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Gene Review

Hspa1a  -  heat shock protein 1A

Mus musculus

Synonyms: HSP70.3, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 3, Hsp68, Hsp70-3, ...
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Disease relevance of Hspa1a

  • BACKGROUND: Hspa1a and Hspa1b genes encode stress-inducible 70-kDa heat shock proteins (Hsp70) that protect cells from insults such as ischemia [1].
  • We conclude that inducible HSP70.1 and HSP70.3 are required for late-phase protection against infarction following IP in mice [2].
  • The findings here that VK1 and VK2 inhibit heat-shock-induced Hsp72 suggest their possible use as an adjuvant for hyperthermia in cancer therapy [3].
  • The first objective was to determine whether Hsp72 is released within air spaces and whether Hsp72 levels in pulmonary edema fluid would correlate with the capacity of the alveolar epithelium to remove alveolar edema fluid in patients with ALI/ARDS [4].
  • The full-length mouse Hsp72 specifically bound to P388D1 cells, but not to mastocytoma P815 cells [5].

High impact information on Hspa1a

  • Hsp72 also inhibited JNK-dependent apoptosis [6].
  • Hsp72 antisense oligonucleotides blocked Hsp72 production in NIH 3T3 cells in response to mild heat shock and concomitantly abolished the suppressive effect of mild heat shock on UV-induced JNK activation and apoptosis [6].
  • In scrapie-infected N2a (ScN2a) cells, Hsp72 and Hsp28 were not induced by heat shock, sodium arsenite, or an amino acid analog, in contrast to uninfected control N2a cells, while other inducible Hsps were increased by these treatments [7].
  • Mouse embryonic fibroblasts (MEFs) prepared from Hsp70.1/3(-/-) mice did not synthesize Hsp70.1 or Hsp70.3 after heat-induced stress [8].
  • In order to determine whether such proteins specifically influence genomic instability, mice deficient for Hsp70.1 and Hsp70.3 (Hsp70.1/3(-/-) mice) were generated by gene targeting [8].

Biological context of Hspa1a


Anatomical context of Hspa1a


Regulatory relationships of Hspa1a


Other interactions of Hspa1a

  • We previously described a recombinational hotspot within the 50-kb Hsp70.3-G7 interval in the class III region of the mouse MHC [16].
  • Although an attenuated increase in Hsp68 mRNA was found in E2F1 -/- mice, no changes in the proapoptotic transcripts were found after ischemia, and a mechanistic inference was not possible [17].
  • Heat-treated v-fos-transformed cells displayed a decreased expression and accumulation of the major stress proteins Hsp68 (68-kDa heat-shock protein) and Hsp25 which probably resulted of a reduced accumulation of the corresponding mRNAs [18].
  • A dramatical increase in Hsp72/Hsp73 expression was found at the 2-cell stage [19].
  • Hsp72 did not inhibit apoptosis in mouse embryo fibroblasts once cytochrome c had been released from the mitochondria [14].

