NDLI: Cross-Desensitization of CCR1, But Not CCR2, Following Activation of the Formyl Peptide Receptor $(FPR1)^{}$

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Cross-Desensitization of CCR1, But Not CCR2, Following Activation of the Formyl Peptide Receptor $(FPR1)^{}$

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Cross-Desensitization of CCR1, But Not CCR2, Following Activation of the Formyl Peptide Receptor $(FPR1)^{}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Song, Changcheng Bednar, Filip Rogers, Thomas J. Cornwell, William Bardi, Giuseppe
Description	Author Affiliation: Bednar F ( Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, PA 19140); Song C ( Center for Inflammation, Translational and Clinical Lung Research, Temple University School of Medicine, Philadelphia, PA 19140.); Bardi G ( Center for Inflammation, Translational and Clinical Lung Research, Temple University School of Medicine, Philadelphia, PA 19140.); Cornwell W ( Center for Inflammation, Translational and Clinical Lung Research, Temple University School of Medicine, Philadelphia, PA 19140.); Rogers TJ ( Center for Inflammation, Translational and Clinical Lung Research, Temple University School of Medicine, Philadelphia, PA 19140 rogerst@temple.edu.)
Abstract	The cross-regulation of G protein-coupled receptors (GPCRs) plays an important role in the immune response. Studies from several laboratories have suggested that a hierarchy of sensitivities to cross-desensitization exists for the chemoattractant GPCRs. We carried out experiments to study the capacity of the formyl peptide receptor-1 (FPR1) to desensitize chemokine receptors CCR1 and CCR2. Our results show that activation of FPR1 resulted in the desensitization and partial internalization of CCR1, but not CCR2, in both primary human monocytes and HEK293 cells coexpressing CCR1, CCR2, and FPR1 (HR1R2F cells). The desensitization of CCR1 by FPR1 stimulation was not due to the simple depletion of the Ca(2+) stores, but was dependent on activation of protein kinase C. Furthermore, we found that the cross-desensitization of CCR1 by FPR1 was associated with CCR1 phosphorylation and moderate reduction of CCR1 cell-surface expression. In contrast, CCR2 was not phosphorylated or internalized after FPR1 activation. Additional studies showed that optimal cross talk between FPR1 and CCR1 was dependent on the functional activity of protein kinase Cß. These results provide a mechanistic basis for the capacity of certain GPCR ligands to exert rapid and selective cross-inactivation of other chemoattractant receptors, and suggest that FPR1 is able to exert 'traffic control' in the migration of inflammatory cells by rapidly inhibiting the cell responses to potentially 'low-priority' chemoattractants such as CCR1 agonists without inhibiting the response to 'higher priority' CCR2 chemoattractants.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1302983
Journal	The Journal of Immunology
Issue Number	11
Volume Number	192
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2014-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Monocytes Immunology Receptors, Ccr1 Receptors, Ccr2 Receptors, Formyl Peptide Calcium Gene Expression Regulation Hek293 Cells Cytology Protein Kinase C Beta Research Support, N.i.h., Extramural Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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Cross-Desensitization of CCR1, But Not CCR2, Following Activation of the Formyl Peptide Receptor $(FPR1)^{}$

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