Identification of Kallidin Degrading Enzymes in the Isolated Perfused Rat Heart

Access this Article

Author(s)

Abstract

Kallidin (KD) is an important vasoactive kinin whose physiological effects are strongly dependent on its degradation through local kininases. In the present study, we examined the spectrum of these enzymes and their contribution to KD degradation in isolated perfused rat hearts. By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 μM), amastatin (40 μM) and phosphoramidon (1 μM), respectively, relative kininase activities were obtained. APM (44%) and ACE (35%) are the main KD degrading enzymes in rat heart; NEP (7%) plays a minor role. A participation of carboxypeptidase N (CPN) could not be found.

Journal

  • The Japanese Journal of Pharmacology

    The Japanese Journal of Pharmacology 79(1), 117-120, 1999-01

    The Japanese Pharmacological Society

References:  17

Codes

  • NII Article ID (NAID)
    10008194342
  • NII NACSIS-CAT ID (NCID)
    AA00691188
  • Text Lang
    ENG
  • Article Type
    SHO
  • ISSN
    00215198
  • NDL Article ID
    4637064
  • NDL Source Classification
    ZS51(科学技術--薬学)
  • NDL Call No.
    Z53-D199
  • Data Source
    CJP  NDL  J-STAGE 
Page Top