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Gene Review

Hspa9  -  heat shock protein 9

Rattus norvegicus

Synonyms: 75 kDa glucose-regulated protein, GRP-75, Grp75, Heat shock 70 kDa protein 9, Hspa9a, ...
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Disease relevance of Hspa9a_predicted

  • However, a deregulation of the expression is observed in rat brain tumor along with the detection of nonpancytosolic mortalin in rat glioma cell line C6 [1].
  • The protein expressions of mitochondrial complex II and complex IV and Grp75 were also down-regulated during sepsis [2].
  • The results showed that hyperglycemic ischemia upregulated the expressions of hsp70, hsp90A, hsp90B, heat shock cognate 71 kD protein (hsc70) and mthsp70 [3].
  • Levels of the chaperones HSP60 and GRP75, as well as HSP60 mRNA were unaffected by hypothyroidism, but paralleled adaptive growth induced by PO [4].

High impact information on Hspa9a_predicted

  • SS mitochondria possess a greater content of the molecular chaperones hsp60 and Grp75, yet import is lower than in IMF mitochondria [5].
  • Thus, the time course of grp75 and grp78 expression did not correlate with that of tolerance [6].
  • Decreased abundance was also observed for cofilin 1, a protein linked to tumorigenesis, and for the GRP 75 precursor and preproalbumin, both of which are responsive to oxidative stress and/or inflammation [7].
  • Sequence structure and phylogenetic analyses predict mitochondrial localization and induction by a calcium ionophore and glucose deprivation in PC12 cells support its identification as rat grp75 [8].
  • It is also highly similar to two non-mitochondrial proteins; mortalin, a senescence-related gene product, and pbp74, a protein implicated in B-cell peptide processing [8].

Biological context of Hspa9a_predicted


Anatomical context of Hspa9a_predicted

  • A comparison of steady-state levels of mitochondrial enzyme activity [cytochrome c oxidase (CYTOX)] with chaperonin levels [the heat-shock protein HSP60, the glucose-regulated protein GRP75 (mtHSP70)] in striated muscles possessing a wide range of oxidative capacities revealed a proportional expression between the two [12].
  • In a running rat model, acute exercise activated the synthesis and accumulation of HSP72, GRP75 and GRP78 in liver cells, pointing towards a multifactorial origin of this response [13].
  • Proteome analysis and functional expression identify mortalin as an antiapoptotic gene induced by elevation of [Na+]i/[K+]i ratio in cultured vascular smooth muscle cells [11].
  • In the kidney: HSP25 was enhanced in proximal tubules after 6 months Al-exposure when abnormal brush borders were observed; HSP72 was induced in proximal tubules only after long Al-treatment; GRP75 was raised in midcortical area sometimes within nuclei [14].
  • There were no alterations in the mitochondrial proteins hsp60 and grp75, suggesting that TA has no effect on the mitochondrion, its effects primarily being confined to the endoplasmic reticulum [15].

Associations of Hspa9a_predicted with chemical compounds

  • Microsequence analysis of the major difluorothioamidyl-L-lysine proteins indicated that P66 is identical, over 14 NH2-terminal residues, to mitochondrial P1 protein (HSP60, a chaperonin) and that P84 is identical, over 14 residues, to a recently isolated novel member of the HSP70 family known as mortalin [16].
  • Northern and Western blotting and immunocytochemistry all have confirmed that treatment of VSMCs with ouabain results in potent induction of mortalin expression [11].
  • Coincident with increases in the import of these matrix-localized precursors were thyroid hormone-induced elevations in the outer membrane receptor Tom20 and the matrix heat-shock protein mthsp70 [17].

Other interactions of Hspa9a_predicted

  • Furthermore, we show that hypoglycaemia induces outflow of cytochrome c from mitochondria and it up-regulates heat-shock proteins HSP70, but not HSP90, glucose-regulated proteins GRP75 and GRP78, as well as expression and activity of the enzyme caspase-2 [18].
  • PURPOSE: The purpose of this investigation was to examine the relationship between the expression of HSP60 and GRP75 and the oxidative potential of skeletal muscle as assessed by the citrate synthase activity following endurance training to sedentary controls [19].

Analytical, diagnostic and therapeutic context of Hspa9a_predicted

  • Beginning with degenerate RT-PCR, we have isolated a rat-brain cDNA encoding a protein highly similar to human grp75, a mitochondrial member of the hsp70-family of stress proteins [8].
  • Although immunocytochemistry suggested that there was increased neuronal expression of grp75 and grp78, no significant differences were found in protein expression as determined by Western blot before (at 1 day), during (at 2-5 days), and after (at 7 days and thereafter) tolerance [6].
  • We have investigated the expression of mortalin in rat tissues by Northern analysis, RNA in situ hybridization, and immunohistochemical studies [1].
  • The expressions of heat shock protein 72 (Hsp72), glucose-regulated protein 75 (Grp75), and mitochondrial complexes I, II, III, and IV were evaluated by Western blot and immunochemical analysis [2].


