Abstract:
:Aggregation of the human high-affinity receptor for immunoglobulin G, FcgammaRI, results in initiation of intracellular signaling cascades. However, as the receptor contains no known signaling motif, it is required to recruit an accessory molecule. The gamma chain has been proposed to fulfil this role. Here, we show that in U937 cells differentiated to a more macrophage-like phenotype with dibutyryl cAMP, FcgammaRI no longer signals through the gamma chain but rather uses FcgammaRIIa to initiate tyrosine phosphorylation. Expression of the gamma chain is, however, increased in the dbcAMP-induced cells, but here the gamma chain specifically associates with the IgA receptor, FcalphaRI. Recruitment of the gamma chain either by FcgammaRI in cytokine-primed cells or by FcalphaRI in dbcAMP-induced cells couples ligand binding to the activation of phosphatidyl choline-specific phospholipase D.
journal_name
Eur J Immunoljournal_title
European journal of immunologyauthors
Cameron AJ,Harnett MM,Allen JMdoi
10.1002/1521-4141(200109)31:9<2718::aid-immu2718>3keywords:
subject
Has Abstractpub_date
2001-09-01 00:00:00pages
2718-25issue
9eissn
0014-2980issn
1521-4141pii
10.1002/1521-4141(200109)31:9<2718::AID-IMMU2718>3journal_volume
31pub_type
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