PMID: 9434137Jan 20, 1998Paper

Protein phosphatase 1 and 2A inhibitors activate acyl-CoA:cholesterol acyltransferase and cholesterol ester formation in isolated rat hepatocytes

Biochimica Et Biophysica Acta
M L HernándezB Ochoa

Abstract

Okadaic acid, calyculin A and cantharidin, potent and specific inhibitors of protein phosphatases 1 (PP1) and 2A (PP2A), stimulated both acyl-CoA:cholesterol acyltransferase (ACAT) activity and cholesterol ester formation in suspension cultures of isolated rat hepatocytes. The activation of microsomal ACAT was marked (up to 14-fold the basal values), fast in onset (within 5 min), persistent in duration (up to 45 min) and concentration-dependent. Concentrations of okadaic acid (OA) or calyculin A > or = 100 nM or of cantharidin > or = 1 microM were required to stimulate enzyme activity, which specifically points to a dominant contribution of PP1. No effects were seen with up to 1 microM nor-okadaone, an inactive OA analogue. Rises in [3H]oleate incorporation into cell cholesteryl esters closely paralleled those in ACAT activity, though were somewhat less accentuated. The increases in microsomal ACAT activity seen in OA-, calyculin A- or cantharidin-treated hepatocytes were not linked to changes in bulk microsomal unesterified cholesterol or in the de novo cholesterol synthesis. The findings firmly indicate a role for protein phosphatase activity, probably that of PP1, in controlling the cholesterol esterification rate and ACAT a...Continue Reading

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Citations

Aug 25, 2001·The British Journal of Nutrition·F BrancaH Verhagen

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