Dual modulation of hepatic and intestinal acyl‐CoA: cholesterol acyltransferase activity by (de‐)phosphorylation and substrate supply in vitro
- 10 January 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 151 (1), 111-116
- https://doi.org/10.1016/0014-5793(83)80354-8
Abstract
Acyl-CoA: cholesterol acyltransferase (ACAT) activity in microsomes from rat liver and rat intestinal epithelial cells was increased by incubation of the microsomes with the 100 000 × g supernatant fraction in the presence of ATP/MgCl2 and NaF. The measured activity was further increased by including cholesterol-rich liposomes in the preincubation. The ACAT activity in rat liver microsomes could be inhibited by preincubation in the presence of 100 000 × g supernatant and MgCl2 and microsomes preactivated by ATP/MgCl2 could also be inhibited in this way. The results suggest that ACAT activity in vitro is modulated by substrate supply and also reversibly by an ATP-dependent process which may be protein phosphorylation.Keywords
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