Serine protease angiotensin II systems.
BACKGROUND
The introduction of angiotensin converting enzyme (ACE) inhibitors and angiotensin II receptor antagonists has increased our understanding of many aspects of the renin-angiotensin system.
One recent observation is the alternative pathway of angiotensin II formation by serine proteases. So far, two types of angiotensin II-forming serine proteases have been identified: (1) aprotinin-sensitive or kallikrein type which forms bradykinin as well as angiotensin II, depending upon pH conditions. This may make some contribution to the regulation of tissue perfusion, as seen in the ischemic dog heart and the human leg; and (2) chymostatin-sensitive or the chymase type which only forms angiotensin II and may participate in structural remodelling of heart and vessels rather than in tissue perfusion. However, this type has high enzymatic potency and therefore may have other, as yet unknown, functions. Specific inhibitors may help to reveal these functions.
Arakawa
K
K
Department of Internal Medicine, School of Medicine, Fukuoka University, Japan.
D000804:Angiotensin II / Q000378:metabolism*; D000818:Animals; D053818:Chymases; D006801:Humans; D007610:Kallikreins / Q000378:metabolism; D012697:Serine Endopeptidases / Q000145:classification / Q000378:metabolism*
D000804:Angiotensin II; D007610:Kallikreins; D012697:Serine Endopeptidases; D053818:Chymases