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Gene Review

HSPE1  -  heat shock 10kDa protein 1

Homo sapiens

Synonyms: 10 kDa chaperonin, 10 kDa heat shock protein, mitochondrial, CPN10, Chaperonin 10, EPF, ...
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Disease relevance of HSPE1

  • In addition, the functional human HSP60-HSP10 complex in the presence of ATP was able to recognize the HIV-1 IN as a substrate [1].
  • Upstream of the cpn10 gene, an inverted repeat and motifs similar to -35 and -10 sequences of sigma70-dependent but not of sigma32-dependent promoters of Escherichia coli were found [2].
  • 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 [2].
  • Overexpression of hsp10 by adenoviral infection decreased myocyte death induced by hydrogen peroxide, sodium cyanide, and simulated ischemia and reoxygenation (SI/RO) [3].
  • While bacterial GroEL is functionally promiscuous with various co-chaperonin partners, its human homologue, Hsp60 functions specifically with its co-chaperonin partner, Hsp10, and not with other co-chaperonins, such as the bacterial GroES or bacteriophage T4-encoded Gp31 [4].

Psychiatry related information on HSPE1

  • Patients with effective portal flow (EPF = portal flow - PUV flow) lower than 692 mL/min (median) had a significantly higher risk of failing the neuropsychological test, or of having an altered EEG [5].

High impact information on HSPE1

  • Reproductive immunology. Early pregnancy factor [6].
  • Using chimeric chaperonin molecules assembled by fusing equatorial and apical domains derived from GroEL and its mammalian mitochondrial homolog, Hsp60, we show that productive folding by Hsp60 and its cognate cochaperonin, Hsp10, proceeds in vitro and in vivo without the formation of a two-ring structure [7].
  • Recombinant Mt cpn10 is a potent stimulator of bone resorption in bone explant cultures and induces osteoclast recruitment, while inhibiting the proliferation of an osteoblast bone-forming cell line [8].
  • Our findings suggest that Mt cpn10 may be a valuable pharmacological target for the clinical therapy of vertebral tuberculosis and possibly other bone diseases [8].
  • Moreover, phylogenetic analyses of hydrogenosomal Hsp70, Hsp60, and Hsp10 show that these proteins branch within a monophyletic group composed exclusively of mitochondrial homologues [9].

Chemical compound and disease context of HSPE1

  • Test populations were standardized by level of reactivity to formalin-fixed Chlamydia trachomatis elementary bodies (EBs) to address whether these associations were reflections of increased overall chlamydial exposure rather than a property specific to Hsp10 [10].
  • These data provide a novel link between Hsp10/Hsp60 and cardiac protection in doxorubicin cardiomyopathy [11].

Biological context of HSPE1


Anatomical context of HSPE1

  • Here we show that purified recombinant human Hsp10 incubated with cells in vitro reduced lipopolysaccharide (LPS)-induced nuclear factor-kappaB activation and secretion of several inflammatory mediators from RAW264.7 cells, murine macrophages, and human peripheral blood mononuclear cells [15].
  • When compared to those from nonvaccinated individuals, T cells from individuals previously vaccinated with live F. tularensis LVS showed an increased proliferative response to DnaK and Cpn60 but not to Cpn10 [2].
  • We examined whether hsp10 can reduce myocyte death by its mitochondrial function or by interacting with cytoplasmic signaling pathways [3].
  • Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells [16].
  • We use this approach to probe the dissociation (and thus association) equilibrium for the heptameric co-chaperonin proteins 10 (cpn10) from Aquifex aeolicus (Aacpn10-del25) and human mitochondria (hmcpn10) [17].

Associations of HSPE1 with chemical compounds

  • We here report on a human mitochondrial co-chaperonin protein 10 (cpn10) variant in which the conserved interface residue leucine-96 is replaced with glycine (Leu96Gly cpn10) [18].
  • Unfolding of human mitochondrial cpn10 in urea results in an unfolded heptameric state whereas GuHCl additions result in unfolded monomers [19].
  • GuHCl-induced denaturation was found to be cpn10 concentration dependent, in accord with a native heptamer to denatured monomer transition [20].
  • This study was carried out to define the roles of two heat-shock proteins, Hsp10 and Hsp60, on doxorubicin-induced apoptosis in primary cardiomyocytes [11].
  • Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27 [21].

Physical interactions of HSPE1

  • 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 [22].

Regulatory relationships of HSPE1


Other interactions of HSPE1

  • Upon import into chloroplasts the spinach cpn10 precursor is processed to its mature form of approximately 24 kDa [24].
  • Recent studies provide data to suggest that immune reactivity to Hsp10 is significantly associated with tubal infertility in a chlamydiae-exposed population [25].
  • Transfection of either the RPL36 cDNA or HSP10 cDNA conferred on KB-3-1 cells 2.5- to 3-fold resistance to cisplatin by clonogenic assays [26].

