The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

Hspa5  -  heat shock protein 5

Rattus norvegicus

Synonyms: 78 kDa glucose-regulated protein, BIP, BiP, GRP-78, GRP78, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Hspa5

 

High impact information on Hspa5

  • Furthermore, overexpression of OASIS resulted in induction of BiP and suppression of ER-stress-induced cell death, whereas knockdown partially reduced BiP levels and led to ER stress in susceptible astrocytes [6].
  • Perturbation of protein folding promotes reversible dissociation of BiP from the lumenal domains of PERK and IRE1 [7].
  • Calcium ionophore A23187 specifically and effectively induced the synthesis of the glucose-regulated protein GRP78 [8].
  • The 78-kDa glucose-regulated protein GRP78 is a stress-inducible protein ubiquitously expressed in animal cells [9].
  • Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression [9].
 

Chemical compound and disease context of Hspa5

 

Biological context of Hspa5

  • In these mice, administration with lipopolysaccharide caused rapid, transient decrease in serum SEAP activity, and it was correlated with up-regulation of grp78 in several organs including the spleen, lung, kidney, liver and heart [14].
  • This may allow modulation of grp78 transactivation by diverse external stimuli [3].
  • Both the ethanol induction and potentiation responses modulated grp78 gene transcription as determined by stable transfection analyses with the rat grp78 promoter [4].
  • Furthermore, the kinetics of BiP interaction with unassembled wild type and with mutant Na,K-ATPase beta-subunits parallels their respective stability against cellular degradation [15].
  • The involvement of p38(MAPK) in the activation of ATF-2, which leads to the transactivation of rat grp78, is confirmed by electrophoretic mobility shift assay using a probe containing the CRE-like sequence as well as by transient transfection assays with a plasmid containing a 710-base pair stretch of the grp78 promoter [3].
 

Anatomical context of Hspa5

  • Immunoprecipitation of Akt from mesangial cell lysate coprecipitated Grp78 and Hsp70 [16].
  • We demonstrate (1) that some cisternae are immunoreactive for antibodies against ribosomal proteins and eIF-2, and (2) that markers of endoplasmic reticulum (BiP), intermediate compartment, and Golgi complex (rab1, CTR433, TGN38) label subsets of these subsynaptic organelles [17].
  • For this purpose, the mRNAs for the constitutive cognate HSC 73, the heat-inducible HSP 70 and the glucose-regulated GRP 78 have been analyzed by: (i) translation in reticulocyte lysates; (ii) hybrid-selected translation, and (iii) Northern blot analysis [2].
  • Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP [15].
  • Using chemical cross-linking, we now demonstrate that BiP, ERp72, and grp94 associate with Tg in two types of cultured thyroid cells, FRTL-5 and PCC13 [18].
 

Associations of Hspa5 with chemical compounds

  • Unexpectedly, the levels of the ER chaperone proteins Grp78/BiP and PDI were not affected by palmitate treatment, suggesting that the cell protective aspects of the unfolded protein response (UPR) are not up-regulated by palmitate [19].
  • Previously we showed that chronic ethanol exposure increases the expression of GRP78 [4].
  • Following translocation of ATP into the lumen of the vesicles, binding to luminal proteins including BiP (immunoglobulin heavy chain-binding protein-glucose-regulated protein 78) and glucose-regulated protein 94 was observed [20].
  • GRP78, a molecular chaperone expressed in the endoplasmic reticulum, is a "glucose-regulated protein" induced by stress responses that deplete glucose or intracisternal calcium or otherwise disrupt glycoprotein trafficking [4].
  • In contrast, co-treatment with the classical GRP inducers thapsigargin and tunicamycin produced only simple additive increases in grp78 promoter activity [4].
 

Physical interactions of Hspa5

 

Regulatory relationships of Hspa5

  • Activation of p38 mitogen-activated protein kinase and mitochondrial Ca(2+)-mediated oxidative stress are essential for the enhanced expression of grp78 induced by the protein phosphatase inhibitors okadaic acid and calyculin A [22].
 

