Multidrug resistance protein 1 is not associated to detergent-resistant membranes

Multidrug resistance protein 1 (MRP1) is a member of the ATP-binding cassette superfamily. Using the energy provided by ATP hydrolysis, it transports a broad spectrum of substrates across the plasma membrane, including hormones, leukotriene C 4, bile salts, and anti-cancer drugs. Recent works have s...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-04, Vol.355 (4), p.1025-1030
Main Authors: Cerf, Emilie, Gasper, Régis, Rychnovsky, Scott, Chang, Xiu-bao, Buyse, Frédéric, Ruysschaert, Jean-Marie
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
ATP-binding cassette (ABC)
ATP-Binding Cassette, Sub-Family B, Member 1 - genetics
ATP-Binding Cassette, Sub-Family B, Member 1 - metabolism
ATPase activity
Biological Transport
Cell Line
Cell Membrane - drug effects
Cell Membrane - metabolism
Cholesterol
Detergent-resistant membrane
Humans
Microscopy, Confocal
MRP1
Octoxynol - pharmacology
Protein Binding
Transport activity
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Summary:Multidrug resistance protein 1 (MRP1) is a member of the ATP-binding cassette superfamily. Using the energy provided by ATP hydrolysis, it transports a broad spectrum of substrates across the plasma membrane, including hormones, leukotriene C 4, bile salts, and anti-cancer drugs. 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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.02.075