Presence of a closely related subgroup in the aldo-ketoreductase family of the mouse.

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  • Author(s): Gui T;Gui T; Tanimoto T; Kokai Y; Nishimura C
  • Source:
    European journal of biochemistry [Eur J Biochem] 1995 Jan 15; Vol. 227 (1-2), pp. 448-53.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • 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:
      Aldehyde Reductase/*genetics; Aldehyde Reductase/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Southern ; DNA, Complementary ; Escherichia coli/genetics ; Humans ; Mice ; Molecular Sequence Data ; RNA, Messenger/genetics ; Rats ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity
    • Abstract:
      Aldose reductase (alditol:NAD(P)+ 1-oxidoreductase), an enzyme implicated in the pathogenesis of various diabetic complications, catalyzes the reduction of a variety of aldehydes. From a mouse kidney library, we isolated aldose reductase cDNA that encodes a 316-amino-acid protein with approximately 97% identity to rat lens aldose reductase, approximately 69% identity to the mouse vas deferens protein and also approximately 69% identity to mouse fibroblast growth-factor-1-regulated protein. RNA-blot analysis demonstrated abundant expression of the enzyme transcript in the testis, skeletal muscle and kidney. However, a very low level of the transcript was detected in the sciatic nerve and lens, where abundant expression and involvement of the enzyme in diabetic complications were documented in other animals species. The isolated cDNA was expressed in Escherichia coli and the recombinant protein was purified to homogeneity by affinity chromatography and chromatofocusing. The expressed enzyme demonstrated reductase activity for various aldo sugars but not for the steroids. The enzyme reaction with DL-glyceraldehyde was, however, competitively inhibited by progesterone or 17 alpha-hydroxyprogesterone. The results not only indicate a unique tissue distribution and enzyme attribute of mouse aldose reductase, but also the presence of a closely related subgroup within the aldo-oxidoreductase superfamily in mouse tissues.
    • Molecular Sequence:
      GENBANK D32250
    • Accession Number:
      0 (DNA, Complementary)
      0 (RNA, Messenger)
      0 (Recombinant Proteins)
      EC 1.1.1.21 (Aldehyde Reductase)
    • Publication Date:
      Date Created: 19950115 Date Completed: 19950313 Latest Revision: 20190620
    • Publication Date:
      20240829
    • Accession Number:
      10.1111/j.1432-1033.1995.tb20408.x
    • Accession Number:
      7851421