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

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

Research output: Contribution to journalArticlepeer-review

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

Original languageEnglish (US)
Pages (from-to)2887-2894
Number of pages8
JournalBlood
Volume96
Issue number8
DOIs
StatePublished - Oct 15 2000
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

Fingerprint Dive into the research topics of 'Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes'. Together they form a unique fingerprint.

Cite this