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Section on Chemical Immunology, Arthritis and Rheumatism Branch, National Institute of Arthritis and Musculoskeletal Diseases, National Institutes of Health, Bethesda, MD 20892
In prior studies aggregation of the high affinity receptors for IgE, Fc
RI, on a rat mast cell line, RBL-2H3, stimulated transcription of the gene for monocyte chemotactic protein-1 (MCP-1) and secretion of the protein. Unexpectedly, those delayed events appeared much less constrained by kinetic proofreading than had been documented for other receptor-initiated responses. The results of the present experiments are consistent with the proposal that the biosynthesis and secretion of MCP-1 result from a soluble messenger formed in the reaction cascades initiated by the receptor, and that Ca2+ could serve as that messenger. Interestingly, whereas receptor-mediated signals were required for transcription of the gene for MCP-1 and secretion of the chemokine, such signals were not required for the intervening step of translation of its mRNA.
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C. Torigoe, J. R. Faeder, J. M. Oliver, and B. Goldstein Kinetic Proofreading of Ligand-Fc{epsilon}RI Interactions May Persist beyond LAT Phosphorylation J. Immunol., March 15, 2007; 178(6): 3530 - 3535. [Abstract] [Full Text] [PDF] |
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