Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1937921 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
Recent works have suggested that P-glycoprotein is associated to cholesterol and sphingolipid-rich membrane microdomains and that cholesterol upregulates its ATPase and drug transport activities. Confocal microscopy experiments and Triton X-100 extraction of detergent-resistant membranes provide evidence that MRP1 is not located in raft-like structures and that its activity is downregulated by cholesterol. The data are discussed in terms of cholesterol-protein interaction and topology.
Keywords
CFTRNBDLTC4MRP1TMDDRMCRACPGPMRPMβCDAMPABCMDRSSDATP-binding cassette (ABC)HEKP-glycoproteinAdenosine TriphosphateATPadenosine monophosphatecholesterol recognition/interaction amino acid consensusnucleotide-binding domaintransmembrane domaincystic fibrosis transmembrane conductance regulatordetergent-resistant membraneATPase activityTransport activityLeukotriene C4methyl-β-cyclodextrinMultidrug resistancemultidrug resistance proteincholesterolhuman embryonic kidneyATP-binding cassette
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Authors
Emilie Cerf, Régis Gasper, Scott Rychnovsky, Xiu-bao Chang, Frédéric Buyse, Jean-Marie Ruysschaert,