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Journal of Lipid Research, Vol 21, 505-517, Copyright © 1980 by Lipid Research, Inc.
MS Brown and JL Goldstein
The availability of compactin (ML-236B), a potent competitive inhibitor of
3-hydroxy-3-methylglutaryl Coenzyme A reductase, has permitted the
demonstration of a hitherto unsuspected aspect of mevalonate metabolism and
isoprenoid synthesis in cultured mammalian cells. 3-Hydroxy-3-
methylglutaryl Coenzyme A reductase, the enzyme that synthesizes
mevalonate, appears to be regulated through a multivalent feedback
mechanism. Full suppression of the reductase requires the presence of at
least two regulators: 1) cholesterol, which is normally derived exogenously
from plasma low density lipoprotein (LDL), and 2) a nonsterol product,
which is normally synthesized endogenously from mevalonate. Evidence
indicates that both of these regulators of the reductase may be essential
for the growth of mammalian cells in culture. The multivalent feedback
regulation of 3-hydroxy-3- methylglutaryl Coenzyme A reductase, together
with secondary regulatory changes in other enzymes of the sterol synthetic
pathway, coordinates the branched pathway of mevalonate metabolism so as to
assure a constant supply of cholesterol and nonsterol products. These new
findings have important implications for the understanding of isoprenoid
metabolism and its relation to cell growth.
REVIEWS
Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth
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