ... This gene, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, ...
Bennardini F, Wrzosek A, Chiesi M (August 1992). "Alpha B-crystallin in cardiac tissue. Association with actin and desmin ... a conserved alpha helix rod, a variable non alpha helix head, and a carboxy-terminal tail. Desmin, as all intermediate ... The rod domain consists of 308 amino acids with parallel alpha helical coiled coil dimers and three linkers to disrupt it. The ... Desmin has been shown to interact with desmoplakin and αB-crystallin. Desmin was first described in 1976, first purified in ...
MP26 and alpha-crystallin are palmitoylated". FEBS Lett. 262 (2): 356-8. doi:10.1016/0014-5793(90)80228-B. PMID 2335219. S2CID ... Prabhakaram M, Katz ML, Ortwerth BJ (1997). "Glycation mediated crosslinking between alpha-crystallin and MP26 in intact lens ... 1991). "Lens protein gene expression: alpha-crystallins and MIP". Lens and Eye Toxicity Research. 8 (2-3): 319-44. PMID 1911643 ...
Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. These ... Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is ... the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Alpha B chain crystallins (αBC) can be induced by heat shock, ... Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Beta-crystallin B3 is a protein that in humans is encoded by the CRYBB3 gene. Crystallins are separated into two classes: taxon ... Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Gamma-crystallin B is a protein that in humans is encoded by the CRYGB gene. Crystallins are separated into two classes: taxon- ... Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Gamma-crystallin A is a protein that in humans is encoded by the CRYGA gene. Crystallins are separated into two classes: taxon- ... Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Beta-crystallin B1 is a protein that in humans is encoded by the CRYBB1 gene. Variants in CRYBB1 are associated with autosomal ... Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Beta-crystallin A4 is a protein that in humans is encoded by the CRYBA4 gene. Crystallins are separated into two classes: taxon ... Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none ...
Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins ... Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is ... the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an ... Alpha-crystallin A chain is a protein that in humans is encoded by the CRYAA gene. Crystallins are separated into two classes: ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Beta-crystallin B2 is a protein that in humans is encoded by the CRYBB2 gene. Crystallins are separated into two classes: taxon ... 2005). "Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in BetaB2-crystallin by simulation and experiment ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Gamma-crystallin S is a protein that in humans is encoded by the CRYGS gene. Crystallins are separated into two classes: taxon- ... "Entrez Gene: CRYGS crystallin, gamma S". Human CRYGS genome location and CRYGS gene details page in the UCSC Genome Browser. ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Crystallin, gamma C, also known as CRYGC, is a protein which in humans is encoded by the CRYGC gene. Crystallins are separated ... Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are organized in a ...
Structurally, this family is characterised by the presence of a conserved C-terminal domain, alpha-crystallin domain, of about ... Merck KB, de Jong WW, Bloemendal H, Groenen PJ (1994). "Structure and modifications of the junior chaperone alpha-crystallin. ...
"Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the ... "Beta-amyloid exhibits antagonistic effects on alpha 7 nicotinic acetylcholine receptors in orchestrated manner". Journal of ...
Kappe G, Franck E, Verschuure P, Boelens WC, Leunissen JA, de Jong WW (Jun 2003). "The human genome encodes 10 alpha-crystallin ... "Entrez Gene: HSPB6 heat shock protein, alpha-crystallin-related, B6". Kato K, Goto S, Inaguma Y, Hasegawa K, Morishita R, Asano ... "Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin". J. Biol. Chem. 269 (21 ... Fontaine JM, Sun X, Benndorf R, Welsh MJ (2005). "Interactions of HSP22 (HSPB8) with HSP20, alphaB-crystallin, and HSPB3". ...
"Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin". Biochemical and Biophysical ...
Shum WK, Maleknia SD, Downard KM (September 2005). "Onset of oxidative damage in alpha-crystallin by radical probe mass ... Downard KM, Kokabu Y, Ikeguchi M, Akashi S (November 2011). "Homology-modelled structure of the βB2B3-crystallin heterodimer ...
Characterization of lens alpha-crystallin tryptophan microenvironments by room temperature phosphorescence spectroscopy. ... The anaerobic photolysis of lens alpha-crystallin: evidence for triplet state mediated photodamage. Photochem Photobiol. 1990 ... Phosphorescence measurements of calf gamma-II, III, and IV crystallins at 77 and 293 K. Exp Eye Res. 1989 May;48(5):627-39. ...
