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Originally published In Press as doi:10.1074/jbc.M204604200 on September 16, 2002

J. Biol. Chem., Vol. 277, Issue 47, 44731-44739, November 22, 2002
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Effect of Gangliosides on the Distribution of a Glycosylphosphatidylinositol-anchored Protein in Plasma Membrane from Chinese Hamster Ovary-K1 Cells*

Pilar Maria CrespoDagger , Adolfo Ramón Zurita§, and Jose Luis Daniotti

From the Centro de Investigaciones en Química Biológica de Córdoba, Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, Córdoba 5000, Argentina

Glycosylphosphatidylinositol (GPI)-anchored proteins are clustered mainly in sphingolipid-cholesterol microdomains of the plasma membrane. The distribution of GPI-anchored fusion yellow fluorescent protein (GPI-YFP) in the plasma membrane of Chinese hamster ovary (CHO)-K1 cells with different glycolipid compositions was investigated. Cells depleted of glycosphingolipids by inhibiting glucosylceramide synthase activity or cell lines expressing different gangliosides caused by stable transfection of appropriate ganglioside glycosyltransferases or exposed to exogenous GM1 were transfected with GPI-YFP cDNA. The distribution of GPI-YFP fusion protein expressed at the plasma membrane was studied using the membrane-impermeable cross-linking agent bis(sulfosuccinimidyl)suberate. Results indicate that GPI-YFP forms clusters at the surface of cells expressing GM3, or cells depleted of glycolipids, or transfected cells expressing mainly GD3 and GT3, or GM1 and GD1a, or mostly GM2, or highly expressing GM1. However, no significant changes in membrane microdomains of GPI-YFP were detected in the different glycolipid environments provided by the membranes of the cell lines under study. On the other hand, wild type CHO-K1 cells exposed to 100 µM GM1 before cross-linking with bis(sulfosuccinimidyl)suberate showed a dramatic reduction in the amount of GPI-YFP clusters. These findings clearly indicate that manipulating the glycolipid content of the cellular membrane, just by changing the ganglioside biosynthetic activity of the cell, did not significantly affect the association of GPI-YFP on the cell surface of CHO-K1 cells. The effect of exogenous GM1 gangliosides on GPI-YFP plasma membrane distribution might be a consequence of the ganglioside level reached in plasma membrane and/or the effect of particular ganglioside species (micelles) that lead to membrane architecture and/or dynamic modifications.

* This work was supported in part by Grants 194/00 and 82/01 from Secretaría de Ciencia y Técnología (SECyT)-Universidad Nacional de Córdoba and Ramon Carrillo-Arturo Oñativia from Ministerio de Salud de la Nación Argentina.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Fellow of Ramon Carrillo-Arturo Oñativia from Ministerio de Salud de la Nación Argentina.

§ Fellow of Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET).

Career Investigator of Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). To whom correspondence should be addressed. E-mail: daniotti@dqb.fcq.unc.edu.ar.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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