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JBC, Vol. 250, Issue 10, 4025-4027, May, 1975
M. S. Brown, S. E. Dana and J. L. Goldstein
Incubation of monolayers of cultured human fibroblasts with oxygenated
sterols (25-hydroxycholesterol, 7-ketocholesterol, or 6-ketocholestanol)
markedly enhanced the rate at which the cells esterified their endogenous
cholesterol and produced an increase in the cellular content of cholesterol
esters. The enhanced esterification capacity was associated with an
increase in the activity of a membrane-bound fatty acyl-CoA:cholesteryl
acyltransferase. Incubation of cells for 5 hours with 5 mug/ml of
25-hydroxycholesterol produced an 8-fold increase in the specific activity
of this enzyme when assayed in cell-free extracts. Since the oxygenated
sterols that elevated the activity of fatty acyl-CoA:cholesteryl
acyl-transferase also suppressed the activity of 3-hydroxy-3-methylglutaryl
coenzyme A reductase, the data suggest that the processes of cholesterol
ester formation and cholesterol synthesis in human fibroblasts are
regulated in a reciprocal manner by coordinate changes in the activities of
these two membrane-bound enzymes.
Cholesterol ester formation in cultured human fibroblasts. Stimulation by oxygenated sterols
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