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  • Title: Conversion of angiotensin I to angiotensin II by chymase activity in human pulmonary membranes.
    Author: Lindberg BF, Gyllstedt E, Andersson KE.
    Journal: Peptides; 1997; 18(6):847-53. PubMed ID: 9285934.
    Abstract:
    An aprotinin-insensitive, angiotensin II (Ang II)-forming chymase has recently been identified in human heart tissue. We studied the hydrolysis of Ang I in human lung membranes. The hydrolysis products Ang II, Ang III, Ang-(1-9), Ang-(2-9), Ang-(1-7) and Ang-(8-10) appeared in membrane preparations from four patients. Two metabolic pathways for the formation of Ang II were identified; one depending on ACE activity (1.4 nmol Ang II/min/mg membrane protein) and the other on serine protease activity (2.1 nmol/min/mg). The serine protease activity was inhibitable to only 30 +/- 8% (mean +/- SEM) by aprotinin, suggesting chymase activity to play a role in the Ang I-conversion of human lung.
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