Bsibsi M, Holtman IR, Gerritsen WH, Eggen BJ, Boddeke E, van der Valk P, van Noort JM, Amor S (2013). "Alpha-B-Crystallin ...
... alpha-crystallin, with molten globule states of bovine alpha-lactalbumin". The Journal of Biological Chemistry. 272 (44): 27722 ... March 1995). "Lactation is disrupted by alpha-lactalbumin deficiency and can be restored by human alpha-lactalbumin gene ... alpha-Lactalbumin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Human LALBA genome location and ... Davies MS, West LF, Davis MB, Povey S, Craig RK (July 1987). "The gene for human alpha-lactalbumin is assigned to chromosome ...
DeJong W.W.; Zweers A.; Goodman M. (1981). "Relationship of aardvark to elephants, hyraxes and sea cows from alpha-crystallin ... DeJong, W.W.; J.A.M. Leunissen & G.J. Wistow (1993). "Eye lens crystallins and the phylogeny of placental orders: evidence for ...
Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Advances in Protein ... "Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle". The Journal of Biological ... Hsp27 is a chaperone of the sHsp (small heat shock protein) group among α-crystallin, Hsp20, and others. The common functions ... Hsp27 is rather unique among sHsps in that its α-crystallin domain contains a cysteine residue at its dimer interface, which ...
"Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin". Biochemical and Biophysical ... coassembly with alpha-crystallin but not with vimentin". Experimental Eye Research. 60 (2): 181-192. doi:10.1016/S0014-4835(95) ...
Goenka S, Raman B, Ramakrishna T, Rao CM (2001). "Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a ... The former class is also called phylogenetically-restricted crystallins. This gene encodes a taxon-specific crystallin protein ... "Entrez Gene: CRYZ crystallin, zeta (quinone reductase)". Human CRYZ genome location and CRYZ gene details page in the UCSC ... Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major ...
Bsibsi M, Holtman IR, Gerritsen WH, Eggen BJ, Boddeke E, van der Valk P, van Noort JM, Amor S (Sep 2013). "Alpha-B-Crystallin ...
... microcornea and corneal opacity and novel mutation in the alpha A crystallin gene (CRYAA)". Am. J. Med. Genet. A. 146 (7): 833- ...
Alpha crystallin (α4- crystallin) or hspb4 is involved in the development of lens in Zebrafish as it is expressed in response ... Expression of the hspb4 gene, which codes for alpha crystallin, increases considerably in the lens in response to heat shock. ... Hsp90, hsp84, hsp70, hsp27, hsp20, and alpha B crystallin all have been reported as having roles in the cardiovasculature. ... A conserved protein binding domain of approximately 80 amino-acid alpha crystallins are known as small heat shock proteins ( ...
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Alpha]B-crystallin genotype has impact on the multiple sclerosis phenotype T van Veen 1 , L van Winsen, J B A Crusius, N F ... Alpha]B-crystallin genotype has impact on the multiple sclerosis phenotype T van Veen et al. Neurology. 2003. . ... Association of Alpha B-Crystallin (CRYAB) genotypes with breast cancer susceptibility in Taiwan. Su CH, Liu LC, Hsieh YH, Wang ... Alpha]B-crystallin is a candidate autoantigen in MS, and there are three polymorphisms in the promoter region of the encoding ...
Is the heat-shock protein alphaB-crystallin a useful biomarker in breast cancer prognosis? ... Association of alphaβ-crystallin With Clinopathological Features and Other Markers. The distribution of the examined markers is ... alphaB-crystallin * Treatment 0.72 0.75 alphaB-crystallin neg vs. pos in non-paclitaxel treated. 1.21. 0.48-3.01. 0.88. 0.35- ... Table 6. Association of alphaB-crystallin protein expression with all examined markers. alphaB-crystallin. p-value (Pearson chi ...
"γ-crystallins are highly specialized proteins of the vertebrate eye lens where they survive without turnover under high ... Zebrafish alpha-crystallins: protein structure and chaperone-like activity compared to their mammalian orthologs. Dahlman JM, ... Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins. Zhao H, Chen Y, Rezabkova L, Wu Z, Wistow G, ... Interaction of heat treated γ-crystallins with human αB-crystallin. Proteins (0.5 mg/mL) were held at temperatures (Tc) that ...
