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This Article Full Text Full Text (PDF) 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 Shen, W. Articles by Wang, J. M. Search for Related Content PubMed PubMed Citation Articles by Shen, W. Articles by Wang, J. M. Related Collections Immunobiology Phagocytes Chemokines, Cytokines, and Interleukins Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 October 2000, Vol. 96, No. 8, pp. 2887-2894 PHAGOCYTES Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes Weiping Shen, Baoqun Li, Michele A. Wetzel, Thomas J. Rogers, Earl E. Henderson, Shao Bo Su, Wanghua Gong, Yingying Le, Robert Sargeant, Dimiter S. Dimitrov, Joost J. Oppenheim, and Ji Ming Wang From the Laboratory of Molecular Immunoregulation and the Laboratory of Experimental and Computational Biology, Division of Basic Sciences, and the Intramural Research Support Program, SAIC Frederick, National Cancer Institute, Frederick, MD; Product Development, Millennium Biotechnology, Ramona, CA; and the Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, PA. Interactions between cell surface receptors are important regulatory elements in the complex host responses to infections. In this study, it is shown that a classic chemotactic factor, the bacterial chemotactic peptide N-formyl-methionyl-leucylphenyl-alanine (fMLF), rapidly induced a protein-kinase-C-mediated serine phosphorylation and down-regulation of the chemokine receptor CCR5, which serves as a major human immunodeficiency virus (HIV)-1 coreceptor. The fMLF binding to its receptor, formyl peptide receptor (FPR), resulted in significant attenuation of cell responses to CCR5 ligands and in inhibition of HIV-1-envelope-glycoprotein-mediated fusion and infection of cells expressing CD4, CCR5, and FPR. The finding that the expression and function of CCR5 can be regulated by peptides that use an unrelated receptor may provide a novel approach to the design of anti-inflamatory and antiretroviral agents. © 2000 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: L. Svensson, E. 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