The Angiotensin-(1-12)/Chymase axis as an alternate component of the tissue renin angiotensin system.
Mol Cell Endocrinol
; 529: 111119, 2021 06 01.
Article
em En
| MEDLINE
| ID: mdl-33309638
ABSTRACT
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) [N-Asp1-Arg2-Val3-Tyr4-Ile5-His6-Pro7-Phe8-His9-Leu10-Val1-Ile12-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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
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Sistema Renina-Angiotensina
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Angiotensina I
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Angiotensina II
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Angiotensinogênio
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Quimases
Limite:
Animals
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Humans
Idioma:
En
Revista:
Mol Cell Endocrinol
Ano de publicação:
2021
Tipo de documento:
Article