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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 induced by the HSR can help prevent protein aggregation that is associated with common neurodegenerative diseases such as Alzheimer's, Huntington's, or Parkinson's disease. [8] The diagram depicts actions taken when a stress is introduced to the cell. Stress will induce HSF-1 and cause proteins to misfold.
The heat shock response involves a class of stress proteins called heat shock proteins. [ 4 ] [ 5 ] These can help defend a cell against damage by acting as 'chaperons' in protein folding, ensuring that proteins assume their necessary shape and do not become denatured. [ 6 ]
3320 15519 Ensembl ENSG00000080824 ENSMUSG00000021270 UniProt P07900 P07901 RefSeq (mRNA) NM_001017963 NM_005348 NM_010480 RefSeq (protein) NP_001017963 NP_005339 NP_034610 Location (UCSC) Chr 14: 102.08 – 102.14 Mb Chr 12: 110.66 – 110.67 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene ...
Chaperonins are characterized by their barrel-shaped structure with binding sites for client proteins inside the barrels. The human HSP90 group consists of 5 members according to the HGNC: [17] [18] HSP90AA1 (heat shock protein 90 kDa alpha, class A, member 1) HSP90AA3P (heat shock protein 90 alpha family class A member 3, pseudogene)
Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. [5] The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria.
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.
Its expression is induced by heat shock. HSP47 is expressed in the endoplasmic reticulum. These cells synthesize and secrete type I and type II collagen. [7] The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. HSP47 is ...