Distribution of angiotensin converting enzyme in human tissues

Abstract Angiotensin converting enzyme (EC 3.4.15.1, dipeptidyl carboxypeptidase, ACE, Kininase II), the peptidase which transforms inactive decapeptide, angiotensin I, to the pressor octapeptide, angiotensin II, and which catalyses also the degradation of vasodilative nonapeptide bradykinin, was measured in 27 human tissue homogenates and physiological fluids. Two assays were used: one which measures the hydrolysis of the substrate hippuryl-glycyl-glycine, by means of high performance liquid chromatography and another, using a colorimetric assay measuring the cleaved glycyl-glycine after arylation with picrylsulfonic acid. All the tissues studied contained measurable converting enzyme activities which were inhibited by captopril (SQ 14.225) in low concentrations. High specific activities of converting enzyme were found in several tissues of the intestinal and urogenital tract, but the highest activity was found in benign prostatic hyperplasia. Normal prostate and prostatic adenocarcinoma have a much lower activity. Results obtained for human tissues are compared with those found in animals.