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HandWiki. HSP60. Encyclopedia. Available online: https://encyclopedia.pub/entry/35732 (accessed on 25 September 2026).
HandWiki. HSP60. Encyclopedia. Available at: https://encyclopedia.pub/entry/35732. Accessed September 25, 2026.
HandWiki. "HSP60" Encyclopedia, https://encyclopedia.pub/entry/35732 (accessed September 25, 2026).
HandWiki. (2022, November 22). HSP60. In Encyclopedia. https://encyclopedia.pub/entry/35732
HandWiki. "HSP60." Encyclopedia. Web. 22 November, 2022.
HSP60
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The content is sourced from: https://handwiki.org/wiki/Biology:HSP60

Heat shock proteins are generally responsible for preventing damage to proteins in response to high levels of heat. Heat shock proteins are classified into six major families based on their molecular mass: small HSPs, HSP40, HSP60, HSP70, HSP90, and HSP110 HSP60 is implicated in mitochondrial protein import and macromolecular assembly. It may facilitate the correct folding of imported proteins, and may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSP60 interacts with HRAS and with HBV protein X and HTLV-1 protein p40tax. HSP60 belongs to the chaperonin (HSP60) family. Note: This description may include information from UniProtKB. Alternate Names: 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1 Heat shock protein 60 (HSP60) is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60’s bacterial homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Further studies have linked HSP60 to diabetes, stress response, cancer and certain types of immunological disorders.

macromolecular lymphocyte polypeptides

References

  1. Gupta RS (January 1995). "Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells". Mol. Microbiol. 15 (1): 1–11. doi:10.1111/j.1365-2958.1995.tb02216.x. PMID 7752884.  https://dx.doi.org/10.1111%2Fj.1365-2958.1995.tb02216.x
  2. "Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration". Eur. J. Biochem. 269 (23): 5931–8. December 2002. doi:10.1046/j.1432-1033.2002.03317.x. PMID 12444982.  https://dx.doi.org/10.1046%2Fj.1432-1033.2002.03317.x
  3. "The mitochondrial chaperonin hsp60 is required for its own assembly". Nature 348 (6300): 455–8. November 1990. doi:10.1038/348455a0. PMID 1978929.  https://dx.doi.org/10.1038%2F348455a0
  4. "Residues in chaperonin GroEL required for polypeptide binding and release". Nature 371 (6498): 614–9. October 1994. doi:10.1038/371614a0. PMID 7935796.  https://dx.doi.org/10.1038%2F371614a0
  5. "Heat shock protein 60: regulatory role on innate immune cells". Cell. Mol. Life Sci. 64 (6): 742–51. March 2007. doi:10.1007/s00018-007-6413-7. PMID 17221165.  https://dx.doi.org/10.1007%2Fs00018-007-6413-7
  6. "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones". Expert Rev Mol Med 2 (8): 1–17. September 2000. doi:10.1017/S1462399400002015. PMID 14585136. http://journals.cambridge.org/abstract_S1462399400002015. 
  7. PDB: 1SRV​; "Taking MAD to the extreme: ultrafast protein structure determination". Acta Crystallogr. D 55 (6): 1168–73. June 1999. doi:10.1107/S0907444999003698. PMID 10329779.  https://www.rcsb.org/structure/1SRV
  8. "Cloning and characterization of the yeast chaperonin HSP60 gene". Genetics 84 (2): 295–300. 2003. doi:10.1016/0378-1119(89)90503-9. PMID 2575559.  https://dx.doi.org/10.1016%2F0378-1119%2889%2990503-9
  9. "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space". Cell 68 (6): 1163–75. March 1992. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. https://epub.ub.uni-muenchen.de/7621/1/Neupert_Walter_7621.pdf. 
  10. Kaufman, BA. Studies on mitochondria DNA nucleoids in Saccharomyces cerevisia: identification of bifunctional proteins. In Genetics and Development, UT Southwestern Medical Center at Dallas, Dallas, TX. 241pp.
  11. Kaufman, B. A. (2003). "A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae". The Journal of Cell Biology 163 (3): 457–461. doi:10.1083/jcb.200306132. ISSN 0021-9525. PMID 14597775.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173642
  12. "Antifolding Activity of HSP60 Couples Protein Import into the Mitochondrial Matrix with Export to the Intermembrane Space". Cell 68 (6): 1163–75. 1992. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. https://epub.ub.uni-muenchen.de/7621/1/Neupert_Walter_7621.pdf. 
  13. "Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration". Eur. J. Biochem. 269 (23): 5931–8. December 2002. doi:10.1046/j.1432-1033.2002.03317.x. PMID 12444982.  https://dx.doi.org/10.1046%2Fj.1432-1033.2002.03317.x
  14. "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter". Hum. Genet. 112 (1): 71–7. January 2003. doi:10.1007/s00439-002-0837-9. PMID 12483302.  https://dx.doi.org/10.1007%2Fs00439-002-0837-9
  15. "Heat Shock and stress response of Taenia solium and T. crassiceps". Parasitology 122 (5): 583–8. 2001. doi:10.1017/s0031182001007764.  https://dx.doi.org/10.1017%2Fs0031182001007764
  16. "In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state". J. Neurochem. 101 (3): 709–17. May 2007. doi:10.1111/j.1471-4159.2006.04367.x. PMID 17241115.  https://dx.doi.org/10.1111%2Fj.1471-4159.2006.04367.x
  17. "Expression of hsp 27, hsp 60, hsc 70, and hsp 70 stress response genes in cultured human urothelial cells (UROtsa) exposed to lethal and sublethal concentrations of sodium arsenite". Environ. Health Perspect. 110 (12): 1225–32. December 2002. doi:10.1289/ehp.021101225. PMID 12460802.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1241110
  18. "Hsp60 and Hsp10 down-regulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease". Cancer 107 (10): 2417–24. November 2006. doi:10.1002/cncr.22265. PMID 17048249.  https://dx.doi.org/10.1002%2Fcncr.22265
  19. "HSP60 may predict good pathological response to neoadjuvant chemoradiotherapy in bladder cancer". Jpn. J. Clin. Oncol. 37 (1): 56–61. January 2007. doi:10.1093/jjco/hyl121. PMID 17095522. http://jjco.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=17095522. 
  20. "Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma". Cancer 98 (5): 970–7. September 2003. doi:10.1002/cncr.11594. PMID 12942564.  https://dx.doi.org/10.1002%2Fcncr.11594
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