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Titolo:
Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers
Autore:
Vyas, KA; Patel, HV; Vyas, AA; Schnaar, RL;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205USA Johns Hopkins Univ Baltimore MD USA 21205 Mol Sci, Baltimore, MD 21205USA Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 urosci, Baltimore, MD 21205 USA
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 2, volume: 382, anno: 2001,
pagine: 241 - 250
SICI:
1431-6730(200102)382:2<241:SOGGAG>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESONANCE ENERGY-TRANSFER; MELANOMA B16 CELLS; TOXIN-B-SUBUNIT; BIOLOGICAL-MEMBRANES; MONOCLONAL-ANTIBODY; ANCHORED PROTEINS; PLASMA-MEMBRANES; MAMMALIAN-CELLS; RAT-BRAIN; SURFACE;
Keywords:
brain; FRET; microdomains; neurones; sphingolipids; Src family kinases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Schnaar, RL Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205USA Johns Hopkins Univ Baltimore MD USA 21205 timore, MD 21205USA
Citazione:
K.A. Vyas et al., "Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers", BIOL CHEM, 382(2), 2001, pp. 241-250

Abstract

Lateral assemblies of sphingolipids, glycosphingolipids and cholesterol, termed rafts, are postulated to be present in biological membranes and to function in important cellular phenomena. We probed whether rafts are heterogeneous by determining the relative distribution of two gangliosides, GM1 and GD3, in artificial supported monolayers, in intact rat primary cerebellargranule neurones, and in membrane rafts isolated from rat cerebellum. Fluorescence resonance energy transfer (FRET) using fluorophore-labelled cholera toxin B subunit (which binds GM1) and mAb R24 (which binds GD3) revealed that GM1 spontaneously self-associates but does not co-cluster with GD3 in supported monolayers and on intact neurones. Cholera toxin and immunocytochemical labelling of isolated membrane rafts from rat cerebellum further demonstrated that GM1 does not co-localise with GD3. Furthermore, whereas the membrane raft resident proteins Lyn and caveolin both co-localise with GD3 in isolated membrane rafts, GM1 appears in separate and distinct aggregates. These data support prior reports that membrane rafts are heterogeneous, although the mechanisms for establishing and maintaining such heterogeneity remain to be determined.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 02:49:52