In vivo modulation of rat liver acyl-coenzyme A:cholesterol acyltransferase by phosphorylation and substrate supply.

Abstract:

:Rats were infused intravenously with a bolus of mevalonolactone or cholesterol-rich chylomicron and microsomes prepared from the livers at times up to 2 h after the infusion. Acyl-CoA cholesterol acyltransferase (ACAT) activity was measured in the microsomes under conditions that define the activity state of the enzyme which recent evidence suggests may depend on the degree of phosphorylation of the enzyme. ACAT activity was increased by both treatments. Some of the observed increase could be attributed to an increase in the supply of substrate cholesterol to the enzyme. The remaining change in activity was consistent with a change in the activity state of ACAT occurring in vivo in response to the influx of cholesterol to the enzyme.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Suckling KE,Stange EF,Dietschy JM

doi

10.1016/0014-5793(83)80410-4

subject

Has Abstract

pub_date

1983-08-08 00:00:00

pages

29-32

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(83)80410-4

journal_volume

159

pub_type

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