期刊
JOURNAL OF IMMUNOLOGY
卷 167, 期 7, 页码 3559-3563出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.167.7.3559
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资金
- NHLBI NIH HHS [HL-54166, HL-63372] Funding Source: Medline
Phosphorylation of G protein-coupled receptors and the subsequent recruitment of beta -arrestin play an important role in desensitization of receptor-mediated responses, including degranulation in leukocytes. In this study, we report that receptor phosphorylation also provides a stimulatory signal for CCR ligand 2 (CCL2) production. C3a stimulated degranulation in a basophilic leukemia RBL-2H3 cell expressing wildtype C3aR or a phosphorylation-deficient mutant (Delta ST-C3aR). In contrast, C3a caused CCL2 production only in C3aR but not Delta ST-C3aR cells. Furthermore, overexpression of G protein-coupled receptor kinase 2 resulted in enhancement of both ligand-induced receptor phosphorylation and CCL2 production but inhibition of degranulation. Agonist activation of C3aR, but not Delta ST-C3aR, led to the translocation of green fluorescent protein tagged beta -arrestin 2 from the cytoplasm to the plasma membrane. These data demonstrate that receptor phosphorylation, which provides a turn off signal for degranulation, is essential for CCL2 production.
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