Crystallin-alpha C Monoclonal Antibody , G-AB-05655 MSRP: Was: Now: $163.00 - $465.00 ... Beta tubulins are one of two core protein families (alpha and beta tubulins) that heterodimerize and assemble to... ... COL2A1 Monoclonal Antibody , G-AB-05735 , Gentaur AntibodiesOverview: This gene encodes the alpha-1 chain of type II collagen, ... AFP Monoclonal Antibody , G-AB-07643 , Gentaur AntibodiesOverview: This gene encodes alpha-fetoprotein, a major plasma protein ...
Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1. ... Solution Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1. ...
The scientists found that as cloudiness increased, alpha-crystallin in the lenses decreased. Alpha-crystallin levels also ... The researchers determined alpha-crystallins light-scattering ability and then used animal models to develop a technique for ... The researchers honed in on a lens protein called alpha-crystallin, which is known to bind to other lens proteins when they ... People are born with a fixed amount of alpha-crystallin, so if the supply becomes depleted due to radiation exposure, smoking, ...
Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin. Proc Natl Acad Sci U S A. 2001; ...
... or the higher rates of alpha-crystallin protein loss, compared to those lenses with the highest baseline levels of alpha- ... The level of alpha-crystallin in the eye declines as cataract progresses. Left: The eye of a patient with an early cataract. ... Alpha-crystallin appears to be depleted in the process of acting as a chaperone, so supplementing it before levels get too low ... But since alpha-crystallin protein is itself too large to be delivered via eyedrops, NIH-funded researchers are trying to ...
5. Expression of alpha-crystallins in human sebaceous carcinoma of the eyelid.. Rigas PK; Kase S; Rao NA. Eur J Ophthalmol; ...
Expression of alpha-crystallins in human sebaceous carcinoma of the eyelid.. Rigas PK; Kase S; Rao NA. Eur J Ophthalmol; 2009; ...
In in-vitro studies, the beta crystallin was more resistant to degradation than were mixtures of alpha and gamma crystallins. ... The loss of alpha crystallin from the isoelectric focusing pattern was due to aggregation to higher molecular weight particles ... A very high molecular weight fraction contained alpha crystallin material. Rabbit lenses were exposed in-vitro and in-vivo to ... of the lenses incubated for 30 minutes at 45 degrees showed a definite loss in the lowest points of the alpha crystallin ...
Alpha B-crystallin interactswith intermediate filaments in response to stress. J. Cell Sci., 110: 2759-2769.. PubMed ... Intermediate filament interactions can be altered by HSP27 and αB-crystallin. J. Cell Sci., 112: 2099-2112.. PubMedDirect Link ...
Highly specific and rigorously validated in-house, β-crystallin B1/crybb1 Rabbit Antibody (CST #95666) is ready to ship. ... which also includes alpha- and gamma-crystallins. Crystallins are expressed at very high levels in the retinal lens and form ... β-crystallin B1, encoded by crybb1, is a member of the β-crystallins, one of three major crystallin types encoded by the ... β-crystallin B1/crybb1 Rabbit Antibody recognizes endogenous levels of total β-crystallin B1 protein. ...
... calcineurin induces cardiac endoplasmic reticulum stress and protects against apoptosis that is mediated by alpha-crystallin-B ... alpha-((2S, 5R)-4-allyl-2, 5-dimethyl-1-piperazinyl)-3-methoxybenzyl]-N, N-diethylbenzamide] and heroin. J. Pharmacol. Exp. ... alpha-(4-allyl-2,5-dimethyl-1-piperazinyl)-3-methoxybenzyl)-N,N-diethylbenzamide. ...
Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins ... Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is ... the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an ... Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family ...
Hsp22 is an alpha-crystallin-related chaperone (small hsp) that localizes to the mitochondrial matrix. The hsp70 and hsp22 ...
... accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and ...
... alpha]A-crystallin binding protein 1, is a negative regulator of the chondrocyte-specific enhancer of the [alpha]1(II) collagen ... alpha]1(X) in Figure 5 in MCB 22:4256-4267, 2002. Similarly, duplicate copies of 18S EtBr stained control bands were used in ... alpha]2(XI) collagen gene,Molecular and Cellular Biology 22:4256-4267, 2002; and Ying Liu, Haochuan Li, Kazuhiro Tanaka, ... alpha]2(XI) collagen gene, Journal of Biological Chemistry (JBC) 275:12712-12718, 2000. ...
... accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and ...
Crystallins, alpha. alpha Crystallin. alpha Crystallins. alpha-Crystallin. Tree number(s):. D12.776.306.366.100. D12.776. ... alpha-Crystallins Entry term(s). Crystallins, alpha alpha Crystallin alpha Crystallins alpha-Crystallin ... The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits. ... The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits.. ...
Alpha]B-crystallin genotype has impact on the multiple sclerosis phenotype. Neurology 2003 Nov 61 (9): 1245-9. van Veen T, van ...
alpha-Crystallins [D12.776.580.157] * alpha-Crystallin A Chain [D12.776.580.157.149] * alpha-Crystallin B Chain [D12.776. ... 2003; for ALPHA-CRYSTALLIN see CRYSTALLINS 1982-2002. History Note. 2003; for ALPHA-CRYSTALLIN use CRYSTALLINS 1982-2002. Date ... Crystallins [D12.776.306.366] * alpha-Crystallins [D12.776.306.366.100] * alpha-Crystallin A Chain [D12.776.306.366.100.149] ... Crystallins, alpha alpha-Crystallin Registry Number. 0. Previous Indexing. Crystallins (1965-2002). Public MeSH Note. ...
alpha-Crystallins [D12.776.580.157] * alpha-Crystallin A Chain [D12.776.580.157.149] * alpha-Crystallin B Chain [D12.776. ... 2003; for ALPHA-CRYSTALLIN see CRYSTALLINS 1982-2002. History Note. 2003; for ALPHA-CRYSTALLIN use CRYSTALLINS 1982-2002. Date ... Crystallins [D12.776.306.366] * alpha-Crystallins [D12.776.306.366.100] * alpha-Crystallin A Chain [D12.776.306.366.100.149] ... Crystallins, alpha alpha-Crystallin Registry Number. 0. Previous Indexing. Crystallins (1965-2002). Public MeSH Note. ...
... protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin ...
Studies of alpha-B crystallin in zebrafish could ultimately lead to improved treatment for cataracts and heart disease. ...
Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the ... The Aggregation of αB-Crystallin under Crowding Conditions Is Prevented by αA-Crystallin: Implications for α-Crystallin ... Crystallins, cataract, and dynamic lens proteostasis. A commentary on P.W.N. Schmid, N.C.H. Lim, C. Peters, K.C. Back, B. ... Amyloid fibrils from readily available sources: milk casein and lens crystallin proteins. Ecroyd, Heath; Garvey, Megan; Thorn, ...
Alpha-B crystallin-related late-onset myopathy Current Synonym true false 3760299010 Alpha-B crystallin-related late-onset ... Alpha-B crystallin-related late-onset myopathy (disorder). Code System Preferred Concept Name. Alpha-B crystallin-related late- ...
crystallin alpha B [Source:HGNC Symbol;.... 32243_g_at. 1410. CRYAB. crystallin alpha B [Source:HGNC Symbol;.... ...
