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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.
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