Desensitization of Chemokine Receptor CCR5 in Dendritic Cells at the Early Stage of Differentiation by Activation of Formyl Peptide Receptors
| Autor: | Wanghua Gong, Earl E. Henderson, Thomas J. Rogers, Michele A. Wetzel, Weiping Shen, Ji Ming Wang, Yingying Le |
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| Rok vydání: | 2001 |
| Předmět: |
Chemokine
Receptors CCR5 Receptors Peptide Chemokine receptor CCR5 Immunology Down-Regulation Peptide Chemokine receptor medicine Humans Immunology and Allergy Phosphorylation Receptors Immunologic Receptors Lipoxin Chemokine CCL4 skin and connective tissue diseases Antigen-presenting cell Receptor Chemokine CCL5 chemistry.chemical_classification biology Monocyte virus diseases Cell Differentiation Dendritic Cells Dendritic cell Macrophage Inflammatory Proteins Receptors Formyl Peptide Cell biology medicine.anatomical_structure chemistry Biochemistry HIV-1 biology.protein |
| Zdroj: | Clinical Immunology. 99:365-372 |
| ISSN: | 1521-6616 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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