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Gene Review

HSPD1  -  heat shock 60kDa protein 1 (chaperonin)

Homo sapiens

Synonyms: 60 kDa chaperonin, 60 kDa heat shock protein, mitochondrial, CPN60, Chaperonin 60, GROEL, ...
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Disease relevance of HSPD1

  • We found that the gene expression of BNIP3 was up-regulated while ZK1, RAD23B, and HSPD1 were down-regulated during early apoptosis of the hepatoma cell mediated by PRE [1].
  • Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60 [2].
  • Using IN-affinity chromatography we identified four yeast proteins interacting with HIV-1 IN, including the yeast chaperonin yHSP60, which is the counterpart of human hHSP60 [3].
  • Of these proteins, Hsp60, Hsp70, and Hsc70 associated with virions purified based on either particle density or size and were shown to be incorporated within the virion membrane, where they were protected from digestion by exogenous protease [4].
  • The groE operon of Francisella tularensis LVS, encoding the heat shock proteins chaperone-10 (Cpn10) and Cpn60, was sequenced and characterized, and the T-cell response of LVS-vaccinated individuals to the two proteins and the third major chaperone, Ft-DnaK, was assayed [5].

Psychiatry related information on HSPD1


High impact information on HSPD1


Chemical compound and disease context of HSPD1

  • Autoantibodies to pancreatic hsp60 precede the development of glucose intolerance in patients with cystic fibrosis [11].
  • CONCLUSION: These results demonstrate that expression of HDJ-2 is significantly increased in atherosclerotic carotid artery plaques as compared with hsp60 and hsp70 and correlates with luminal stenosis in ulcerated atherosclerotic carotid artery plaques [12].
  • Induction of mitochondrial chaperonin, hsp60, by cadmium in human hepatoma cells [13].
  • We have altered the groEL gene (encoding the essential Escherichia coli HSP60 chaperonin) so that the protein produced lacks its 16 final (including nine gly, and five met) residues [14].
  • In contrast to E. coli, where Hsp60 was localized exclusively in the cytoplasm, in L. pneumophila Hsp60 was predominantly associated with the cell envelope, conforming to a distribution pattern typical of surface molecules that included the major outer membrane protein OmpS and lipopolysaccharide [15].

Biological context of HSPD1


Anatomical context of HSPD1

  • Thus, during cellular stress an increased proportion of HLA-E molecules may bind the nonprotective hsp60 signal peptide, leading to a reduced capacity to inhibit a major NK cell population [19].
  • A 60-kDa protein that is present in the plasma membrane of a human leukemic CD4(+) CEM-SS T cell line and is phosphorylated by protein kinase A (PKA) was identified as hsp60 [17].
  • However, direct evidence that hsp60 functions as a chaperone outside of mitochondria is presently lacking [17].
  • Mean levels of hsp60 expression in c-ALL BCPs at initial presentation and at relapse were similar and not distinguishable from that in normal BM BCPs, however, elevated (by a factor of 2-3) compared with that in PB B-cells [20].
  • However, interestingly, whereas an overexpression of mortalin extended in vitro life span of normal fibroblasts (TIG-1), overexpression of HSP60 was neutral [21].

Associations of HSPD1 with chemical compounds

  • The specificity of the interaction was confirmed in vitro for the recombinant proteins PrPc23-231 and rPrP27-30 fused to glutathione S-transferase with recombinant human Hsp60 as well as the bacterial GroEL [18].
  • Control Abs, including human anti-hsp65/60 low titer antiserum, human Ig fraction deprived of hsp65/60 Ab, and mAbs to Factor VIII, alpha-actin, hsp70, and CD3 showed no cytotoxic effect [22].
  • Identification of heat shock protein 60 as a molecular mediator of alpha 3 beta 1 integrin activation [23].
  • Heat shock protein 60: specific binding of lipopolysaccharide [24].
  • In addition, A-ODNs specific for Hsp60 also inhibit replication of a mutant HBV strain that is resistant to the nucleoside analogue 3TC, which is the main drug used for HBV treatment, and we suggest that A-ODNs directed against Hsp60 are possible reagents as anti-HBV drugs [25].
  • Following in vitro activation with Hsp60, significant amounts of tumor necrosis factor alpha, interleukin-1beta (IL-1beta), and IL-10 were produced [26].

