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Hspa9  -  heat shock protein 9

Mus musculus

Synonyms: 74kDa, 75 kDa glucose-regulated protein, C3H-specific antigen, CSA, Csa, ...
 
 
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Disease relevance of Hspa9

 

High impact information on Hspa9

 

Biological context of Hspa9

 

Anatomical context of Hspa9

  • After coupled transcription-translation the precursor of PBP74 is imported into isolated yeast mitochondria, where it becomes processed to the mature protein [1].
  • Here we report the mortalin immunostaining observations on 21 human cell lines [7].
  • Differential subcellular distribution of mortalin in mortal and immortal mouse and human fibroblasts [8].
  • Four patterns of mortalin immunostaining were observed: granular-juxtanuclear cap, granular-gradient from nuclear to cell membrane, granular-juxtanuclear arch, and fibrous-perinuclear [7].
  • The mRNA for GRP75, a mitochondrial chaperone, HSC70, a cytoplasmic chaperone, protein disulfide isomerase, an endoplasmic reticulum chaperone, and C/EBPalpha, a transcription factor, was not regulated [9].
 

Associations of Hspa9 with chemical compounds

  • It was also cloned as glucose regulated protein, GRP75 and peptidebinding protein, PBP74 [5].
  • Western blot analysis indicates that one out of these two residues, arginine at residue 578 in the PBP74/CSA sequence of C3H mouse, contributes to the immunogenicity of CSA [10].
  • These six oxidation-sensitive proteins were identified by mass spectrometry as glial fibrillary acidic protein, creatine kinase BB, disulfide isomerase, chaperonin subunit 5, dihydropyrimidase-related protein 2, and mortalin [11].
  • Conversely, when phosphorylated mortalin was treated with tyrosine phosphatase, its interaction with FGF-1 was abrogated [12].
  • Interestingly, mortalin was preferentially tyrosine phosphorylated at the same time, and when its normally weak phosphorylation in early G1 phase was augmented by treating the cells with vanadate, a strong interaction between mortalin and FGF-1 was established [12].
 

Physical interactions of Hspa9

 

Regulatory relationships of Hspa9

 

Other interactions of Hspa9

  • Western analyses of transient and stable clones revealed that upregulation of p21WAF1 in stable NIH 3T3/mot-2 cells may be mediated by cyclin D1 and cdk-2 [14].
  • Our results show that mortalin and HisRS genes, which map closely to the Egr1 locus, have conserved the 129/Sv haplotype despite numerous back-crossing of the null mice progeny with C57Bl/6J animals [15].
  • Finally, we report the identification of new isoforms of HisRS and mortalin (mot-3) encoded by the 129/Sv haplotype [15].
 

Analytical, diagnostic and therapeutic context of Hspa9

  • By confocal immunofluorescence microscopy PBP74 is detected in mitochondria, colocalizing with the mitochondrial 60-kDa heat shock protein [1].
  • Cell fractionation studies demonstrated PBP74 in purified mitochondria in a protease-protected location [1].
  • To determine the genetic relation between the pancytosolic (uniformly distributed in cytoplasm-p66mot-1) and the perinuclear (p66mot-2) mortalin proteins found in normal and immortal mouse cells, respectively, we initiated the present study using PCR cloning, sequencing, and single nucleotide primer extension analyses [16].
  • In the present study, we report mot-2 cDNA cloning from RS-4 cells--an immortal clone from CD1-ICR mouse embryonic fibroblasts--and the chromosomal assignments of mortalin related genes to mouse chromosomes 18 and X by fluorescence in situ hybridization [17].
  • We describe here the use of quantum dots in mortalin imaging of normal and cancer cells [18].

