The biological role of cell membrane domains has been investigated in a number of eukariotic cells, but less attention has been paid to the neuron. In the present investigation, we assessed the changes in lipid and protein composition of detergent-resistant membrane fractions prepared from cultured rat cerebellar granule cells, during differentiation and maturation in vitro. At any stage of the cell life, low-density, detergent-resistant fractions, characterised by the specific presence of prion protein, were enriched in glycolipids, cholesterol, and sphingomyelin. The enrichment in sphingomyelin was developmentally regulated, increasing continuously during cell differentiation and maturation. Concerning proteins, domains were enriched in Fyn and TAG-1, which present exclusively within this fraction at any stage of cell culture, and in GAP-43, mainly during the differentiation stage. On the other side, proteins affecting signal transduction and cytoskeleton-related proteins (heterotrimeric G-proteins, protein kinase C, MARCKS, tubulin), were not enriched within detergent-resistant fractions during cell differentiation, but were recovered within this fraction in mature neurons. These results indicate that during different cellular life stages, specific proteins are recruited within detergent-resistant membrane domains of the neuron and suggest their involvement in specific physiological phenomena (differentiation, maturation and/or aging). (C) 2002 Wiley-Liss, Inc

Palestini, P., Botto, L., Guzzi, F., Calvi, C., Ravasi, D., Masserini, M., et al. (2002). Developmental changes in the protein composition of sphingolipid- and cholesterol-enriched membrane domains of rat cerebellar granule cells. JOURNAL OF NEUROSCIENCE RESEARCH, 67(6), 729-738 [10.1002/jnr.10170].

Developmental changes in the protein composition of sphingolipid- and cholesterol-enriched membrane domains of rat cerebellar granule cells

PALESTINI, PAOLA NOVERINA ADA;BOTTO, LAURA MARIA;GUZZI, FRANCESCA;MASSERINI, MASSIMO ERNESTO;PITTO, MARINA
2002

Abstract

The biological role of cell membrane domains has been investigated in a number of eukariotic cells, but less attention has been paid to the neuron. In the present investigation, we assessed the changes in lipid and protein composition of detergent-resistant membrane fractions prepared from cultured rat cerebellar granule cells, during differentiation and maturation in vitro. At any stage of the cell life, low-density, detergent-resistant fractions, characterised by the specific presence of prion protein, were enriched in glycolipids, cholesterol, and sphingomyelin. The enrichment in sphingomyelin was developmentally regulated, increasing continuously during cell differentiation and maturation. Concerning proteins, domains were enriched in Fyn and TAG-1, which present exclusively within this fraction at any stage of cell culture, and in GAP-43, mainly during the differentiation stage. On the other side, proteins affecting signal transduction and cytoskeleton-related proteins (heterotrimeric G-proteins, protein kinase C, MARCKS, tubulin), were not enriched within detergent-resistant fractions during cell differentiation, but were recovered within this fraction in mature neurons. These results indicate that during different cellular life stages, specific proteins are recruited within detergent-resistant membrane domains of the neuron and suggest their involvement in specific physiological phenomena (differentiation, maturation and/or aging). (C) 2002 Wiley-Liss, Inc
Articolo in rivista - Articolo scientifico
membrane domains; detergent-resistant fractions; glycolipids; differentiation; cerebellar granule cells
English
2002
67
6
729
738
none
Palestini, P., Botto, L., Guzzi, F., Calvi, C., Ravasi, D., Masserini, M., et al. (2002). Developmental changes in the protein composition of sphingolipid- and cholesterol-enriched membrane domains of rat cerebellar granule cells. JOURNAL OF NEUROSCIENCE RESEARCH, 67(6), 729-738 [10.1002/jnr.10170].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/1018
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