  • miR-491 exerts its role by directly targeting alphaB-crystallin (CRYAB) in OS. (cusabio.com)
  • Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. (expasy.org)
  • Beta- and gamma-crystallins (such as CRYGC) are similar in sequence, structure and domains topology, and thus have been grouped together as a protein superfamily called βγ-Crystallins. (wikipedia.org)
  • More proteins containing βγ-crystallin domains have now been characterized as calcium binding proteins with Greek key motif as a novel calcium-binding motif. (wikipedia.org)
  • The crystallins of different groups of organisms are related to a large number of different proteins, with those from birds and reptiles related to lactate dehydrogenase and argininosuccinate lyase, those of mammals to alcohol dehydrogenase and quinone reductase, and those of cephalopods to glutathione S-transferase and aldehyde dehydrogenase. (wikipedia.org)
  • The α-crystallin family and βγ-crystallins compose the major family of proteins present in the crystalline lens. (wikipedia.org)
  • Alpha-crystallin occurs as large aggregates, comprising two types of related subunits (A and B) that are highly similar to the small (15-30kDa) heat shock proteins (sHsps), particularly in their C-terminal halves. (wikipedia.org)
  • Alpha-crystallin has chaperone-like properties including the ability to prevent the precipitation of denatured proteins and to increase cellular tolerance to stress. (wikipedia.org)
  • The concentration of beta crystallin proteins was reduced by in-vivo exposures. (cdc.gov)
  • 11 As the turnover of crystallins is negligible, 11 these proteins persist in the lens throughout life, 12 their transparency depending on their structural integrity. (arvojournals.org)
  • In addition, several other intrinsic neuroprotective pathways have been described, including those involving small heat shock proteins such as α-crystallins. (eneuro.org)
  • After demonstrating the paracrine protective effect of αA-crystallins secreted by primary Müller glial cells (MGCs), we purified and characterized recombinant αA-crystallin proteins mutated on the T148 regulatory residue. (eneuro.org)
  • Altogether, our study demonstrates the paracrine role of αA-crystallin in the central nervous system as well as the therapeutic potential of functionally enhanced αA-crystallin recombinant proteins to prevent metabolic-stress induced neurodegeneration. (eneuro.org)
  • The protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. (thermofisher.cn)
  • Bioinformatics analysis showed that the proteins encoded by these five HcHSPs contained typical α-crystallin domains. (bvsalud.org)
  • So far, it has been demonstrated that crystallin β b2 (crybb2) may be a neurite-promoting factor. (wikipedia.org)
  • In anatomy, a crystallin is a water-soluble structural protein found in the lens and the cornea of the eye accounting for the transparency of the structure. (wikipedia.org)
  • Since it has been shown that lens injury may promote nerve regeneration, crystallin has been an area of neural research. (wikipedia.org)
  • The main function of crystallins at least in the lens of the eye is probably to increase the refractive index while not obstructing light. (wikipedia.org)
  • It has become clear that crystallins may have several metabolic and regulatory functions, both within the lens and in other parts of the body. (wikipedia.org)
  • Whether these crystallins are products of a fortuitous accident of evolution, in that these particular enzymes happened to be transparent and highly soluble, or whether these diverse enzymatic activities are part of the protective machinery of the lens, is an active research topic. (wikipedia.org)
  • Crystallins from a vertebrate eye lens are classified into three main types: alpha, beta and gamma crystallins. (wikipedia.org)
  • Divergence probably occurred prior to evolution of the eye lens, alpha-crystallin being found in small amounts in tissues outside the lens. (wikipedia.org)
  • Calf lens homogenates were incubated at temperatures ranging from 37 to 45 degrees-C. Isoelectric focused gel analysis of the lenses incubated for 30 minutes at 45 degrees showed a definite loss in the lowest points of the alpha crystallin components. (cdc.gov)
  • The synthesis of lens crystallins by the fiber cells starts in the embryonic period and continues throughout life. (arvojournals.org)
  • αA-crystallin is a chaperone protein that has been long known for its critical role in the lens proteostasis. (eneuro.org)
  • Although the presence of α-crystallins was initially described and studied in the ocular lens, their expression is not limited to this tissue. (eneuro.org)
  • α-crystallin is an abundant constituent of the eye lens of most vertebrate species. (expasy.org)
  • Xla.Tg(Xtr.lmo2:Katushka;cryga:Venous) EXRC This Tg X. laevis line carries a 4755bp X. tropicalis sequence for lmo2 promoter driving the red fluorescent protein, Katushka , and a second cassette as marker for integration, gamma crystallin ( cryga ) driving Venus expression in lens, and was made by the EXRC. (xenbase.org)
