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Am J Physiol Heart Circ Physiol 266: H93-H98, 1994;
0363-6135/94 $5.00
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AJP - Heart and Circulatory Physiology, Vol 266, Issue 1 93-H98, Copyright © 1994 by American Physiological Society


ARTICLES

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

X. P. Gao, P. Anding, R. A. Robbins, S. I. Rennard and I. Rubinstein
Department of Internal Medicine, University of Nebraska Medical Center, Omaha 68198-4575.

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 microM) before and after topical application of captopril (10.0 microM) 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 microM)-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.


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