The Angiotensin-(1-12)/Chymase axis as an alternate component of the tissue renin angiotensin system

被引：12
作者：
Ferrario, Carlos M. [1 ]
Groban, Leanne [2 ]
Wang, Hao [2 ]
Cheng, Che Ping [3 ]
VonCannon, Jessica L. [1 ]
Wright, Kendra N. [1 ]
Sun, Xuming [2 ]
Ahmad, Sarfaraz [1 ]
机构：
[1] Wake Forest Sch Med, Dept Surg & Physiol Pharmacol, Winston Salem, NC 27157 USA
[2] Wake Forest Sch Med, Dept Anesthesiol, Winston Salem, NC 27157 USA
[3] Wake Forest Sch Med, Dept Internal Med, Sect Cardiovasc Med, Winston Salem, NC 27157 USA
来源：
MOLECULAR AND CELLULAR ENDOCRINOLOGY | 2021年 / 529卷
关键词：
Renin-angiotensin system; Angiotensinogen; Angiotensin peptides; Angiotensin-(1-12); Angiotensin I; Angiotensin II; Renin; Chymase; Angiotensin-converting enzyme; Metabolism; ACUTE MYOCARDIAL-INFARCTION; CONVERTING ENZYME; CHYMASE INHIBITOR; BLOOD-PRESSURE; BONE-MARROW; DIFFERENTIAL EXPRESSION; DIASTOLIC DYSFUNCTION; OXIDATIVE STRESS; CARDIAC TISSUE; DIABETIC-RATS;
D O I：
10.1016/j.mce.2020.111119
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
The identification of an alternate extended form of angiotensin I composed of the first twelve amino acids at the N-terminal of angiotensinogen has generated new knowledge of the importance of noncanonical mechanisms for renin independent generation of angiotensins. The human sequence of the dodecapeptide angiotensin-(1-12) [NAsp(1)-Arg(2)-Val(3)-Tyr(4)-Ile(5)-His(6)-Pro(7)-Phe(8)-His(9)-Leu(10)-Val(11)-Ile(12)-COOH] is an endogenous substrate that in the rat has been documented to be present in multiple organs including the heart, brain, kidney, gut, adrenal gland, and the bone marrow. Newer studies have confirmed the existence of Ang-(1-12) as an Ang II-forming substrate in the blood and heart of normal and diseased patients. Studies to-date document that angiotensin II generation from angiotensin-(1-12) does not require renin participation while chymase rather than angiotensin converting enzyme shows high catalytic activity in converting this tissue substrate into angiotensin II directly.
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页数：7
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