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Activation of the chemotactic peptide receptor FPRL1 in monocytes phosphorylates the chemokine receptor CCR5 and attenuates cell responses to selected chemokines

  1. Author:
    Shen, W. P.
    Proost, P.
    Li, B. Q.
    Gong, W. H.
    Le, Y. Y.
    Sargeant, R.
    Murphy, P. M.
    Van Damme, J.
    Wang, J. M.

  2. Author Address

    Wang JM NCI, Frederick Canc Res & Dev Ctr, Div Basic Sci, Mol Immunoregulat Lab Bldg 560,Room 31-40 Frederick, MD 21701 USA NCI, Frederick Canc Res & Dev Ctr, Div Basic Sci, Mol Immunoregulat Lab Frederick, MD 21701 USA Katholieke Univ Leuven, Rega Inst, Lab Mol Immunol Louvain Belgium NCI, Frederick Canc Res & Dev Ctr, SAIC, Intramural Res Support Program Frederick, MD 21702 USA ProSci Inc, Prod Dev Poway, CA 92064 USA NIAID, Host Def Lab, NIH Bethesda, MD 20892 USA
    1. Year: 2000
  2. Journal: Biochemical and Biophysical Research Communications
    1. 272
    2. 1
    3. Pages: 276-283
  4. Type of Article: Article
  1. Abstract:

    FPRL1 is a seven-transmembrane (STM), G-protein coupled receptor which was originally identified as a low affinity receptor for the bacterial chemotactic formyl peptide and a high affinity receptor for the Lipid metabolite lipoxin A4. me recently discovered that a number of peptides, including several synthetic domains of the HIV-1 envelope proteins and the serum amyloid A, use FPRL1 to induce migration and calcium mobilization in human monocytes and neutrophils. In this study, we report that a synthetic peptide domain of the V3 region of the HIV-1 envelope gp120, activates the FPRL1 receptor in monocytes and neutrophils. Furthermore, monocytes prestimulated with V3 peptide showed reduced response to several chemokines that use multiple cell receptors. This is associated with a rapid phosphorylation of the chemokine receptor CCR5 on the serine residues. Our study suggests that FPRL1, as a classical chemoattractant receptor, may play an important role in modulating monocyte activation in the presence of multiple stimuli. (C) 2000 Academic Press. [References: 34]

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