Differences in phosphorylation of formylpeptide and C5a chemoattractant receptors correlate with differences in desensitization.
作者： H Ali , R.M. Richardson , E.D. Tomhave , J.R. Didsbury , R Snyderman
DOI: 10.1016/S0021-9258(20)80517-1
关键词:
摘要: To define the regulation of chemoattractant receptors, epitope-tagged human formyl peptide and C5a receptor cDNAs (ET-FR ET-C5aR) were stably expressed in rat basophilic leukemia, RBL-2H3 cells. An antibody (12CA5) specific to "ET" was used immunoprecipitate ET-FR ET-C5aR. fMLP caused time- dose-dependent phosphorylation their respective receptors. Phosphorylated migrated as a single broad band between 50 70 kDa on SDS-polyacrylamide gel electrophoresis, whereas ET-C5aR exhibited both fast (39-45 kDa) broadly (39-52 migrating forms. Fast form alone observed at low concentrations (0.001-0.01 microM), or early times (5-30 s) with higher concentration (0.1 microM). Phorbol 12-myristate 13-acetate, thrombin, antigen no but stimulated exclusively The protein kinase C inhibitor staurosporine did not inhibit blocked component phosphorylated Homologous desensitization correlated ligand-induced Of note, underwent heterologous by antigen, phorbol thrombin. data suggest that mediates C5aR FR, yet, receptors are homologously desensitized staurosporine-resistant kinase.
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