Other interactions of Hspa5

  • BiP (also known as GRP78), ERp55, and ERp57 showed marked swings with peaks occurring in midwinter and midsummer [23].
  • Conclusively, we present that both the disturbances of mitochondrial calcium homeostasis and reactive oxygen intermediates are essential for rapid transactivation of grp78, and this pathway is separate from protein kinase A (PKA)-dependent CREB activation or p38 mitogen-activated protein kinase (p38(MAPK))-dependent ATF-2 activation and signalling [24].
  • Three of the down-regulated genes, GRP78 (BiP), Dad1, and mitochondrial aspartate aminotransferase have been previously shown to be directly androgen regulated [25].
  • The transcription of key ER proteins including GADD153, PERK, GRP78, PDI, GRP94 and calreticulin were up-regulated by mefloquine, suggesting that the drug induced an ER stress response [26].
  • Protracted lithium treatment protects against the ER stress elicited by thapsigargin in rat PC12 cells: roles of intracellular calcium, GRP78 and Bcl-2 [27].
 

Analytical, diagnostic and therapeutic context of Hspa5

References

  1. Steroidogenesis-activator polypeptide isolated from a rat Leydig cell tumor. Pedersen, R.C., Brownie, A.C. Science (1987) [Pubmed]
  2. Expression of different members of heat shock protein 70 gene family in liver and hepatomas. Cairo, G., Schiaffonati, L., Rappocciolo, E., Tacchini, L., Bernelli-Zazzera, A. Hepatology (1989) [Pubmed]
  3. Involvement of p38 mitogen-activated protein kinase signaling pathway in the rapid induction of the 78-kDa glucose-regulated protein in 9L rat brain tumor cells. Chen, K.D., Chen, L.Y., Huang, H.L., Lieu, C.H., Chang, Y.N., Chang, M.D., Lai, Y.K. J. Biol. Chem. (1998) [Pubmed]
  4. Interaction of ethanol with inducers of glucose-regulated stress proteins. Ethanol potentiates inducers of grp78 transcription. Hsieh, K.P., Wilke, N., Harris, A., Miles, M.F. J. Biol. Chem. (1996) [Pubmed]
  5. Induction of GRP78 by ischemic preconditioning reduces endoplasmic reticulum stress and prevents delayed neuronal cell death. Hayashi, T., Saito, A., Okuno, S., Ferrand-Drake, M., Chan, P.H. J. Cereb. Blood Flow Metab. (2003) [Pubmed]
  6. OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes. Kondo, S., Murakami, T., Tatsumi, K., Ogata, M., Kanemoto, S., Otori, K., Iseki, K., Wanaka, A., Imaizumi, K. Nat. Cell Biol. (2005) [Pubmed]
  7. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Bertolotti, A., Zhang, Y., Hendershot, L.M., Harding, H.P., Ron, D. Nat. Cell Biol. (2000) [Pubmed]
  8. Heat shock response of the rat lens. de Jong, W.W., Hoekman, W.A., Mulders, J.W., Bloemendal, H. J. Cell Biol. (1986) [Pubmed]
  9. Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression. Chang, S.C., Wooden, S.K., Nakaki, T., Kim, Y.K., Lin, A.Y., Kung, L., Attenello, J.W., Lee, A.S. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  10. Differential display PCR reveals novel targets for the mood-stabilizing drug valproate including the molecular chaperone GRP78. Wang, J.F., Bown, C., Young, L.T. Mol. Pharmacol. (1999) [Pubmed]
  11. Reprogramming of gene expression in postischemic rat liver: induction of proto-oncogenes and hsp 70 gene family. Schiaffonati, L., Rappocciolo, E., Tacchini, L., Cairo, G., Bernelli-Zazzera, A. J. Cell. Physiol. (1990) [Pubmed]
  12. Induction of glucose regulated protein (grp78) and inducible heat shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal ischemia. Wang, S., Longo, F.M., Chen, J., Butman, M., Graham, S.H., Haglid, K.G., Sharp, F.R. Neurochem. Int. (1993) [Pubmed]
