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Gene Review

Hspa5  -  heat shock protein 5

Mus musculus

Synonyms: 78 kDa glucose-regulated protein, 78kDa, AL022860, AU019543, BiP, ...
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Disease relevance of Hspa5

  • The predominant binding protein purified from 1-LN prostate cancer cells was Grp 78 with small amounts of LRP, a fact that is consistent with our previous observations that there is little LRP present on the surface of these cells [1].
  • Confocal immunocytofluorescence demonstrated that hypoxia induced GRP78 in neonatal rat and isolated adult mouse ventricular myocytes [2].
  • Moreover, mouse hearts subjected to in vivo myocardial infarction exhibited increased GRP78 expression in cardiac myocytes near the infarct, but not in healthy cells distal to the infarct [2].
  • Grp78 participates in numerous pathological processes, including the regulation of the coagulation cascade, but the mechanism of Grp78 regulation of coagulation is unknown [3].
  • Identification of the mechanism by which Grp78 regulates TF function may advance insight into the pathobiology of atherosclerosis and associated arterial thrombosis [3].

Psychiatry related information on Hspa5

  • BiP/GRP78 expression is increased with increasing durations of sleep deprivation (6, 9 and 12 h) [4].
  • Using C57/B6 male mice maintained on a 12:12 light/dark cycle, we examined, in cerebral cortex, the effect of different durations of prolonged wakefulness (0, 3, 6, 9 and 12 h) from the beginning of the lights-on inactivity period, on the protein expression of BiP/GRP78, a chaperone and classical UPR marker [4].

High impact information on Hspa5

  • We report that the wz mutation disrupts the gene Sil1 that encodes an adenine nucleotide exchange factor of BiP, a crucial ER chaperone [5].
  • The first constant domain (CH1) of immunoglobulin heavy (H) chains is essential for BiP-mediated retention of unassembled H chains in the endoplasmic reticulum (ER) [6].
  • Upon persistent misfolding, tsO45 G was slowly released from calnexin and entered a second level of retention-based ER quality control by forming BiP/GRP78-associated disulfide-bonded aggregates [7].
  • In the development of diabetes in Akita mice, mRNAs for the ER chaperone Bip and the ER stress-associated apoptosis factor Chop were induced in the pancreas [8].
  • BiP protein, a marker of ER stress, was elevated in the colonic mucosa of IRE1beta(-/-) mice, and, when exposed to dextran sodium sulfate (DSS) to induce inflammatory bowel disease, mutant mice developed colitis 3-5 days earlier than did wild-type or IRE1beta(+/-) mice [9].