Analytical, diagnostic and therapeutic context of Hspa1a


  1. Deletion of the inducible 70-kDa heat shock protein genes in mice impairs cardiac contractile function and calcium handling associated with hypertrophy. Kim, Y.K., Suarez, J., Hu, Y., McDonough, P.M., Boer, C., Dix, D.J., Dillmann, W.H. Circulation (2006) [Pubmed]
  2. HSP70.1 and -70.3 are required for late-phase protection induced by ischemic preconditioning of mouse hearts. Hampton, C.R., Shimamoto, A., Rothnie, C.L., Griscavage-Ennis, J., Chong, A., Dix, D.J., Verrier, E.D., Pohlman, T.H. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  3. Vitamins K1 and K2 potentiate hyperthermia by down-regulating Hsp72 expression in vitro and in vivo. Shimohara, S., Murakami, T., Morikawa, M., Matsuo, J., Nagayama, S., Shuto, T., Suico, M.A., Okiyoneda, T., Yamatsu, I., Mizushima, T., Shimasaki, T., Kai, H. Int. J. Oncol. (2005) [Pubmed]
  4. Extracellular heat shock protein 72 is a marker of the stress protein response in acute lung injury. Ganter, M.T., Ware, L.B., Howard, M., Roux, J., Gartland, B., Matthay, M.A., Fleshner, M., Pittet, J.F. Am. J. Physiol. Lung Cell Mol. Physiol. (2006) [Pubmed]
  5. Functional region of mouse heat shock protein 72 for its binding to lymphoid neoplastic P388D1 cells. Ohno, M., Kitabatake, N., Tani, F. Mol. Immunol. (2007) [Pubmed]
  6. Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. Park, H.S., Lee, J.S., Huh, S.H., Seo, J.S., Choi, E.J. EMBO J. (2001) [Pubmed]
  7. Scrapie prions selectively modify the stress response in neuroblastoma cells. Tatzelt, J., Zuo, J., Voellmy, R., Scott, M., Hartl, U., Prusiner, S.B., Welch, W.J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  8. Genomic instability and enhanced radiosensitivity in Hsp70.1- and Hsp70.3-deficient mice. Hunt, C.R., Dix, D.J., Sharma, G.G., Pandita, R.K., Gupta, A., Funk, M., Pandita, T.K. Mol. Cell. Biol. (2004) [Pubmed]
  9. Inhibition of hsp70-1 and hsp70-3 expression disrupts preimplantation embryogenesis and heightens embryo sensitivity to arsenic. Dix, D.J., Garges, J.B., Hong, R.L. Mol. Reprod. Dev. (1998) [Pubmed]
  10. Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man. Ito, Y., Ando, A., Ando, H., Ando, J., Saijoh, Y., Inoko, H., Fujimoto, H. J. Biochem. (1998) [Pubmed]
  11. Protective effect of heat shock proteins 70.1 and 70.3 on retinal photic injury after systemic hyperthermia. Kim, J.H., Kim, J.H., Yu, Y.S., Jeong, S.M., Kim, K.W. Korean journal of ophthalmology : KJO. (2005) [Pubmed]
  12. Insights into regulation and function of the major stress-induced hsp70 molecular chaperone in vivo: analysis of mice with targeted gene disruption of the hsp70.1 or hsp70.3 gene. Huang, L., Mivechi, N.F., Moskophidis, D. Mol. Cell. Biol. (2001) [Pubmed]
  13. Bacterial superantigen-treated intestinal epithelial cells upregulate heat shock proteins 25 and 72 and are resistant to oxidant cytotoxicity. Musch, M.W., Petrof, E.O., Kojima, K., Ren, H., McKay, D.M., Chang, E.B. Infect. Immun. (2004) [Pubmed]
  14. Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1. Steel, R., Doherty, J.P., Buzzard, K., Clemons, N., Hawkins, C.J., Anderson, R.L. J. Biol. Chem. (2004) [Pubmed]
  15. Methylation-associated transcriptional silencing of the major histocompatibility complex-linked hsp70 genes in mouse cell lines. Gorzowski, J.J., Eckerley, C.A., Halgren, R.G., Mangurten, A.B., Phillips, B. J. Biol. Chem. (1995) [Pubmed]
  16. Molecular analysis of the major MHC recombinational hot spot located within the G7c gene of the murine class III region that is involved in disease susceptibility. Snoek, M., Teuscher, C., van Vugt, H. J. Immunol. (1998) [Pubmed]
  17. Absence of the transcription factor E2F1 attenuates brain injury and improves behavior after focal ischemia in mice. MacManus, J.P., Jian, M., Preston, E., Rasquinha, I., Webster, J., Zurakowski, B. J. Cereb. Blood Flow Metab. (2003) [Pubmed]
  18. Thermal sensitivity in NIH 3T3 fibroblasts transformed by the v-fos oncogene. Correlation with reduced accumulation of 68-kDa and 25-kDa stress proteins after heat shock. Fabre-Jonca, N., Gonin, S., Diaz-Latoud, C., Rouault, J.P., Arrigo, A.P. Eur. J. Biochem. (1995) [Pubmed]
  19. Stored of Hsp72/Hsp73 in germinal vesicle-stage mouse oocytes. Liu, C.H., Yang, C.C., Lin, D.P., Wu, M.H., Tsai, K.J. Reprod. Domest. Anim. (2004) [Pubmed]
  20. Effects of hyperthermia on spermatogenesis, apoptosis, gene expression, and fertility in adult male mice. Rockett, J.C., Mapp, F.L., Garges, J.B., Luft, J.C., Mori, C., Dix, D.J. Biol. Reprod. (2001) [Pubmed]
  21. A novel monoclonal antibody directed against the heat-inducible 68 kDa heat shock protein. Heine, L., Drabent, B., Benecke, B.J., Günther, E. Hybridoma (1991) [Pubmed]
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