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Desensitization of chemokine receptor CCR5 in dendritic cells at the early stage of differentiation by activation of formyl peptide receptors

  1. Author:
    Le, Y. Y.
    Wetzel, M. A.
    Shen, W. P.
    Gong, W. H.
    Rogers, T. J.
    Henderson, E. E.
    Wang, J. M.

  2. Author Address

    NCI Frederick, DBS, LMI, Bldg 560, Room 31-40, Frederick, MD 21702 USA. NCI Frederick, DBS, LMI, Frederick, MD 21702 USA. NCI Frederick, SAIC Frederick, Intramural Res Support Program, Frederick, MD 21702 USA. Temple Univ, Sch Med, Dept Microbiol & Immunol, Philadelphia, PA 19140 USA.
    1. Year: 2001
  2. Journal: Clinical Immunology
    1. 99
    2. 3
    3. Pages: 365-372
  4. Type of Article: Article
  1. Abstract:

    Chemokine receptors are subjected to heterologous desensitization by activation of formyl peptide receptors, We investigated the cross-talk between formyl peptide receptors and the chemokine receptor CCR5 in human monocyte- differentiated immature dendritic cells (iDC), Monocytes cultured with GM-CSF and IL-4 for 4 days exhibit markers characteristic of iDC and maintain the expression of both formyl peptide receptors FPR and FPRL1, as well as CCR5, Pretreatment of IDC with W peptide (WKYMVm), a potent agonist for FPR and FPRL1 but with preference for FPRL1, resulted in down-regulation of CCR5 from the cell surface and reduced cell response to the CCR5 ligands through a PKC-dependent pathway. Furthermore, W peptide induced a PKC-dependent phosphorylation of CCR5 and inhibited infection of iDC by R5 HIV-1. Our results indicate that the expression and functions of CCR5 in IDC can be attenuated by W peptide, which activates formyl peptide receptors, and suggest an approach to the design of novel anti- HIV-1 agents. (C) 2001 Academic Press.

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