  • For example, alpha, beta, and delta crystallins are found in avian and reptilian lenses, and the alpha, beta, and gamma families are found in the lenses of all other vertebrates. (wikipedia.org)
  • Beta- and gamma- crystallin form a separate family. (wikipedia.org)
  • Structurally, beta and gamma crystallins are composed of two similar domains which, in turn, are each composed of two similar motifs with the two domains connected by a short connecting peptide. (wikipedia.org)
  • However, beta crystallin is an oligomer, composed of a complex group of molecules, whereas gamma crystallin is a simpler monomer. (wikipedia.org)
  • In in-vitro studies, the beta crystallin was more resistant to degradation than were mixtures of alpha and gamma crystallins. (cdc.gov)
  • line with 205bp rat ( Rno ) elastase ( elas ) promoter driving dominant negative (DN) thyroid receptor alpha ( thra ) (also known as TRDN) fused ( - ) to GFP, and carrying a gamma crystallin ( cryga ) GFP cassette as marker of integration. (xenbase.org)
  • We further demonstrated the therapeutic potential of a functionally enhanced αA-crystallin recombinant protein in promoting neuronal survival. (eneuro.org)
  • This is supported by the observation that alpha-crystallin mutations show an association with cataract formation. (wikipedia.org)
  • The N-terminal domain of alpha-crystallin is not necessary for dimerisation or chaperone activity, but appears to be required for the formation of higher order aggregates. (wikipedia.org)
  • In the current study, we explored how mutation of this residue affected αA-crystallin chaperone function, secretion, and paracrine protective function using primary glial and neuronal cells. (eneuro.org)
  • The broad chaperone and cytoprotective functions of αA-crystallin make it a very attractive target in the context of the dire need for novel protective therapies for neurodegenerative diseases. (eneuro.org)
  • Structure and modifications of the junior chaperone alpha-crystallin. (expasy.org)
  • The measured time correlation functions from alpha crystallin suspensions will be compared with Langevin dynamics simulations. (lu.se)
  • The loss of alpha crystallin from the isoelectric focusing pattern was due to aggregation to higher molecular weight particles which could not enter the gel. (cdc.gov)
  • A very high molecular weight fraction contained alpha crystallin material. (cdc.gov)
  • Proteína ácida que se encuentra en el SISTEMA NEUROENDOCRINO y que funciona como una chaperona molecular para la PROPROTEÍNA-CONVERTASA 2. (bvsalud.org)
  • and delta-crystallin is found exclusively in reptiles and birds. (wikipedia.org)
  • The current study demonstrates that αA-crystallin secreted by Müller glial cells (MGCs) plays a paracrine protective role for retinal neurons. (eneuro.org)
  • Some crystallins are active enzymes, while others lack activity but show homology to other enzymes. (wikipedia.org)
  • We recently identified residue threonine 148 (T148) and its phosphorylation as a critical regulator of αA-crystallin intrinsic neuroprotective function. (eneuro.org)
  • Our previous work has shown that phosphorylation on threonine 148 (T148) is a critical regulator of the cytoprotective function of αA-crystallin. (eneuro.org)
  • XPCS, dynamic light scattering and neutron spin echo measurements will be compiled to yield a comparison of concentrated alpha crystalline suspensions with hard sphere colloid theory over a wide range of length and time scales. (lu.se)
  • While initially considered as a purely intracellular mechanism, both αA-crystallins and αB-crystallins have been recently reported to be secreted by glial cells. (eneuro.org)
  • Dr. Datiles and Dr. Walter J. Stark, professor and chief of the cataract and corneal diseases program of the Wilmer Eye Institute, studied this loss of alpha-crystallin over time by measuring levels of the protein every six months among 45 people, age 34 to 79, (66 eyes). (nih.gov)
  • The loss of alpha crystallin from the isoelectric focusing pattern was due to aggregation to higher molecular weight particles which could not enter the gel. (cdc.gov)
  • People are born with a fixed amount of alpha-crystallin, so if the supply becomes depleted due to radiation exposure, smoking, diabetes or other causes, a cataract is more likely to form. (nih.gov)
  • The researchers determined alpha-crystallin's light-scattering ability and then used animal models to develop a technique for detecting and measuring the amount of alpha-crystallin in lenses. (nih.gov)
  • We're born with a finite amount of alpha-crystallin, which doesn't pose a problem in our early years. (nih.gov)
  • Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. (nih.gov)
  • Alpha and beta families are further divided into acidic and basic groups. (maayanlab.cloud)
  • Crystallin genes: lens specificity of the murine alpha A-crystallin gene. (nih.gov)
  • Alpha]B-crystallin is a candidate autoantigen in MS, and there are three polymorphisms in the promoter region of the encoding gene (CRYAB): at positions -C249G, -C650G, and -A652G. (nih.gov)
