Characterization of the 105-kDa molecular chaperone. Identification, biochemical properties, and localization.

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  • Additional Information
    • Source:
      Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
      Original Publication: Berlin, New York, Springer.
    • Subject Terms:
      HSP70 Heat-Shock Proteins/*chemistry ; HSP70 Heat-Shock Proteins/*genetics ; Molecular Chaperones/*chemistry; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Brain/embryology ; Brain/metabolism ; Chromatography, High Pressure Liquid ; Cytosol/metabolism ; Electrophoresis, Polyacrylamide Gel ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/metabolism ; Immunoblotting ; Immunohistochemistry ; Kidney/metabolism ; Male ; Molecular Sequence Data ; Neuroglia/cytology ; PC12 Cells ; Protein Binding ; Protein Structure, Secondary ; Rats ; Rats, Wistar ; Sepharose/pharmacology ; Sequence Homology, Amino Acid ; Testis/embryology ; Testis/metabolism ; Time Factors ; Tissue Distribution
    • Abstract:
      We have characterized the biochemical properties of the testis and brain-specific 105-kDa protein which is cross-reacted with an anti-bovine HSP90 antibody. The protein was induced in germ cells by heat stress, resulting in a protein which is one of the heat shock proteins [Kumagai, J., Fukuda, J., Kodama, H., Murata, M., Kawamura, K., Itoh, H. & Tanaka, T. (2000) Eur. J. Biochem.267, 3073-3078]. In the present study, we characterized the biochemical properties of the protein. The 105-kDa protein inhibited the aggregation of citrate synthase as a molecular chaperone in vitro. ATP/MgCl2 has a slight influence of the suppression of the citrate synthase aggregation by the 105-kDa protein. The protein possessed chaperone activity. The protein was able to bind to ATP-Sepharose like the other molecular chaperone HSP70. A partial amino-acid sequence (24 amino-acid residues) of the protein was determined and coincided with those of the mouse testis- and brain-specific APG-1 and osmotic stress protein 94 (OSP94). The 105-kDa protein was detected only in the medulla of the rat kidney sections similar to OSP94 upon immunoblotting. The purified 105-kDa protein was cross-reacted with an antibody against APG-1. These results suggested that APG-1 and OSP94 are both identical to the 105-kDa protein. There were highly homologous regions between the 105-kDa protein/APG-1/OSP94 and HSP90. The region of HSP90 was also an immunoreactive site. An anti-bovine HSP90 antibody may cross-react with the 105-kDa protein similar to HSP90 in the rat testis and brain. We have investigated the localization and developmental induction of the protein in the rat brain. In the immunohistochemical analysis, the protein was mainly detected in the cytoplasm of the nerve and glial cells of the rat brain. Although the 105-kDa protein was localized in all rat brain segments, the expression pattern was fast in the cerebral cortex and hippocampus and slow in the cerebellum.
    • Accession Number:
      0 (HSP70 Heat-Shock Proteins)
      0 (Heat-Shock Proteins)
      0 (Hspa4l protein, rat)
      0 (Molecular Chaperones)
      0 (Osp94 protein, mouse)
      8L70Q75FXE (Adenosine Triphosphate)
      9012-36-6 (Sepharose)
    • Publication Date:
      Date Created: 20021109 Date Completed: 20030114 Latest Revision: 20200501
    • Publication Date:
      20231215
    • Accession Number:
      10.1046/j.1432-1033.2002.03272.x
    • Accession Number:
      12423363