References

  1. PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein. Dahlseid, J.N., Lill, R., Green, J.M., Xu, X., Qiu, Y., Pierce, S.K. Mol. Biol. Cell (1994) [Pubmed]
  2. Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Domanico, S.Z., DeNagel, D.C., Dahlseid, J.N., Green, J.M., Pierce, S.K. Mol. Cell. Biol. (1993) [Pubmed]
  3. Inactivation of tumor suppressor p53 by mot-2, a hsp70 family member. Wadhwa, R., Takano, S., Robert, M., Yoshida, A., Nomura, H., Reddel, R.R., Mitsui, Y., Kaul, S.C. J. Biol. Chem. (1998) [Pubmed]
  4. Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis. Merrick, B.A., Patterson, R.M., Witcher, L.L., He, C., Selkirk, J.K. Electrophoresis (1994) [Pubmed]
  5. Mortalin: a potential candidate for biotechnology and biomedicine. Wadhwa, R., Taira, K., Kaul, S.C. Histol. Histopathol. (2002) [Pubmed]
  6. Induction of cellular senescence by transfection of cytosolic mortalin cDNA in NIH 3T3 cells. Wadhwa, R., Kaul, S.C., Sugimoto, Y., Mitsui, Y. J. Biol. Chem. (1993) [Pubmed]
  7. Correlation between complementation group for immortality and the cellular distribution of mortalin. Wadhwa, R., Pereira-Smith, O.M., Reddel, R.R., Sugimoto, Y., Mitsui, Y., Kaul, S.C. Exp. Cell Res. (1995) [Pubmed]
  8. Differential subcellular distribution of mortalin in mortal and immortal mouse and human fibroblasts. Wadhwa, R., Kaul, S.C., Mitsui, Y., Sugimoto, Y. Exp. Cell Res. (1993) [Pubmed]
  9. Dietary energy tissue-specifically regulates endoplasmic reticulum chaperone gene expression in the liver of mice. Dhahbi, J.M., Mote, P.L., Tillman, J.B., Walford, R.L., Spindler, S.R. J. Nutr. (1997) [Pubmed]
  10. Antigenic protein specific for C3H strain mouse is a mitochondrial stress-70 protein. Michikawa, Y., Baba, T., Arai, Y., Sakakura, T., Tanaka, M., Kusakabe, M. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  11. Proteomic identification of specific oxidized proteins in ApoE-knockout mice: relevance to Alzheimer's disease. Choi, J., Forster, M.J., McDonald, S.R., Weintraub, S.T., Carroll, C.A., Gracy, R.W. Free Radic. Biol. Med. (2004) [Pubmed]
  12. Cell-cycle dependent tyrosine phosphorylation on mortalin regulates its interaction with fibroblast growth factor-1. Mizukoshi, E., Suzuki, M., Misono, T., Loupatov, A., Munekata, E., Kaul, S.C., Wadhwa, R., Imamura, T. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  13. An N-terminal region of mot-2 binds to p53 in vitro. Kaul, S.C., Reddel, R.R., Mitsui, Y., Wadhwa, R. Neoplasia (2001) [Pubmed]
  14. p53-independent upregulation of p21WAF1 in NIH 3T3 cells malignantly transformed by mot-2. Takano, S., Wadhwa, R., Mitsui, Y., Kaul, S.C. Cell Res. (2001) [Pubmed]
  15. New mortalin and histidyl tRNA synthetase isoforms point out a pitfall in proteomic analysis of Egr1 genetically modified mice. Chardonnet, S., Decottignies, P., Amar, L., Le Caer, J.P., Davis, S., Laroche, S., Le Mar??chal, P. Proteomics (2007) [Pubmed]
  16. Genetic differences between the pancytosolic and perinuclear forms of murine mortalin. Wadhwa, R., Akiyama, S., Sugihara, T., Reddel, R.R., Mitsui, Y., Kaul, S.C. Exp. Cell Res. (1996) [Pubmed]
  17. Mouse and human chromosomal assignments of mortalin, a novel member of the murine hsp70 family of proteins. Kaul, S.C., Wadhwa, R., Matsuda, Y., Hensler, P.J., Pereira-Smith, O.M., Komatsu, Y., Mitsui, Y. FEBS Lett. (1995) [Pubmed]
  18. Mortalin imaging in normal and cancer cells with quantum dot immuno-conjugates. Kaul, Z., Yaguchi, T., Kaul, S.C., Hirano, T., Wadhwa, R., Taira, K. Cell Res. (2003) [Pubmed]
 
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