Peptidases modulate bradykinin-induced arteriolar dilation in the hamster cheek pouch

X. P. Gao, P. Anding, R. A. Robbins, S. I. Rennard, I. Rubinstein

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

The purpose of this study was to investigate whether angiotensin- converting enzyme (ACE; EC 3.4.15.1) and neutral endopeptidase (NEP; EC 3.4.24.11), two membrane-bound metalloenzymes that are widely distributed in the peripheral microcirculation and degrade kinins very effectively, modulate bradykinin-induced arteriolar dilation in vivo. Using intravital microscopy, we measured diameter of second-order arterioles in the hamster cheek pouch during suffusion of bradykinin (0.1-10.0 μM) before and after topical application of captopril (10.0 μM) and phosphoramidon (10.0 nM). We found that each inhibitor significantly potentiated bradykinin-induced increase in arteriolar diameter (P < 0.05). Suffusion of other proteinase inhibitors (excluding ACE and NEP inhibitors) had no significant effect on bradykinin- induced responses. Captopril and phosphoramidon did not potentiate isoproterenol (0.1 μM)-induced arteriolar dilation in the cheek pouch. Collectively, these data indicate that ACE and NEP each plays an important role in regulating bradykinin-induced vasorelaxation in the peripheral microcirculation in vivo.

Original languageEnglish (US)
Pages (from-to)H93-H98
JournalAmerican Journal of Physiology - Heart and Circulatory Physiology
Volume266
Issue number1 35-1
DOIs
StatePublished - 1994

Keywords

  • angiotensin-converting enzyme
  • endothelium
  • isoproterenol
  • microcirculation
  • neutral endopeptidase
  • proteinase inhibitors
  • proteinases

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine
  • Physiology (medical)

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