Biochem Biophys Res Commun. 1991 Aug 30;179(1):599-604.

Apoprotein A-1 is a cofactor independent substrate of protein kinase C.

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Department of Surgery, University of Illinois College of Medicine, Chicago 60680.

Abstract

Apoprotein A-1 (apo A-1), the predominant protein constituent of high density lipoproteins (HDL), was phosphorylated by protein kinase C (PKC). Optimal phosphorylation of lipid-free apo A-1 occurs in the absence of calcium, phosphatidyl serine (PS), and diolein (DO). However, HDL-bound apo A-1 was not phosphorylated by PKC. Furthermore, addition of either native or reconstituted HDL particles to lipid-free apo A-1 resulted in a concentration-dependent inhibition of phosphorylation. It appears that the phosphorylatable sites on apo A-1 are involved in hydrophobic interaction with the lipids of HDL. Apo A-1 is a novel substrate of PKC because it does not require calcium and lipid cofactors for optimal phosphorylation.

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Apoprotein A-1 is a cofactor independent substrate of protein kinase C.

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