Physical interactions of HSPD1

  • Cpn10 binds to only one end of the cpn60 structure and is visible as an additional layer of density forming a cap on one end of the cpn60 cylinder [27].
  • RA sera show the greatest increase in IgA binding to the mycobacterial hsp65, but no increase in IgA binding to the E. coli homologue [28].
  • Both procedures used here gave results that were consistent with there being 1 rhodanese binding site/cpn60 tetradecamer [29].
  • Previous studies on Spanish patients with Primary Biliary Cirrhosis (PBC) have shown extensive, disease-specific cross-reactivity between the 65-kDa heat shock protein (hsp65) of Mycobacterium gordonae and pyruvate dehydrogenase complex-E2 (PDC-E2), the major target of anti-mitochondrial antibody (AMA) [30].
  • The level of endoplasmic reticulum Ca(2+)-binding chaperones ERp57 and ERp72 and of anti-apoptotic proteins Bcl-2 and Bcl-x(L) was decreased whereas that of Ca(2+)-binding protein calmodulin and the stress protein HSP60 was elevated following ALA-PDT [31].

Enzymatic interactions of HSPD1


Regulatory relationships of HSPD1

  • Similarly, DNA vaccination with Hsp60 induced Hsp70-specific T cell immunity [33].
  • Further studies are needed to gain insight into the detailed mechanism of how the IL-6 gene polymorphism at position -174 influences anti-hsp60 autoantibody levels [34].
  • Additionally, inhibiting the surface expression of endogenous HSP60 by nonactin inhibited activation of the alpha 3 beta 1 integrin by IGF1 [23].
  • Differences between individuals in MHC class II may influence the selection of a particular hsp60 epitope and the corresponding target antigen that gives rise to an autoimmune disease [35].
  • Co-operative binding of hsp60 may promote transfer from hsp70 and correct folding of imported proteins in mitochondria [corrected] [36].

Other interactions of HSPD1

  • This peptide gains access to HLA-E intracellularly, resulting in up-regulated HLA-E/hsp60 signal peptide cell-surface levels on stressed cells [19].
  • Hsp60 physically associated with H2B when both molecules were in their dephospho forms [17].
  • In addition, our results suggest that the regulatory mechanisms induced by Hsp60, Hsp70, and Hsp90 are reinforced by an immune network that connects their reactivities [33].
  • On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60 [37].
  • Expression of Hsp73 was weak and Hsp60 was not detectable in the IMA [38].
  • The short interfering RNA-mediated knockdown experiments revealed that in BMD188-induced apoptosis, HSP60 has a pro-death function and that the pro-death role of HSP60 seems to involve caspase-3 maturation and activation in the cytosol [39].

