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.
Original language | English (US) |
---|---|
Pages (from-to) | 111-116 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 151 |
Issue number | 1 |
DOIs | |
State | Published - Jan 10 1983 |
Keywords
- Acyl-CoA: cholesterol acyltransferase
- Liposomes
- Rat Liver
- Rat intestine Phosphorylation
- Regulation
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology