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] 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.[5] 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).[6] 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 kilodaltons in size, respectively.[7] The small 8-kilodalton protein ubiquitin, which marks proteins for degradation, also has features of a heat shock protein.[8] A conserved protein binding domain of approximately 80 amino-acid alpha crystallins are known as small heat shock proteins (sHSP).[9]
^Ritossa F (1962). "A new puffing pattern induced by temperature shock and DNP in drosophila". Experimental. 18 (12): 571–573. doi:10.1007/BF02172188. ISSN 0014-4754. S2CID 32525462.
^Matz JM, Blake MJ, Tatelman HM, Lavoi KP, Holbrook NJ (July 1995). "Characterization and regulation of cold-induced heat shock protein expression in mouse brown adipose tissue". The American Journal of Physiology. 269 (1 Pt 2): R38–R47. doi:10.1152/ajpregu.1995.269.1.R38. PMID 7631901.
^Cao Y, Ohwatari N, Matsumoto T, Kosaka M, Ohtsuru A, Yamashita S (August 1999). "TGF-beta1 mediates 70-kDa heat shock protein induction due to ultraviolet irradiation in human skin fibroblasts". Pflügers Archiv. 438 (3): 239–244. doi:10.1007/s004240050905. PMID 10398851. S2CID 28219505.
^Laplante AF, Moulin V, Auger FA, Landry J, Li H, Morrow G, et al. (November 1998). "Expression of heat shock proteins in mouse skin during wound healing". The Journal of Histochemistry and Cytochemistry. 46 (11): 1291–1301. doi:10.1177/002215549804601109. PMID 9774628..
^De Maio A (January 1999). "Heat shock proteins: facts, thoughts, and dreams". Shock. 11 (1): 1–12. doi:10.1097/00024382-199901000-00001. PMID 9921710.
^Wu C (1995). "Heat shock transcription factors: structure and regulation". Annual Review of Cell and Developmental Biology. 11: 441–469. doi:10.1146/annurev.cb.11.110195.002301. PMID 8689565.
^Li Z, Srivastava P (February 2004). Heat-shock proteins. Vol. Appendix 1. pp. Appendix 1T. doi:10.1002/0471142735.ima01ts58. ISBN 978-0471142737. PMID 18432918. S2CID 11858453. {{cite book}}: |journal= ignored (help)
^Raboy B, Sharon G, Parag HA, Shochat Y, Kulka RG (1991). "Effect of stress on protein degradation: role of the ubiquitin system". Acta Biologica Hungarica. 42 (1–3): 3–20. PMID 1668897.
^Lahvic JL, Ji Y, Marin P, Zuflacht JP, Springel MW, Wosen JE, et al. (December 2013). "Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish". Developmental Biology. 384 (2): 166–180. doi:10.1016/j.ydbio.2013.10.009. PMC 3924900. PMID 24140541.
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