Analytical, diagnostic and therapeutic context of HSPD1


  1. Paeoniae Radix, a Chinese herbal extract, inhibit hepatoma cells growth by inducing apoptosis in a p53 independent pathway. Lee, S.M., Li, M.L., Tse, Y.C., Leung, S.C., Lee, M.M., Tsui, S.K., Fung, K.P., Lee, C.Y., Waye, M.M. Life Sci. (2002) [Pubmed]
  2. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Hansen, J.J., Dürr, A., Cournu-Rebeix, I., Georgopoulos, C., Ang, D., Nielsen, M.N., Davoine, C.S., Brice, A., Fontaine, B., Gregersen, N., Bross, P. Am. J. Hum. Genet. (2002) [Pubmed]
  3. Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60. Parissi, V., Calmels, C., De Soultrait, V.R., Caumont, A., Fournier, M., Chaignepain, S., Litvak, S. J. Virol. (2001) [Pubmed]
  4. Specific incorporation of heat shock protein 70 family members into primate lentiviral virions. Gurer, C., Cimarelli, A., Luban, J. J. Virol. (2002) [Pubmed]
  5. Characterization of the nucleotide sequence of the groE operon encoding heat shock proteins chaperone-60 and -10 of Francisella tularensis and determination of the T-cell response to the proteins in individuals vaccinated with F. tularensis. Ericsson, M., Golovliov, I., Sandström, G., Tärnvik, A., Sjöstedt, A. Infect. Immun. (1997) [Pubmed]
  6. Expression of the human groEL stress-protein homologue in the brain and spinal cord. Martin, J.E., Swash, M., Mather, K., Leigh, P.N. J. Neurol. Sci. (1993) [Pubmed]
  7. Autoantibodies against 60-kDa heat shock protein in schizophrenia. Schwarz, M.J., Riedel, M., Gruber, R., Müller, N., Ackenheil, M. European archives of psychiatry and clinical neuroscience. (1998) [Pubmed]
  8. Autoimmune and inflammatory mechanisms in atherosclerosis. Wick, G., Knoflach, M., Xu, Q. Annu. Rev. Immunol. (2004) [Pubmed]
  9. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Ostermann, J., Horwich, A.L., Neupert, W., Hartl, F.U. Nature (1989) [Pubmed]
  10. Molecular evidence for the early evolution of photosynthesis. Xiong, J., Fischer, W.M., Inoue, K., Nakahara, M., Bauer, C.E. Science (2000) [Pubmed]
  11. Autoantibodies to pancreatic hsp60 precede the development of glucose intolerance in patients with cystic fibrosis. Jensen, P., Johansen, H.K., Carmi, P., Høiby, N., Cohen, I.R. J. Autoimmun. (2001) [Pubmed]
  12. Increased expression of HDJ-2 (hsp40) in carotid artery atherosclerosis: a novel heat shock protein associated with luminal stenosis and plaque ulceration. Nguyen, T.Q., Jaramillo, A., Thompson, R.W., Dintzis, S., Oppat, W.F., Allen, B.T., Sicard, G.A., Mohanakumar, T. J. Vasc. Surg. (2001) [Pubmed]
  13. Induction of mitochondrial chaperonin, hsp60, by cadmium in human hepatoma cells. Hiranuma, K., Hirata, K., Abe, T., Hirano, T., Matsuno, K., Hirano, H., Suzuki, K., Higashi, K. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  14. The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable. McLennan, N.F., Girshovich, A.S., Lissin, N.M., Charters, Y., Masters, M. Mol. Microbiol. (1993) [Pubmed]
  15. Immunolocalization of Hsp60 in Legionella pneumophila. Garduño, R.A., Faulkner, G., Trevors, M.A., Vats, N., Hoffman, P.S. J. Bacteriol. (1998) [Pubmed]
  16. Single-nucleotide variations in the genes encoding the mitochondrial Hsp60/Hsp10 chaperone system and their disease-causing potential. Bross, P., Li, Z., Hansen, J., Hansen, J.J., Nielsen, M.N., Corydon, T.J., Georgopoulos, C., Ang, D., Lundemose, J.B., Niezen-Koning, K., Eiberg, H., Yang, H., K??lvraa, S., Bolund, L., Gregersen, N. J. Hum. Genet. (2007) [Pubmed]
  17. Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane. Khan, I.U., Wallin, R., Gupta, R.S., Kammer, G.M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  18. Prion protein PrPc interacts with molecular chaperones of the Hsp60 family. Edenhofer, F., Rieger, R., Famulok, M., Wendler, W., Weiss, S., Winnacker, E.L. J. Virol. (1996) [Pubmed]
  19. A signal peptide derived from hsp60 binds HLA-E and interferes with CD94/NKG2A recognition. Michaëlsson, J., Teixeira de Matos, C., Achour, A., Lanier, L.L., Kärre, K., Söderström, K. J. Exp. Med. (2002) [Pubmed]
  20. Expression levels of hsc70 and hsp60 are developmentally regulated during B-cell maturation and not associated to childhood c-ALL at presentation or relapse. Wehner, P.S., Nielsen, B., Hokland, M. Eur. J. Haematol. (2003) [Pubmed]
  21. Quantum dot-based protein imaging and functional significance of two mitochondrial chaperones in cellular senescence and carcinogenesis. Kaul, Z., Yaguchi, T., Kaul, S.C., Wadhwa, R. Ann. N. Y. Acad. Sci. (2006) [Pubmed]
