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1991 Fiscal Year Final Research Report Summary

Structure, Biosynthesis and Processing of Cathepsin E.

Research Project

Project/Area Number 01580145
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 物質生物化学
Research InstitutionHokkaido University

Principal Investigator

YONEZAWA Satoshi  Hokkaido University Faculty of Science Department of Zoology Lecturer, 理学部, 講師 (90001867)

Project Period (FY) 1989 – 1991
KeywordsCathepsin E / Aspartic proteinase / Primary structure / Processing / Endothelin-converting enzyme / ligosaccharide unit
Research Abstract

Cathepsin E is a member of the aspartic proteinase superfamily. The amino-terminal structure of rat gastric cathepsin E was identified and compared with the corresponding regions of human procathepsin E and other aspartic proteinases. The alignment revealed that cathepsin E has the most extended amino-terminal structure in the superfamily, thus suggesting that the activation peptide(propeptide)of the human enzyme is 39-residues long. Analysis of oligosaccharide units suggested that rat cathepsin E possesses one N-linked carbohydrate unit, probably of the high mannose type. No evidence was obtained for the presence of 0-linked sugars in rat cathepsin E.
Macrophages labelled with[^<35> S]Met for 30 min contained mainly a single radioactive polypeptide immunoprecipitable with polyclonal antibody to rat gastric cathepsin E. The apparent molecular weight of the predominant band was 46kDa. This band was detectable even in 48hr-chased cells, but any newly formed, smaller molecule was not detected in cells chased for 1 to 48hr. When monoclonal-antibody was used as immunoprecipitant, no radioactive peptides were recovered from protein A-Cellulofine beads.
Rat gastric cathepsin E cleaved big endothelin-1, -2 and -3 to generate mature endothelins, under mildly acidic conditions. The reaction was highly for endothelin generation, as judged by amino acid analysis of HPLC separated peptides and by their cross-reactivity with monoclonal antibody to the carboxy-terminal segment of endothelin-1. It was found, however, that human, bovine or rat endothelial cells possessed no detectable amounts of cathepsin E activity, indicating that the enzyme is not responsible for the endothelin production by endothelial cells. Possible participation of cathepsin E in endothelin generation in vivo is discussed in Ref. 3.

  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] Yonezawa,S et al: "Structural Studies of rat cathepsin E:Amino-terminal structure and carbohydrate units ot mature enzyme." Biochem.Biophys.Res.Commun.166. 1032-1038 (1990)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Yonezawa,S et al: "Species-specific distribution of cathepsin E in mammalian blood cells." Biochim.Biophys.Acta. 1073. 155-160 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Yonezawa,S et al: "Production of mature endothelins by cathepsin E in ritro and its biological implications." Zool.Sci.

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Yonezawa,S.et al.: "Two different molecular forms of rat thymus cathepsin E:Procathepsin E is active in acid solution." Zool.Sci.

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Yonezawa,S.: "Structural,Functional and Evolutionary aspects of cathepsin E(Review)"

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Yonezawa, S., et al.: "Structural studies of rat cathepsin E : Amino-terminal structure and carbohydrate units of mature enzyme." Biochem. Biophys. Res. Commun.166 No. 2. 1032-1038 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Yonezawa, S. and Nakamura, K.: "Species-specific distribution of cathepsin E in mammalian blood cells." Biochim. Biophys. Acta. 1073 No. 1. 155-160m (1991)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Yonezawa, S., et al.: "Production of mature endothelins by cathepsin E in vitro and its biological implications." Zool. Sci.

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1993-03-16  

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