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Prepublished online as a Blood First Edition Paper on April 17, 2002; DOI 10.1182/blood-2001-11-0087. This Article Full Text Full Text (PDF) All Versions of this Article: 2001-11-0087v1 99/12/4298    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Nguyen, D. H. Articles by Taub, D. Search for Related Content PubMed PubMed Citation Articles by Nguyen, D. H. Articles by Taub, D. Related Collections Chemokines, Cytokines, and Interleukins Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 June 2002, Vol. 99, No. 12, pp. 4298-4306 CHEMOKINES Cholesterol is essential for macrophage inflammatory protein 1 binding and conformational integrity of CC chemokine receptor 5 Dzung H. Nguyen and Dennis Taub From the Gerontology Research Center, National Institute on Aging, National Institutes of Health, Baltimore, MD. The chemokine receptor, CCR5, is used as a human immunodeficiency virus coreceptor in combination with CD4 during transmission and early infection. CCR5 has been shown to be palmitoylated and targeted to cholesterol- and sphingolipid-rich membrane microdomains termed "lipid rafts." However, the role of cholesterol and lipid rafts on chemokine binding and signaling through CCR5 remains unknown. We found that cholesterol extraction by hydroxypropyl--cyclodextrin (BCD) significantly reduced the binding and signaling of macrophage inflammatory protein 1 (MIP-1) using CCR5-expressing CEM-NKR T cells. Reloading treated cells with cholesterol but not 4-cholesten-3-one, an oxidized form of cholesterol, restored MIP-1 binding to BCD-treated cells. Antibodies specific for distinct CCR5 epitopes lost their ability to bind to the cell surface after cholesterol extraction to varying degrees. Moreover, cells stained with fluorescently labeled MIP-1 extensively colocalized with the GM1 lipid raft marker while using anti-CCR5 antibodies; most of CCR5 on these cells only partially colocalized with GM1, suggesting that active ligand binding facilitates receptor association with lipid rafts or that raft association promotes a higher affinity conformation of CCR5. Together, these data demonstrate that cholesterol and lipid rafts are important for the maintenance of the CCR5 conformation and are necessary for both the binding and function of this chemokine receptor. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J.-E. Alard, M. Dueymes, R. A. Mageed, A. Saraux, P. Youinou, and C. Jamin Mitochondrial heat shock protein (HSP) 70 synergizes with HSP60 in transducing endothelial cell apoptosis induced by anti-HSP60 autoantibody FASEB J, August 1, 2009; 23(8): 2772 - 2779. [Abstract] [Full Text] [PDF] A. Meiser, A. Mueller, E. L. Wise, E. M. McDonagh, S. J. Petit, N. Saran, P. C. Clark, T. J. Williams, and J. E. Pease The Chemokine Receptor CXCR3 Is Degraded following Internalization and Is Replenished at the Cell Surface by De Novo Synthesis of Receptor J. Immunol., May 15, 2008; 180(10): 6713 - 6724. 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	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020