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Originally published In Press as doi:10.1074/jbc.M010666200 on March 22, 2001

J. Biol. Chem., Vol. 276, Issue 24, 21136-21145, June 15, 2001
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Changes in the Lipid Turnover, Composition, and Organization, as Sphingolipid-enriched Membrane Domains, in Rat Cerebellar Granule Cells Developing in Vitro*

Alessandro Prinetti, Vanna Chigorno, Simona Prioni, Nicoletta Loberto, Nadia MaranoDagger , Guido Tettamanti, and Sandro Sonnino§

From the Study Center for the Functional Biochemistry of Brain Lipids, Department of Medical Chemistry and Biochemistry-Laboratorio Interdisciplinare Tecnologie Avanzate, Medical School, University of Milan, Segrate, Italy 20090

In the present paper, we report on the properties of sphingolipid-enriched domains of rat cerebellar granule cells in culture at different stages of neuronal development. The major lipid components of these domains were glycerophospholipids and cholesterol. Glycerophospholipids were 45-75% and cholesterol 15-45% of total lipids of the domains. This corresponded to 5-17% of total cell glycerophospholipids and 15-45% of total cell cholesterol. Phosphatidylcholine, mainly dipalmitoylphosphatidylcholine, was 66-85% of all the glycerophospholipids associated with these domains. Consequently, the palmitoyl residue was significantly enriched in the domains. The surface occupied by these structures increased during development. 40-70% of cell sphingolipids segregated in sphingolipid-enriched membrane domains, with the maximum ganglioside density in fully differentiated neurons. A high content of ceramide was found in the domains of aging neurons. Then, the sphingolipid/glycerophospholipid molar ratio was more than doubled during the initial stage of development, whereas the cholesterol/glycerophospholipid molar ratio gradually decreased during in vitro differentiation. Phosphorylated phosphoinositides, which were scant in the domains of undifferentiated cells, dramatically increased during differentiation and aging in culture. Proteins were minor components of the domains (0.1-2.8% of all domain components). Phosphotyrosine-containing proteins were selectively recovered in the sphingolipid-enriched domain. Among these, Src family protein-tyrosine kinases, known to participate to the process of neuronal differentiation, were associated with the sphingolipid-enriched domains in a way specific for the type of kinase and for the developmental stage of the cell. Proteins belonging to other signaling pathways, such as phosphoinositide 3-kinase and its downstream target, Akt, were not associated with the domains.

* This research was supported by the Cofinanziamento Ministero dell' Università e delle Ricerca Scientifica e Tecnologica Progetti di Interesse Nazionale (MURST PRIN) 1997 (to S. S. and G. T.), Cofinanziamento MURST PRIN 1998 (to V. C.), and by Consiglio Nazionale delle Ricerche (Target project Biotechnology to G. T. and S. S.), Italy.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 Permanent address: Dept. of Chemistry, Saint Lawrence University, Canton, NY 13617.

§ To whom correspondence should be addressed: Dipartimento di Chimica e Biochimica Medica-LITA-Segrate, Via Fratelli Cervi 93, 20090 Segrate, Milano, Italy. Tel.: 39-02-2642-3204; Fax: 39-02-2642-3209; E-mail: Sandro.Sonnino@unimi.it.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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