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  • Journal
    Digital Access
    Provider
    Version
    Oxford
    v. 42-, 2002-
    JSTOR
    v. 42-, 2002- Full text delayed 6+ years
    BioOne
    v. 42-45, no. 5, 2002-07.
  • Article
    Cornish KG, Joyner WL, Gilmore JP.
    Circ Res. 1979 Apr;44(4):540-4.
    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 (TDP). A I and TDP caused a localized vasoconstriction that was not blocked by converting enzyme inhibitors (CEI: BPF5a for A I and BPF5a and the nonapeptide inhibitor for TDP). However, both the A II antagonist [Sar1, Ala8]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 was 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 A II by a route that does not involve kininase II.
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