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Heat shock proteins (HSPs) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, [1] but are now known to also be expressed during other stresses including exposure to cold, [2] UV light [3] and during wound healing or tissue remodeling. [4]
Heat shock proteins are also believed to play a role in the presentation of pieces of proteins (or peptides) on the cell surface to help the immune system recognize diseased cells. [22] The major HSPs involved in the HSR include HSP70, HSP90, and HSP60. [5] Chaperones include the HSP70s and HSP90s while HSP60s are considered to be chaperonins. [17]
Heat shock factor protein 1 (HSF 1) is a protein that in humans is encoded by the HSF1 gene. [4] HSF1 is highly conserved in eukaryotes and is the primary mediator of transcriptional responses to proteotoxic stress with important roles in non-stress regulation such as development and metabolism.
By temporarily binding to hydrophobic residues exposed by stress, Hsp70 prevents these partially denatured proteins from aggregating, and inhibits them from refolding. Low ATP is characteristic of heat shock and sustained binding is seen as aggregation suppression, while recovery from heat shock involves substrate binding and nucleotide cycling.
Heat shock protein beta-6 (HSPB6) is a protein that in humans is encoded by the HSPB6 gene. [5] [6] [7]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).
A heat shock protein (HSP) is one of group of proteins which increase their expression when the cells which contain them are exposed to high temperatures. For more information, see heat shock protein .
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. [ 5 ] [ 6 ] Hsp27 is a chaperone of the sHsp (small heat shock protein ) group among α- crystallin , Hsp20 , and others.
Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.