  13. Regulated expression of GRP78 during vasopressin-induced hypertrophy of heart-derived myocytes. Brostrom, M.A., Mourad, F., Brostrom, C.O. J. Cell. Biochem. (2001) [Pubmed]
  14. Real-time detection and continuous monitoring of ER stress in vitro and in vivo by ES-TRAP: evidence for systemic, transient ER stress during endotoxemia. Hiramatsu, N., Kasai, A., Hayakawa, K., Yao, J., Kitamura, M. Nucleic Acids Res. (2006) [Pubmed]
  15. Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP. Beggah, A., Mathews, P., Beguin, P., Geering, K. J. Biol. Chem. (1996) [Pubmed]
  16. A proteomic screen identified stress-induced chaperone proteins as targets of Akt phosphorylation in mesangial cells. Barati, M.T., Rane, M.J., Klein, J.B., McLeish, K.R. J. Proteome Res. (2006) [Pubmed]
  17. Dendritic and postsynaptic protein synthetic machinery. Gardiol, A., Racca, C., Triller, A. J. Neurosci. (1999) [Pubmed]
  18. Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation. Kuznetsov, G., Chen, L.B., Nigam, S.K. J. Biol. Chem. (1994) [Pubmed]
  19. Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. Karaskov, E., Scott, C., Zhang, L., Teodoro, T., Ravazzola, M., Volchuk, A. Endocrinology (2006) [Pubmed]
  20. Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94. Clairmont, C.A., De Maio, A., Hirschberg, C.B. J. Biol. Chem. (1992) [Pubmed]
  21. GRP78-binding protein regulates cAMP-induced glial fibrillary acidic protein expression in rat C6 glioblastoma cells. Oh-hashi, K., Hirata, Y., Koga, H., Kiuchi, K. FEBS Lett. (2006) [Pubmed]
  22. Activation of p38 mitogen-activated protein kinase and mitochondrial Ca(2+)-mediated oxidative stress are essential for the enhanced expression of grp78 induced by the protein phosphatase inhibitors okadaic acid and calyculin A. Chen, K.D., Lai, M.T., Cho, J.H., Chen, L.Y., Lai, Y.K. J. Cell. Biochem. (2000) [Pubmed]
  23. The effect of aging on the chaperone concentrations in the hepatic, endoplasmic reticulum of male rats: the possible role of protein misfolding due to the loss of chaperones in the decline in physiological function seen with age. Erickson, R.R., Dunning, L.M., Holtzman, J.L. J. Gerontol. A Biol. Sci. Med. Sci. (2006) [Pubmed]
  24. Mitochondrial calcium-mediated reactive oxygen species are essential for the rapid induction of the grp78 gene in 9L rat brain tumour cells. Chang, W.M., Chen, K.D., Chen, L.Y., Lai, M.T., Lai, Y.K. Cell. Signal. (2003) [Pubmed]
  25. Gene expression analysis in the ventral prostate of rats exposed to vinclozolin or procymidone. Rosen, M.B., Wilson, V.S., Schmid, J.E., Gray, L.E. Reprod. Toxicol. (2005) [Pubmed]
  26. The acute neurotoxicity of mefloquine may be mediated through a disruption of calcium homeostasis and ER function in vitro. Dow, G.S., Hudson, T.H., Vahey, M., Koenig, M.L. Malar. J. (2003) [Pubmed]
  27. Protracted lithium treatment protects against the ER stress elicited by thapsigargin in rat PC12 cells: roles of intracellular calcium, GRP78 and Bcl-2. Hiroi, T., Wei, H., Hough, C., Leeds, P., Chuang, D.M. Pharmacogenomics J. (2005) [Pubmed]
  28. Reperfusion causes significant activation of heat shock transcription factor 1 in ischemic rat heart. Nishizawa, J., Nakai, A., Higashi, T., Tanabe, M., Nomoto, S., Matsuda, K., Ban, T., Nagata, K. Circulation (1996) [Pubmed]
  29. The kinetics of steroidogenesis activator polypeptide in the rat adrenal cortex. Effects of adrenocorticotropin, cyclic adenosine 3':5'-monophosphate, cycloheximide, and circadian rhythm. Mertz, L.M., Pedersen, R.C. J. Biol. Chem. (1989) [Pubmed]
 
WikiGenes - Universities