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• W2075056638 endingPage "257" @default.
• W2075056638 startingPage "245" @default.
• W2075056638 abstract "Mast cells secrete α- and β-chymases. Primate α-chymases generate angiotensin (AT) II by selectively hydrolyzing AT I’s Phe8–His9 bond. This is distinct from the AT converting enzyme (ACE) pathway. In humans, α-chymase is the major non-ACE AT II-generator. In rats, β-chymases destroy AT II by cleaving at Tyr4–Ile5. Past studies predicted that AT II production versus destruction discriminates α- from β-chymases and that Lys40 in the substrate-binding pocket determines α-chymase Phe8 specificity. This study examines these hypotheses by comparing AT II generation by human α-chymase (containing Lys40), dog α-chymase (lacking Lys40), and mouse mMCP-4 (a β-chymase lacking Lys40; orthologous to AT II-destroying rat chymase rMCP-1). The results suggest that human and dog α-chymase generate AT II exclusively and with comparable efficiency, although dog chymase contains Ala40 rather than Lys40. Furthermore, AT II is the major product generated by degranulation supernatants from cultured dog mast cells, which release tryptases and dipeptidylpeptidase as well as α-chymase. In contrast to rMCP-1, mMCP-4 β-chymase readily generates AT II. Although there is competing AT I hydrolysis at Tyr4, mMCP-4 does not destroy AT II quickly once it is formed. We conclude (1) that chymases are the dominant AT I-hydrolyzing mast cell peptidases, (2) that residues other than Lys40 are key determinants of α-chymase AT I Phe8 specificity, (3) that β-chymases can generate AT II, and (4) that α- and β-chymases are not strictly dichotomous regarding AT I cleavage specificity." @default.
• W2075056638 created "2016-06-24" @default.
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• W2075056638 date "2000-07-01" @default.
• W2075056638 modified "2023-09-23" @default.
• W2075056638 title "Angiotensin II generation by mast cell α- and β-chymases" @default.
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• W2075056638 doi "https://doi.org/10.1016/s0167-4838(00)00076-5" @default.
• W2075056638 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10899625" @default.
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