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SHsp
The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a family of heat shock proteins. Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp). Amongst them is a family of proteins with an average molecular weight of 20 kDa, known as the hsp20 proteins. These seem to act as protein chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterised by the presence of a conserved C-terminal domain, alpha-crystallin domain, of about 100 residues. Recently, small heat shock proteins (sHSPs) were found in marine viruses (cyanophages). Function and regulation Hsp20, like all heat shock proteins, is in abundance when cells are under stressed conditions. Hsp20 is known to be expressed in many human tiss ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Family
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. The most important of these is sequence similarity (usually amino-acid sequence), since it is the strictest indicator of homology and therefore the clearest indicator of common ancestry. A fairly well developed framework exists for evaluating the significance of similarity between a group of sequences using sequence alignment methods. Proteins that do not share a common ancestor are very unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein famil ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HSPB3
Heat shock protein beta-3 (HspB3) also known as heat shock 27kDa protein 3 is a protein that in humans is encoded by the HSPB3 gene. Function This gene encodes a muscle-specific small heat shock protein. Clinical significance A mutation In biology, a mutation is an alteration in the nucleic acid sequence of the genome of an organism, virus, or extrachromosomal DNA. Viral genomes contain either DNA or RNA. Mutations result from errors during DNA or viral replication, m ... in this gene is the cause of autosomal dominant distal hereditary motor neuropathy type 2C. References Further reading * * * * * * * {{gene-5-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HSPB8
Heat shock protein beta-8 is a protein that in humans is encoded by the ''HSPB8'' gene. Interactions HSPB8 has been shown to interact with: * HSPB2, and * Hsp27 Heat shock protein 27 (Hsp27) also known as heat shock protein beta-1 (HSPB1) is a protein that in humans is encoded by the ''HSPB1'' gene. Hsp27 is a chaperone of the sHsp (small heat shock protein) group among α-crystallin, Hsp20, and others. .... Clinical importance Mutations in this gene have been associated with an autosomal dominant rimmed vacuolar myopathyAl-Tahan S, Weiss L, Yu H, Tang S, Saporta M, Vihola A, Mozaffar T, Udd B, Kimonis V (2019) New family with HSPB8-associated autosomal dominant rimmed vacuolar myopathy. Neurol Genet 5(4):e349 The clinical features of this condition are distal and proximal myopathy. MRI show severe relatively symmetric multifocal fatty degenerative changes within the muscles. Muscle biopsy shows rimmed vacuoles, muscle fiber atrophy and endomysial fibrosis. References ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HSPB7
Heat Shock Protein Family B (small) member 7 (HSPB7) in humans is a protein encoded by a gene of the same name with four exons that is located on chromosome 1p36.13.,. HSPB7 contains 170 amino acids and has a molecular weight of 18,611 Da. HSPB7 is a member of human small heat shock protein (HSPB) family, which contains eleven family members of chaperone proteins. HSPB7 and its gene pair SRARP are located 5 kb apart on the opposite strands of chromosome 1p36.13. Expression and molecular function HSPB7 is widely expressed throughout the body and its highest expression is observed in the cardiac tissue ,. HSPB protein family, including HSPB7, act protectively on aggregation of several proteins containing an extended polyglutamine (polyQ) stretch that are linked to a variety of neurodegenerative diseases. Among these proteins, HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of chaperones. In addition, HSPB7 protein contains a HSP20 domain and strongly ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HSPB6
Heat shock protein beta-6 (HSPB6) is a protein that in humans is encoded by the ''HSPB6'' gene. HSPB6 is a 17-kDa member of the heat shock family of proteins. HSPB6 was first identified in 1994 when it was isolated from rat and human skeletal muscle as a complex with HSPB1 (also known as HSP27) and HSPB5 (also known as αB-crystallin). HSPB6 is expressed in multiple tissues; however, HSPB6 is most highly and constitutively expressed in vascular, airway, colonic, bladder, uterine smooth muscle, cardiac muscle and skeletal muscle. HSPB6 has specific functions for vasodilation, platelet function, and insulin resistance Insulin resistance (IR) is a pathological condition in which cells fail to respond normally to the hormone insulin. Insulin is a hormone that facilitates the transport of glucose from blood into cells, thereby reducing blood glucose (blood sugar ... and in smooth and cardiac muscle. References Further reading * * * * * * * * External links * {{gene-19-s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CRYAB
Alpha-crystallin B chain is a protein that in humans is encoded by the ''CRYAB'' gene. It is part of the small heat shock protein family and functions as molecular chaperone that primarily binds misfolded proteins to prevent protein aggregation, as well as inhibit apoptosis and contribute to intracellular architecture. Post-translational modifications decrease the ability to chaperone. Mutations in ''CRYAB'' cause different cardiomyopathies, skeletal myopathies mainly myofibrillar myopathy, and also cataracts. In addition, defects in this gene/protein have been associated with cancer and neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. Structure Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystalli ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CRYAA
Alpha-crystallin A chain is a protein that in humans is encoded by the ''CRYAA'' gene. Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HSPB2
Heat shock protein beta-2 is a protein that in humans is encoded by the ''HSPB2'' gene. Interactions HSPB2 has been shown to interact with: * CRYAB, * HSPB8, * Myotonic dystrophy protein kinase and * TRAF6 TRAF6 is a TRAF human protein. Function The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins are associated with, and mediate signal transduction from members of the TNF recep .... References Further reading * * * * * * * * * * * * * * * * {{gene-11-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heat Shock Proteins
Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). HSPs are found in virtually all living organisms, from bacteria to humans. Heat-shock proteins are named according to their molecular weight. For example, Hsp60, Hsp70 and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70 and 90 kilodal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HSPB1
Heat shock protein 27 (Hsp27) also known as heat shock protein beta-1 (HSPB1) is a protein that in humans is encoded by the ''HSPB1'' gene. Hsp27 is a chaperone of the sHsp (small heat shock protein) group among α-crystallin, Hsp20, and others. The common functions of sHsps are chaperone activity, thermotolerance, inhibition of apoptosis, regulation of cell development, and cell differentiation. They also take part in signal transduction. Structure sHsps have some structural features in common: Very characteristic is a homologous and highly conserved amino acid sequence, the so-called α-crystallin domain near the C-terminus. These domains consist of 80 to 100 residues with sequence homology between 20% and 60% and fold into β-sheets, which are important for the formation of stable dimers. Hsp27 is rather unique among sHsps in that its α-crystallin domain contains a cysteine residue at its dimer interface, which can become oxidized to form a disulfide bond that covalently li ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cyanophage
Cyanophages are viruses that infect cyanobacteria, also known as Cyanophyta or blue-green algae. Cyanobacteria are a phylum of bacteria that obtain their energy through the process of photosynthesis. Although cyanobacteria metabolize photoautotrophically like eukaryotic plants, they have prokaryotic cell structure. Cyanophages can be found in both freshwater and marine environments. Marine and freshwater cyanophages have icosahedral heads, which contain double-stranded DNA, attached to a tail by connector proteins. The size of the head and tail vary among species of cyanophages. Cyanophages infect a wide range of cyanobacteria and are key regulators of the cyanobacterial populations in aquatic environments, and may aid in the prevention of cyanobacterial blooms in freshwater and marine ecosystems. These blooms can pose a danger to humans and other animals, particularly in eutrophic freshwater lakes. Infection by these viruses is highly prevalent in cells belonging to ''Synechococc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
