TY - JOUR AU - MOMBOULI Jean-Vivien AU - BALLARD Kevin D AU - VANHOUTTE Paul M PY - 2016 TI - Kininase-independent potentiation of endothelium-dependent relaxations to kinins by converting enzyme inhibitor perindoprilat. JF - Acta Pharmacologica Sinica; Vol 23, No 3 (March 2002): Acta Pharmacologica Sinica Y2 - 2016 KW - N2 - AIM: The present study examined whether or not the resistance to degradation of bradykinin analogs affects the kinin-potentiating action of the inhibitor of converting enzyme, perindoprilat. METHODS: Hydrolysis of Hyp3,Tyr(Me)8 -bradykinin by ACE present in isolated canine coronary arteries was assessed by determination of peptide metabolites using electrospray mass spectrometry, and compared to that of bradykinin. Contractions and relaxations of isolated rings of coronary arteries, with and without endothelium, were recorded as changes in isometric force. RESULTS: After a 30 min incubation, most of the bradykinin was degraded by the arteries, while less than 10 % of Hyp3,Tyr(Me)8 -bradykinin was hydrolysed. In organ chambers, Hyp3,Tyr(Me)8 -bradykinin like bradykinin caused relaxations of isolated canine coronary arteries with endothelium that could be attributed to both NO and endothelium-derived hyperpolarizing factor (EDHF). Perindoprilat caused a comparable leftward shift in the concentration-relaxation curves for bradykinin and Hyp3,Tyr(Me)8 -bradykinin. CONCLUSION: Impairment of the degradation of bradykinin is not an essential mechanism by which perindoprilat potentiates the actions of kinins. UR - http://www.chinaphar.com/article/view/7152