  • From NCBI Gene: Mammalian lens crystallins are divided into alpha, beta, and gamma families. (nih.gov)
  • and Ying Liu, Haochuan Li, Kazuhiro Tanaka, Noriyuki Tsumaki, and Yoshihiko Yamada, ``Identification of an enhancer sequence with the first intron required for cartilage-specific transcription of the [alpha]2(XI) collagen gene,' Journal of Biological Chemistry (JBC) 275:12712-12718, 2000. (nih.gov)
  • To gain insight into important, evolutionarily conserved properties and functionality of γ-crystallins, zebrafish (Danio rerio) γM2b and γM7 were compared with mouse γS and human γD. (nih.gov)
  • Studies of alpha-B crystallin in zebrafish could ultimately lead to improved treatment for cataracts and heart disease. (vumc.org)
  • Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). (maayanlab.cloud)
  • The level of alpha-crystallin in the eye declines as cataract progresses. (nih.gov)
  • Crystallins, cataract, and dynamic lens proteostasis. (bvsalud.org)
  • In addition, fish γM-crystallins do not conserve the paired tryptophan residues found in each domain in mammalian γ-crystallins and in the related β-crystallins. (nih.gov)
  • The scientists found that as cloudiness increased, alpha-crystallin in the lenses decreased. (nih.gov)
  • Alpha-crystallin levels also decreased as the participants' ages increased, even when the lenses were still transparent. (nih.gov)
  • Calf lens homogenates were incubated at temperatures ranging from 37 to 45 degrees-C. Isoelectric focused gel analysis of the lenses incubated for 30 minutes at 45 degrees showed a definite loss in the lowest points of the alpha crystallin components. (cdc.gov)
  • the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. (nih.gov)
  • Here, we perform mass spectrometry experiments to study αB-crystallin and extract detailed information as to its oligomeric distribution and exchange of subunits under a range of conditions. (ox.ac.uk)
  • Western blot analysis of extracts from rat eye, mouse eye, and mouse lung using β-crystallin B1/crybb1 Rabbit Antibody (upper) and α-Actinin (D6F6) XP ® Rabbit mAb #6487 (lower). (cellsignal.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Hexosaminidase A Alpha (HEXa) in serum, plasma, tissue homogenates and other biological fluids. (tuberculosistest.net)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human RAR Related Orphan Receptor Alpha (RORa) in Tissue homogenates, cell lysates and other biological fluids. (2sars.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human RAR Related Orphan Receptor Alpha (RORa) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (2sars.com)
  • Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. (maayanlab.cloud)
  • For this reason, quantitative studies of the molecular chaperone αB-crystallin, which populates a range of interconverting oligomeric states, have been difficult, and the physicochemical basis for its polydispersity has remained unknown. (ox.ac.uk)
  • 5. Expression of alpha-crystallins in human sebaceous carcinoma of the eyelid. (nih.gov)
  • He also used duplicate copies of bands to falsely represent the RNA expression in ATDC5 cells grown under different conditions for either collagen Type II in Figure 3, MCB 2000 or collagen [alpha]1(X) in Figure 5 in MCB 22:4256-4267, 2002. (nih.gov)
  • Hsp22 is an alpha-crystallin-related chaperone (small hsp) that localizes to the mitochondrial matrix. (nih.gov)
  • Description: A sandwich ELISA kit for detection of Hexosaminidase A Alpha from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (tuberculosistest.net)
  • Description: A sandwich ELISA kit for detection of RAR Related Orphan Receptor Alpha from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (2sars.com)
  • alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. (nih.gov)
  • Alpha-crystallin appears to be depleted in the process of acting as a chaperone, so supplementing it before levels get too low may be a viable prevention strategy. (nih.gov)
  • Monitoring the prevention of amyloid fibril formation by alpha-crystallin. (bvsalud.org)
  • Preliminary evidence from human lens studies in the laboratory suggests that alpha-crystallins are involved in presbyopia. (nih.gov)
  • By virtue of its capacity to synthesize alpha crystallins, the lens epithelium may become strongly antigenic. (medscape.com)
  • The researchers measured and monitored alpha-crystallin levels using a fiber optic-based technology called dynamic light scattering, initially developed to conduct fluid physics experiments in space. (nih.gov)
  • This study demonstrates, for the first time, the functional role of αB-crystallin in epithelial-mesenchymal transition (EMT) of retinal pigment epithelium (RPE) cells and its association with subretinal fibrosis. (ca.gov)
  • Even in mammals, γ-crystallins have high contents of sulfur-containing methionine and cysteine, but this reaches extremes in fish γM-crystallins with up to 15% Met. (nih.gov)
  • A very high molecular weight fraction contained alpha crystallin material. (cdc.gov)

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