  22. Autoantibodies against heat shock protein 60 mediate endothelial cytotoxicity. Schett, G., Xu, Q., Amberger, A., Van der Zee, R., Recheis, H., Willeit, J., Wick, G. J. Clin. Invest. (1995) [Pubmed]
  23. Identification of heat shock protein 60 as a molecular mediator of alpha 3 beta 1 integrin activation. Barazi, H.O., Zhou, L., Templeton, N.S., Krutzsch, H.C., Roberts, D.D. Cancer Res. (2002) [Pubmed]
  24. Heat shock protein 60: specific binding of lipopolysaccharide. Habich, C., Kempe, K., van der Zee, R., Rümenapf, R., Akiyama, H., Kolb, H., Burkart, V. J. Immunol. (2005) [Pubmed]
  25. Antisense oligodeoxynucleotides targeted against molecular chaperonin Hsp60 block human hepatitis B virus replication. Park, S.G., Lee, S.M., Jung, G. J. Biol. Chem. (2003) [Pubmed]
  26. Hsp60 in inflamed muscle tissue is the target of regulatory autoreactive T cells in patients with juvenile dermatomyositis. Elst, E.F., Klein, M., de Jager, W., Kamphuis, S., Wedderburn, L.R., van der Zee, R., Albani, S., Kuis, W., Prakken, B.J. Arthritis Rheum. (2008) [Pubmed]
  27. ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Saibil, H.R., Zheng, D., Roseman, A.M., Hunter, A.S., Watson, G.M., Chen, S., Auf Der Mauer, A., O'Hara, B.P., Wood, S.P., Mann, N.H., Barnett, L.K., Ellis, R.J. Curr. Biol. (1993) [Pubmed]
  28. Elevated IgG antibody levels to the mycobacterial 65-kDa heat shock protein are characteristic of patients with rheumatoid arthritis. Tsoulfa, G., Rook, G.A., Bahr, G.M., Sattar, M.A., Behbehani, K., Young, D.B., Mehlert, A., Van-Embden, J.D., Hay, F.C., Isenberg, D.A. Scand. J. Immunol. (1989) [Pubmed]
  29. Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry. Mendoza, J.A., Lorimer, G.H., Horowitz, P.M. J. Biol. Chem. (1991) [Pubmed]
  30. Disease-specific cross-reactivity between mimicking peptides of heat shock protein of Mycobacterium gordonae and dominant epitope of E2 subunit of pyruvate dehydrogenase is common in Spanish but not British patients with primary biliary cirrhosis. Bogdanos, D.P., Pares, A., Baum, H., Caballeria, L., Rigopoulou, E.I., Ma, Y., Burroughs, A.K., Rodes, J., Vergani, D. J. Autoimmun. (2004) [Pubmed]
  31. Mitochondrial and endoplasmic reticulum stress-induced apoptotic pathways are activated by 5-aminolevulinic acid-based photodynamic therapy in HL60 leukemia cells. Grebenová, D., Kuzelová, K., Smetana, K., Pluskalová, M., Cajthamlová, H., Marinov, I., Fuchs, O., Soucek, J., Jarolím, P., Hrkal, Z. J. Photochem. Photobiol. B, Biol. (2003) [Pubmed]
  32. Long-term effect of heat shock protein 60 from Actinobacillus actinomycetemcomitans on epithelial cell viability and mitogen-activated protein kinases. Zhang, L., Pelech, S., Uitto, V.J. Infect. Immun. (2004) [Pubmed]
  33. Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein: immune cross-regulation with the 60-kd heat-shock protein. Quintana, F.J., Carmi, P., Mor, F., Cohen, I.R. Arthritis Rheum. (2004) [Pubmed]
  34. The promoter polymorphism of the IL-6 gene is associated with levels of antibodies to 60-kDa heat-shock proteins. Veres, A., Prohászka, Z., Kilpinen, S., Singh, M., Füst, G., Hurme, M. Immunogenetics (2002) [Pubmed]
  35. Sequence homologies between hsp60 and autoantigens. Jones, D.B., Coulson, A.F., Duff, G.W. Immunol. Today (1993) [Pubmed]
  36. Co-operative binding of hsp60 may promote transfer from hsp70 and correct folding of imported proteins in mitochondria [corrected]. Endo, T. FEBS Lett. (1991) [Pubmed]
  37. On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60. Deocaris, C.C., Kaul, S.C., Wadhwa, R. Cell Stress Chaperones (2006) [Pubmed]
  38. Thermal preconditioning protects the human internal mammary artery from hypoxia/re-oxygenation-induced damage. Hammerer-Lercher, A., Haeusler, C., Prelog, M., Bonatti, J., Hoefer, D., Ruttmann, E., Laufer, G., Werner, E.R., Dirnhofer, S., Puschendorf, B., Mair, J. Clin. Exp. Pharmacol. Physiol. (2006) [Pubmed]
  39. Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. Chandra, D., Choy, G., Tang, D.G. J. Biol. Chem. (2007) [Pubmed]
  40. Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter. Hansen, J.J., Bross, P., Westergaard, M., Nielsen, M.N., Eiberg, H., Børglum, A.D., Mogensen, J., Kristiansen, K., Bolund, L., Gregersen, N. Hum. Genet. (2003) [Pubmed]
  41. Immunotherapy of a human papillomavirus type 16 E7-expressing tumor by administration of fusion protein comprised of Mycobacterium bovis BCG Hsp65 and HPV16 E7. Chu, N.R., Wu, H.B., Wu, T.C., Boux, L.J., Mizzen, L.A., Siegel, M.I. Cell Stress Chaperones (2000) [Pubmed]
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