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J. Biol. Chem., Vol. 259, Issue 20, 12382-12387, 10, 1984
FR Taylor, SE Saucier, EP Shown, EJ Parish and AA Kandutsch
Support for the role of a cytosolic oxysterol-binding protein in the
regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase was
obtained by correlating the relative binding affinities of a wide range of
oxysterols to their potency in suppressing HMG-CoA reductase activity in
mouse fibroblast cell cultures. Forty-seven oxysterols encompassing a
100-fold range of activity in both assays were tested and the two
parameters were closely correlated for 35 of the sterols. Twelve sterols
showed poor binding when compared to their ability to suppress HMG-CoA
reductase activity in cell cultures. Among these were seven sterols with a
ketone function at C-3. For this group, the discrepancy could be explained
by their rapid conversion within cells to the 3 beta-hydroxy derivatives
which have a much higher affinity for the binding protein. One sterol with
3-keto-4-ene grouping was not reduced to its 3 beta-hydroxy derivative in
cells and thereby showed no discrepancy in the two assays. The remaining
five sterols exhibiting discordant activities in the two tests contained
4,4-dimethyl moieties and were relatively weak suppressors of HMG-CoA
reductase activity. Cellular metabolism of these sterols was not detected.
Possible reasons for their apparent inactivity in the binding assay are
discussed.
Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
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