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J. Biol. Chem., Vol. 266, Issue 16, 10104-10111, Jun, 1991
AJ Mendez, JF Oram and EL Bierman
The interaction of high density lipoproteins (HDL) with the HDL receptor
stimulates the translocation of cholesterol from intracellular pools to the
plasma membrane where the cholesterol becomes available for removal by
appropriate acceptors. The role of signal transduction through protein
kinase C in HDL receptor-dependent cholesterol translocation and efflux was
examined using cholesterol-loaded cultured human skin fibroblasts.
Treatment of cells with HDL3 activated protein kinase C, demonstrated by a
transient increase in membrane associated kinase activity. Kinase
activation appeared to be dependent on binding of HDL3 to the HDL receptor,
since tetranitromethane-modified HDL3, which does not bind to the receptor,
was without effect. Translocation of intracellular sterol to the plasma
membrane was stimulated by treatment of cells with the protein kinase C
activators, dioctanoylglycerol and phorbol myristic acetate, and the
calcium ionophore A23187. Conversely, treatment of cells with sphingosine,
a protein kinase C inhibitor, reduced HDL3-mediated translocation and
efflux of intracellular sterols. However, sphingosine had no effect on
efflux of labeled cholesterol derived from the plasma membrane. Down-
regulation of cellular protein kinase C activity by long term incubation
with phorbol esters also inhibited HDL3-mediated efflux of intracellular
sterols and abolished the ability of sphingosine to further inhibit
HDL3-mediated efflux. These studies support the conclusion that HDL
receptor-mediated translocation and efflux of intracellular cholesterol
occurs through activation of protein kinase C.
Protein kinase C as a mediator of high density lipoprotein receptor- dependent efflux of intracellular cholesterol
University of Washington, Department of Medicine, Seattle 98195.
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