Journal
CLINICA CHIMICA ACTA
Volume 305, Issue 1-2, Pages 191-195Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0009-8981(01)00379-5
Keywords
angiotensin II; angiotensin-converting enzyme; chymase; human; rat; vascular tissue
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We studied the angiotensin II-forming pathways in extracts from human and rat vascular tissues. In the extract from human artery, angiotensin I mainly converted to two products, angiotensin-(l-9) and angiotensin II, while in the extract from rat artery, the major angiotensin I products were angiotensin II and angiotensin-(5-10), The concentrations of angiotensin II and angiotensin-(l-9) generated in the human extract (1 mg protein/ml) after incubation for 30 min were 3.2 and 2.5 nmol, respectively, and that of angiotensin II and angiotensin-(5-10) generated in the rat extract (1 mg protein/ml) were 0.28 and 2.3 nmoI, respectively. In the extract from human vascular tissues, the angiotensin II formation was inhibited by 8% with lisinopril and by 95% with chymostatin. The other product, angiotensin-(l-9) was inhibited completely by carboxypeptidase inhibitor. In the extract from rat vascular tissues, the angiotensin II formation was suppressed to 4% by lisinopril, but not by chymostatin. The angiotensin-(5-10) formation was completely inhibited by chymostatin. These findings suggest clearly that human vascular tissues contain two angiotensin II-forming enzymes, angiotensin-converting enzyme and chymase, but rat vascular tissues have no chymase-dependent angiotensin II-forming pathway. (C) 2001 Elsevier Science B.V. All rights reserved.
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