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      ATP-binding cassette transporters are enriched in non-caveolar detergent-insoluble glycosphingolipid-enriched membrane domains (DIGs) in human multidrug-resistant cancer cells.

      The Journal of Biological Chemistry
      ATP-Binding Cassette Transporters, chemistry, physiology, Adenosine Triphosphate, Caveolae, metabolism, Cell Line, Tumor, Cell Membrane, Chemokines, CC, biosynthesis, Detergents, pharmacology, Drug Resistance, Multiple, Glycosphingolipids, Humans, Immunoblotting, Immunohistochemistry, Octoxynol, P-Glycoprotein, Polyethylene Glycols, Precipitin Tests, Protein Structure, Tertiary, Reverse Transcriptase Polymerase Chain Reaction

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          Abstract

          In this study we show that P-glycoprotein in multidrug-resistant 2780AD human ovarian carcinoma cells and multidrug resistance-associated protein 1 in multidrug-resistant HT29col human colon carcinoma cells are predominantly located in Lubrol-based detergent-insoluble glycosphingolipid-enriched membrane domains. This localization is independent of caveolae, since 2780AD cells do not express caveolin-1. Although HT29col cells do express caveolin-1, the ATP-binding cassette transporter and caveolin-1 were dissociated on the basis of differential solubility in Triton X-100 and absence of microscopical colocalization. While both the multidrug resistance-associated protein 1 and caveolin-1 are located in Lubrol-based membrane domains, they occupy different regions of these domains.

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