Analytical, diagnostic and therapeutic context of HSPE1


  1. 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]
  2. 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]
  3. Myocyte protection by 10 kD heat shock protein (Hsp10) involves the mobile loop and attenuation of the Ras GTP-ase pathway. Lin, K.M., Hollander, J.M., Kao, V.Y., Lin, B., Macpherson, L., Dillmann, W.H. FASEB J. (2004) [Pubmed]
  4. The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. Richardson, A., Schwager, F., Landry, S.J., Georgopoulos, C. J. Biol. Chem. (2001) [Pubmed]
  5. Central nervous system alterations in liver cirrhosis: the role of portal-systemic shunt and portal hypoperfusion. Del Piccolo, F., Sacerdoti, D., Amodio, P., Bombonato, G., Bolognesi, M., Mapelli, D., Gatta, A. Metabolic brain disease. (2003) [Pubmed]
  6. Reproductive immunology. Early pregnancy factor. Whyte, A., Heap, R.B. Nature (1983) [Pubmed]
  7. A single ring is sufficient for productive chaperonin-mediated folding in vivo. Nielsen, K.L., Cowan, N.J. Mol. Cell (1998) [Pubmed]
  8. Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: a potential contributory factor in Pott's disease. Meghji, S., White, P.A., Nair, S.P., Reddi, K., Heron, K., Henderson, B., Zaliani, A., Fossati, G., Mascagni, P., Hunt, J.F., Roberts, M.M., Coates, A.R. J. Exp. Med. (1997) [Pubmed]
  9. A common evolutionary origin for mitochondria and hydrogenosomes. Bui, E.T., Bradley, P.J., Johnson, P.J. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  10. Seroreactivity to Chlamydia trachomatis Hsp10 correlates with severity of human genital tract disease. LaVerda, D., Albanese, L.N., Ruther, P.E., Morrison, S.G., Morrison, R.P., Ault, K.A., Byrne, G.I. Infect. Immun. (2000) [Pubmed]
  11. Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells. Shan, Y.X., Liu, T.J., Su, H.F., Samsamshariat, A., Mestril, R., Wang, P.H. J. Mol. Cell. Cardiol. (2003) [Pubmed]
  12. Identification of early pregnancy factor as chaperonin 10: implications for understanding its role. Cavanagh, A.C. Rev. Reprod. (1996) [Pubmed]
  13. 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]
  14. The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10. Cavanagh, A.C., Morton, H. Eur. J. Biochem. (1994) [Pubmed]
  15. Heat shock protein 10 inhibits lipopolysaccharide-induced inflammatory mediator production. Johnson, B.J., Le, T.T., Dobbin, C.A., Banovic, T., Howard, C.B., Flores, F.d.e. .M., Vanags, D., Naylor, D.J., Hill, G.R., Suhrbier, A. J. Biol. Chem. (2005) [Pubmed]
  16. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. Samali, A., Cai, J., Zhivotovsky, B., Jones, D.P., Orrenius, S. EMBO J. (1999) [Pubmed]
  17. Dissecting homo-heptamer thermodynamics by isothermal titration calorimetry: entropy-driven assembly of co-chaperonin protein 10. Luke, K., Apiyo, D., Wittung-Stafshede, P. Biophys. J. (2005) [Pubmed]
  18. Interface mutation in heptameric co-chaperonin protein 10 destabilizes subunits but not interfaces. Brown, C., Liao, J., Wittung-Stafshede, P. Arch. Biochem. Biophys. (2005) [Pubmed]
  19. Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified. Guidry, J.J., Shewmaker, F., Maskos, K., Landry, S., Wittung-Stafshede, P. BMC Biochem. (2003) [Pubmed]
  20. Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant. Guidry, J.J., Moczygemba, C.K., Steede, N.K., Landry, S.J., Wittung-Stafshede, P. Protein Sci. (2000) [Pubmed]
  21. Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. Thériault, J.R., Lambert, H., Chávez-Zobel, A.T., Charest, G., Lavigne, P., Landry, J. J. Biol. Chem. (2004) [Pubmed]
  22. 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]
  23. HSP-10 in ovarian cancer: expression and suppression of T-cell signaling. Akyol, S., Gercel-Taylor, C., Reynolds, L.C., Taylor, D.D. Gynecol. Oncol. (2006) [Pubmed]
  24. Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants. Bertsch, U., Soll, J., Seetharam, R., Viitanen, P.V. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  25. Chlamydial heat shock proteins and disease pathology: new paradigms for old problems? LaVerda, D., Kalayoglu, M.V., Byrne, G.I. Infectious diseases in obstetrics and gynecology. (1999) [Pubmed]
  26. Identification by functional cloning from a retroviral cDNA library of cDNAs for ribosomal protein L36 and the 10-kDa heat shock protein that confer cisplatin resistance. Shen, D.W., Liang, X.J., Suzuki, T., Gottesman, M.M. Mol. Pharmacol. (2006) [Pubmed]
  27. Purification and characterization of chaperonins 60 and 10 from Methylobacillus glycogenes. Kawata, Y., Doi, K., Omoto, H., Mizobata, T., Nagai, J. Cell Stress Chaperones (1998) [Pubmed]
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