We studied the angiotensin II-forming pathways in extracts from human and r
at 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 angioten
sin II and angiotensin-(5-10), The concentrations of angiotensin II and ang
iotensin-(l-9) generated in the human extract (1 mg protein/ml) after incub
ation for 30 min were 3.2 and 2.5 nmol, respectively, and that of angiotens
in 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 t
issues, the angiotensin II formation was inhibited by 8% with lisinopril an
d by 95% with chymostatin. The other product, angiotensin-(l-9) was inhibit
ed completely by carboxypeptidase inhibitor. In the extract from rat vascul
ar tissues, the angiotensin II formation was suppressed to 4% by lisinopril
, but not by chymostatin. The angiotensin-(5-10) formation was completely i
nhibited 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 ang
iotensin II-forming pathway. (C) 2001 Elsevier Science B.V. All rights rese
rved.