Abstract
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 C4, 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.
Original language | English (US) |
---|---|
Pages (from-to) | 1025-1030 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 355 |
Issue number | 4 |
DOIs | |
State | Published - Apr 20 2007 |
Keywords
- ATP-binding cassette (ABC)
- ATPase activity
- Cholesterol
- Detergent-resistant membrane
- MRP1
- Transport activity
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology