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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 ...
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.
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.
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 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. [ 4 ] , . [ 5 ] HSPB7 contains 170 amino acids and has a molecular weight of 18,611 Da . [ 6 ]