  1. Expression analysis of mortalin, a unique member of the Hsp70 family of proteins, in rat tissues. Kaul, S.C., Matsui, M., Takano, S., Sugihara, T., Mitsui, Y., Wadhwa, R. Exp. Cell Res. (1997) [Pubmed]
  2. Heat shock pretreatment prevents cardiac mitochondrial dysfunction during sepsis. Chen, H.W., Hsu, C., Lu, T.S., Wang, S.J., Yang, R.C. Shock (2003) [Pubmed]
  3. Induction of heat shock proteins by hyperglycemic cerebral ischemia. Muranyi, M., He, Q.P., Fong, K.S., Li, P.A. Brain Res. Mol. Brain Res. (2005) [Pubmed]
  4. Effects of hypothyroidism and aortic construction on mitochondria during cardiac hypertrophy. Nishio, M.L., Ornatsky, O.I., Hood, D.A. Medicine and science in sports and exercise. (1995) [Pubmed]
  5. Protein import into subsarcolemmal and intermyofibrillar skeletal muscle mitochondria. Differential import regulation in distinct subcellular regions. Takahashi, M., Hood, D.A. J. Biol. Chem. (1996) [Pubmed]
  6. Stress proteins and tolerance to focal cerebral ischemia. Chen, J., Graham, S.H., Zhu, R.L., Simon, R.P. J. Cereb. Blood Flow Metab. (1996) [Pubmed]
  7. Proteomic analysis reveals changes in the liver protein pattern of rats exposed to dietary folate deficiency. Chanson, A., Sayd, T., Rock, E., Chambon, C., Santé-Lhoutellier, V., Potier de Courcy, G., Brachet, P. J. Nutr. (2005) [Pubmed]
  8. Cloning of rat grp75, an hsp70-family member, and its expression in normal and ischemic brain. Massa, S.M., Longo, F.M., Zuo, J., Wang, S., Chen, J., Sharp, F.R. J. Neurosci. Res. (1995) [Pubmed]
  9. Cytochrome c oxidase as the target of the heat shock protective effect in septic liver. Chen, H.W., Kuo, H.T., Lu, T.S., Wang, S.J., Yang, R.C. International journal of experimental pathology. (2004) [Pubmed]
  10. Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells. Liu, Y., Liu, W., Song, X.D., Zuo, J. Mol. Cell. Biochem. (2005) [Pubmed]
  11. Proteome analysis and functional expression identify mortalin as an antiapoptotic gene induced by elevation of [Na+]i/[K+]i ratio in cultured vascular smooth muscle cells. Taurin, S., Seyrantepe, V., Orlov, S.N., Tremblay, T.L., Thibault, P., Bennett, M.R., Hamet, P., Pshezhetsky, A.V. Circ. Res. (2002) [Pubmed]
  12. Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle. Ornatsky, O.I., Connor, M.K., Hood, D.A. Biochem. J. (1995) [Pubmed]
  13. Induction, modification and accumulation of HSP70s in the rat liver after acute exercise: early and late responses. González, B., Manso, R. J. Physiol. (Lond.) (2004) [Pubmed]
  14. Stress proteins expression in rat kidney and liver chronically exposed to aluminium sulphate. Stacchiotti, A., Rodella, L.F., Ricci, F., Rezzani, R., Lavazza, A., Bianchi, R. Histol. Histopathol. (2006) [Pubmed]
  15. Two-dimensional electrophoretic analysis of compartment-specific hepatic protein charge modification induced by thioacetamide exposure in rats. Witzmann, F.A., Fultz, C.D., Mangipudy, R.S., Mehendale, H.M. Fundamental and applied toxicology : official journal of the Society of Toxicology. (1996) [Pubmed]
  16. Mitochondrial HSP60 (P1 protein) and a HSP70-like protein (mortalin) are major targets for modification during S-(1,1,2,2-tetrafluoroethyl)-L-cysteine-induced nephrotoxicity. Bruschi, S.A., West, K.A., Crabb, J.W., Gupta, R.S., Stevens, J.L. J. Biol. Chem. (1993) [Pubmed]
  17. Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation. Craig, E.E., Chesley, A., Hood, D.A. Am. J. Physiol. (1998) [Pubmed]
  18. Hypoglycaemia-induced cell death: features of neuroprotection by the P2 receptor antagonist basilen blue. Cavaliere, F., D'Ambrosi, N., Sancesario, G., Bernardi, G., Volonté, C. Neurochem. Int. (2001) [Pubmed]
  19. Induction of mitochondrial stress proteins following treadmill running. Mattson, J.P., Ross, C.R., Kilgore, J.L., Musch, T.I. Medicine and science in sports and exercise. (2000) [Pubmed]
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