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Expression of angiotensin‐converting enzyme activity in cultured pulmonary artery endothelial cells
Author(s) -
del Vecchio Peter J.,
Smith James R.
Publication year - 1981
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041080307
Subject(s) - enzyme , angiotensin converting enzyme , bradykinin , endothelial stem cell , angiotensin ii , renin–angiotensin system , homeostasis , biology , microbiology and biotechnology , cell culture , enzyme assay , biochemistry , endocrinology , in vitro , blood pressure , receptor , genetics
Angiotensin‐converting enzyme (EC 3.4.15.1) is a carboxyterminal dipeptidyl peptidase. The enzyme catalyzes the conversion of the decapeptide angiotensin I to the octapeptide angiotensin II. In addition, the enzyme catabolizes bradykinin. Because of these actions, the enzyme is of pivotal importance in blood pressure homeostasis. Numerous investigators have demonstrated the presence of the enzyme in association with endothelial cells but relatively little is known concerning the factors controlling the expression of enzyme activity by endothelial cells in culture. We have demonstrated that endothelial cells in culture do not express significant amounts of enzyme activity until several days after growth ceases due to high cell density. This is important because it demonstrates a change in function with stage of growth in culture and a possible difference in functional capabilities between nondividing endothelial cells and cells that are dividing in response to injury. Since density‐dependent expression of differentiated traits does not appear to be unique to endothelial cells an understanding of the mechanisms underlying this phenomenon may provide a general explanation for the expression of differentiated traits by cultured cells.