Chemical compound and disease context of Hspa5


Biological context of Hspa5


Anatomical context of Hspa5


Associations of Hspa5 with chemical compounds


Physical interactions of Hspa5


Regulatory relationships of Hspa5


Other interactions of Hspa5


Analytical, diagnostic and therapeutic context of Hspa5


  1. The role of Grp 78 in alpha 2-macroglobulin-induced signal transduction. Evidence from RNA interference that the low density lipoprotein receptor-related protein is associated with, but not necessary for, GRP 78-mediated signal transduction. Misra, U.K., Gonzalez-Gronow, M., Gawdi, G., Hart, J.P., Johnson, C.E., Pizzo, S.V. J. Biol. Chem. (2002) [Pubmed]
  2. Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes. Thuerauf, D.J., Marcinko, M., Gude, N., Rubio, M., Sussman, M.A., Glembotski, C.C. Circ. Res. (2006) [Pubmed]
  3. Regulation of tissue factor--mediated initiation of the coagulation cascade by cell surface grp78. Bhattacharjee, G., Ahamed, J., Pedersen, B., El-Sheikh, A., Mackman, N., Ruf, W., Liu, C., Edgington, T.S. Arterioscler. Thromb. Vasc. Biol. (2005) [Pubmed]
  4. Sleep deprivation induces the unfolded protein response in mouse cerebral cortex. Naidoo, N., Giang, W., Galante, R.J., Pack, A.I. J. Neurochem. (2005) [Pubmed]
  5. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Zhao, L., Longo-Guess, C., Harris, B.S., Lee, J.W., Ackerman, S.L. Nat. Genet. (2005) [Pubmed]
  6. Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG. Kaloff, C.R., Haas, I.G. Immunity (1995) [Pubmed]
  7. Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Molinari, M., Galli, C., Vanoni, O., Arnold, S.M., Kaufman, R.J. Mol. Cell (2005) [Pubmed]
  8. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. Oyadomari, S., Koizumi, A., Takeda, K., Gotoh, T., Akira, S., Araki, E., Mori, M. J. Clin. Invest. (2002) [Pubmed]
  9. Increased sensitivity to dextran sodium sulfate colitis in IRE1beta-deficient mice. Bertolotti, A., Wang, X., Novoa, I., Jungreis, R., Schlessinger, K., Cho, J.H., West, A.B., Ron, D. J. Clin. Invest. (2001) [Pubmed]
  10. Brefeldin A, thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. Price, B.D., Mannheim-Rodman, L.A., Calderwood, S.K. J. Cell. Physiol. (1992) [Pubmed]
  11. Expression of glucose-regulated proteins (GRP78 and GRP94) in hearts and fore-limb buds of mouse embryos exposed to hypoglycemia in vitro. Barnes, J.A., Smoak, I.W., Branch, S. Cell Stress Chaperones (1999) [Pubmed]
  12. Expression of a defective mouse mammary tumor virus envelope glycoprotein precursor which binds stably to GRP78 within the lumen of the endoplasmic reticulum is associated with decreased glucocorticoid-induced apoptosis in mouse lymphoma cells. Lam, M., Stallcup, M., Distelhorst, C.W. Cell Death Differ. (1997) [Pubmed]
  13. Modulation of VP-16 cytotoxicity by carboplatin and 41.8 degrees C hyperthermia. Katschinski, D.M., Jacobson, E.L., Wiedemann, G.J., Robins, H.I. J. Cancer Res. Clin. Oncol. (2001) [Pubmed]
  14. Isolation, partial characterisation and immunomodulating activities of polysaccharides from Vernonia kotschyana Sch. Bip. ex Walp. Nergard, C.S., Diallo, D., Michaelsen, T.E., Malterud, K.E., Kiyohara, H., Matsumoto, T., Yamada, H., Paulsen, B.S. Journal of ethnopharmacology. (2004) [Pubmed]
  15. Production of a novel class of polyreactive pathogenic autoantibodies in BXD2 mice causes glomerulonephritis and arthritis. Hsu, H.C., Zhou, T., Kim, H., Barnes, S., Yang, P., Wu, Q., Zhou, J., Freeman, B.A., Luo, M., Mountz, J.D. Arthritis Rheum. (2006) [Pubmed]
  16. Genomic organization of the mouse Msh4 gene producing bicistronic, chimeric and antisense mRNA. Hirano, M., Noda, T. Gene (2004) [Pubmed]
  17. GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Luo, S., Mao, C., Lee, B., Lee, A.S. Mol. Cell. Biol. (2006) [Pubmed]
  18. The role of MTJ-1 in cell surface translocation of GRP78, a receptor for alpha 2-macroglobulin-dependent signaling. Misra, U.K., Gonzalez-Gronow, M., Gawdi, G., Pizzo, S.V. J. Immunol. (2005) [Pubmed]
  19. Up-regulation of GRP78 and antiapoptotic signaling in murine peritoneal macrophages exposed to insulin. Misra, U.K., Pizzo, S.V. J. Leukoc. Biol. (2005) [Pubmed]
  20. The mouse FKBP23 binds to BiP in ER and the binding of C-terminal domain is interrelated with Ca2+ concentration. Zhang, X., Wang, Y., Li, H., Zhang, W., Wu, D., Mi, H. FEBS Lett. (2004) [Pubmed]
  21. KDEL proteins are found on the surface of NG108-15 cells. Xiao, G., Chung, T.F., Pyun, H.Y., Fine, R.E., Johnson, R.J. Brain Res. Mol. Brain Res. (1999) [Pubmed]
  22. Identification of highly conserved regulatory domains and protein-binding sites in the promoters of the rat and human genes encoding the stress-inducible 78-kilodalton glucose-regulated protein. Resendez, E., Wooden, S.K., Lee, A.S. Mol. Cell. Biol. (1988) [Pubmed]
  23. Ligation of cell surface-associated glucose-regulated protein 78 by receptor-recognized forms of alpha 2-macroglobulin: activation of p21-activated protein kinase-2-dependent signaling in murine peritoneal macrophages. Misra, U.K., Sharma, T., Pizzo, S.V. J. Immunol. (2005) [Pubmed]
  24. Increased level of cellular Bip critically determines estrogenic potency for a xenoestrogen kepone in the mouse uterus. Ray, S., Xu, F., Li, P., Sanchez, N.S., Wang, H., Das, S.K. Endocrinology (2007) [Pubmed]
  25. Expression of the glucose-regulated proteins (GRP94 and GRP78) in differentiated and undifferentiated mouse embryonic cells and the use of the GRP78 promoter as an expression system in embryonic cells. Kim, S.K., Kim, Y.K., Lee, A.S. Differentiation (1990) [Pubmed]
  26. Differential screening of a cDNA library with cDNA probes amplified in a heterologous host: isolation of murine GRP78 (BiP) and other serum-regulated low-abundance mRNAs. Parfett, C.L., Hofbauer, R., Brudzynski, K., Edwards, D.R., Denhardt, D.T. Gene (1989) [Pubmed]
  27. Suppression of stress protein GRP78 induction in tumor B/C10ME eliminates resistance to cell mediated cytotoxicity. Sugawara, S., Takeda, K., Lee, A., Dennert, G. Cancer Res. (1993) [Pubmed]
  28. ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress. Leno, G.H., Ledford, B.E. Eur. J. Biochem. (1989) [Pubmed]
  29. Induction of Grp78/BiP by translational block: activation of the Grp78 promoter by ATF4 through and upstream ATF/CRE site independent of the endoplasmic reticulum stress elements. Luo, S., Baumeister, P., Yang, S., Abcouwer, S.F., Lee, A.S. J. Biol. Chem. (2003) [Pubmed]
  30. Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides. Nair, S., Wearsch, P.A., Mitchell, D.A., Wassenberg, J.J., Gilboa, E., Nicchitta, C.V. J. Immunol. (1999) [Pubmed]
  31. Tolbutamide alters glucose transport and metabolism in the embryonic mouse heart. Smoak, I.W. Teratology (2002) [Pubmed]
  32. Targeting of the c-Abl tyrosine kinase to mitochondria in endoplasmic reticulum stress-induced apoptosis. Ito, Y., Pandey, P., Mishra, N., Kumar, S., Narula, N., Kharbanda, S., Saxena, S., Kufe, D. Mol. Cell. Biol. (2001) [Pubmed]
  33. Rapid degradation of an unassembled immunoglobulin light chain is mediated by a serine protease and occurs in a pre-Golgi compartment. Gardner, A.M., Aviel, S., Argon, Y. J. Biol. Chem. (1993) [Pubmed]
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