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Biochim Biophys Acta. 2002 Aug 31;1564(2):473-78.

Cholesterol-dependent insertion of glycosylphosphatidylinositol-anchored enzyme.

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Laboratoire de Physico-Chimie Biologique, UMR-CNRS 5013, Bâtiment Chevreul, Université Claude Bernard Lyon I, 43, boulevard du 11 novembre 1918, F-69622 Villeurbanne Cedex, France.


Evidence is now accumulating that the plasma membrane is organized in different lipid and protein subdomains. Thus, glycosylphosphatidylinositol (GPI)-anchored proteins are proposed to be clustered in membrane microdomains enriched in cholesterol and sphingolipids, called rafts. By a detergent-mediated method, alkaline phosphatase, a GPI-anchored enzyme, was efficiently inserted into the membrane of sphingolipids- and cholesterol-rich liposomes as demonstrated by flotation in sucrose gradients. We have determined the enzyme extraluminal orientation. Using defined lipid components to assess the possible requirements for GPI-anchored protein insertion, we have demonstrated that insertion into membranes was cholesterol-dependent as the cholesterol addition increased the enzyme incorporation in simple phosphatidylcholine liposomes.

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