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Cloning of a kinin-tensin enzyme and kinin-destruction enzyme in the dog heart

Research Project

Project/Area Number 08670838
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Circulatory organs internal medicine
Research InstitutionFukuoka University

Principal Investigator

SASAGURI Manabu  Fukuoka University, School of Medicine, Instructor, 医学部, 講師 (00178675)

Co-Investigator(Kenkyū-buntansha) NODA Keita  Fukuoka University, School of Medicine, Instructor, 医学部, 講師 (70289536)
Project Period (FY) 1996 – 1997
Project Status Completed (Fiscal Year 1997)
Budget Amount *help
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1997: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1996: ¥1,200,000 (Direct Cost: ¥1,200,000)
Keywordskallikrein / angiotensin / kinin / kinin-tensin enzyme
Research Abstract

We have previously shown that the purified kinin-forming enzyme from the dog heart is similar to tissue kalikrein and is also able to convert angiotensin (Ang) I to Ang II.The aim of the present study is to clarify the structure and tissue localization of this enzyme. Antiserum against the purified enzyme from the heart was raised in rabbits. Western blot analysis indicated the presence of this enzyme not only the heart (atria, ventiricule, coronary artery) but also other tissues such as sorta, kidney, pancreas, small intestine, and skeletal muscle. Its presence was also demonstrated in MDCK cell originated fron canine distal tubules. The kallikrein-like enzyme has been purified from homogenates of the kidney and aorta by a DEAE-Sepharose and aprotinin affinity columnn. Purified enzyme from the kidney and aorta was visualized at the relative molecular weight of 65 kDa on Western blotting which is identical to that of the kallikrein-like enzyme purified from the heart. The porified enzyme from the heart was proceeded to amino acid composition and sequence analysis. It was cleaved by lysyl-endopeptidase at 37゚C for 14 hrs and fractionated on a C18 column with a linear (0-90%) acetonitrile gradient in 0.1% trigluoroacetic acid. After fractionation, it was used for sequence analysis. However, the amino acid composition of purified kallikrein-like enzeme from the heart was different from that of dog urinary kallikrein. It has N-terminal bloked amino acid. the present study has shown that kallikrein-like enzyme is distributed not only in the heart, but also in the other tissues such as aorta, kidney, pancreas, small intestine, and skeletal muscle. This enzyme may exert pathophysiological effects through generating kinins and Ang II.The cloning og this enzyme iks now ongoing using antibody against the enzyme.

Report

(3 results)
  • 1997 Annual Research Report   Final Research Report Summary
  • 1996 Annual Research Report
  • Research Products

    (11 results)

All Other

All Publications (11 results)

  • [Publications] Sasaguri M et al.: "Purification and charaterization of a kinin-and angiotensin II-forming enzyme in the dog heart." J Hypertens. 15. 675-682 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Sasaguri M et al.: "Structure of kallikrein-like enzyme and its tissue localization in the dog.(Abstract)" J Hypertens. (in press).

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Sasaguri M et al.: "“Kallikrein:Physiological role in angiotensin II formation"" “Drugs,Enzymes and receptors of the renin angiotensin system.A century of discovery"Robert. M Graham Edited.Harwood Academic Publishers/Gordon and Breach Science International Publishers. (in press).

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Sasaguri M et al.: "“Role of Kallikrein in Alternative Angiotensin II Formation"" “Receptors in Cardiovascular Disease"published in Mediphacs.Healthmark.(in Press).

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Sasaguri M,Maeda H,Noda K,Tsuji E,Kinoshita A,Ideishi M,Ogata S,Arakawa K.: "Purification and characterization of a kinin-and angiotensin II-forming enzyme in the dog heart" J Hypertens. 15. 675-682 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Sasaguri M,Noda K,Tsuji E,Kinoshita A,Ideishi M,Ogata S,Arakawa K.: "Structure of kallikrein-like enzyme and its tissue localization in the dog. (Abstract)" J Hypertens. (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Sasaguri M and Arakawa K.: ""Kallikrein : Physiological role in angiotensin II formation"" "Drugs, Enzymes and receptors of the renin angiotensin system. A century of discovery". Robert M Graham Edited. Harwood Academic Publishers/Gordon and Breach Science International Publishers (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Sasaguri M and Arakawa K.: ""Role of Kallikrein in Alternative Angiotensin II Formation"" "Receptors in Cardiovascular Disease". published in Mediphacs. Healthmark. (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] M.Sasaguri et al.: "Purification and characterization of a kinin-and angiotensin II-forming enzyme in the dog heart" J Hypertens. 15. 675-682 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] M.Sasaguri,et al: "Characterization of a kinin-tensin enzyme in the dog heart" Hypertens Res (abstract). 18. 334 (1995)

    • Related Report
      1996 Annual Research Report
  • [Publications] M.Sasaguri,et al: "Purification and characterization of a kinin-and angiotensin II-forming enzyme in the dog heart." J Hypertens (abstract). 14(Suppl 1). S141 (1995)

    • Related Report
      1996 Annual Research Report

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Published: 1996-04-01   Modified: 2016-04-21  

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