Dual modulation of hepatic and intestinal acyl-CoA: cholesterol acyltransferase activity by (de-)phosphorylation and substrate supply in vitro

Keith E. Suckling, Eduard F. Strange, John M. Dietschy

Research output: Contribution to journalArticle

39 Scopus citations

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 languageEnglish (US)
Pages (from-to)111-116
Number of pages6
JournalFEBS Letters
Volume151
Issue number1
DOIs
StatePublished - 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

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