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J. Biol. Chem., Vol. 262, Issue 20, 9649-9655, 07, 1987
MP Reinhart, JT Billheimer, JR Faust and JL Gaylor
We have used isopycnic density gradient centrifugation to study the
distribution of several rat liver microsomal enzymes of cholesterol
synthesis and metabolism. All of the enzymes assayed in the pathway from
lanosterol to cholesterol (lanosterol 14-demethylase, steroid 14-
reductase, steroid 8-isomerase, cytochrome P-450, and cytochrome b5) are
distributed in both smooth (SER) and rough endoplasmic reticulum (RER). The
major regulatory enzyme in the pathway, hydroxymethylglutaryl-CoA
reductase, also was found in both smooth and rough fractions, but we did
not observe any associated with either plasma membrane or golgi. Since
cholesterol can only be synthesized in the presence of these requisite
enzymes, we conclude that the intracellular site of cholesterol
biosynthesis is the endoplasmic reticulum. This is consistent with the
long-held hypothesis. When the overall pathway was assayed by the
conversion of mevalonic acid to non- saponifiable lipids (including
cholesterol), the pattern of distribution obtained in density gradients
verified its general endoplasmic reticulum localization. The enzyme
acyl-CoA-cholesterol acyltransferase which removes free cholesterol from
the membrane by esterification, was found only in the rough fraction of
endoplasmic reticulum. In addition, when the RER was degranulated by the
addition of EDTA, the activity of acyl-CoA-cholesterol acyltransferase not
only shifted to the density of SER but was stimulated approximately 3-fold.
The localization of these enzymes coupled with the stimulatory effect of
degranulation on acyl-CoA-cholesterol acyltransferase activity has led us
to speculate that the accumulation of free cholesterol in the RER membrane
might be a driving factor in the conversion of RER to SER.
Subcellular localization of the enzymes of cholesterol biosynthesis and metabolism in rat liver
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