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Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes

  1. Author:
    Shen, W. P.
    Li, B. Q.
    Wetzel, M. A.
    Rogers, T. J.
    Henderson, E. E.
    Su, S. B.
    Gong, W. H.
    Le, Y. Y.
    Sargeant, R.
    Dimitrov, D. S.
    Oppenheim, J. J.
    Wang, J. M.

  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, DBS, LMI, Bldg 560, Rm 31- 40, Frederick, MD 21702 USA. NCI, Frederick Canc Res & Dev Ctr, DBS, LMI, Frederick, MD 21702 USA. NCI, SAIC Frederick, Div Basic Sci, Lab Expt & Computat Biol, Frederick, MD 21702 USA. NCI, SAIC Frederick, Intramural Res Support Program, Frederick, MD 21702 USA. Millennium Biotechnol, Prod Dev, Ramona, CA USA. Temple Univ, Sch Med, Dept Immunol & Microbiol, Philadelphia, PA 19122 USA.
    1. Year: 2000
  2. Journal: Blood
    1. 96
    2. 8
    3. Pages: 2887-2894
  4. Type of Article: Article
  1. Abstract:

    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-enveiopeglycoprotein- 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. (C) 2000 by The American Society of Hematology.

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