Direct Evidence for the Presence of a Different Converting Enzyme in the Hamster Cheek Pouch

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Abstract

SUMMARY

Kininase II (angiotensin I-converting enzyme) is generally accepted to be the enzyme responsible for the conversion of angiotensin I (A I) to angiotensin II (A II). This study examined the response of the microvasculature of the hamster cheek pouch to the local application of A I, A II, and the renin substrate, tetradecapeptide (TUP). A I and TDP caused a localized vasoconstriction that was not blocked by converting enzyme inhibitors (CEI; BPFj. for A I and BPF6. and the nonapeptide inhibitor for TDP). However, both the A II antagonist [Sar1, Ala']angiotensin II and the antiserum to A II blocked completely the A I- and TDP-induced vasoconstriction. Sixty-eight percent of the applied A I wat converted to A II in the presence of CEI as well as in its absence. It is concluded that the vasculature of the hamster cheek pouch converts significant amounts of A I to AII by a route that does not involve kininase II. Ore Res 44: 540-644, 1979

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