Differential recruitment of accessory molecules by FcgammaRI during monocyte differentiation.

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 Immunol

authors

Cameron AJ,Harnett MM,Allen JM

doi

10.1002/1521-4141(200109)31:9<2718::aid-immu2718>3

keywords:

subject

Has Abstract

pub_date

2001-09-01 00:00:00

pages

2718-25

issue

9

eissn

0014-2980

issn

1521-4141

pii

10.1002/1521-4141(200109)31:9<2718::AID-IMMU2718>3

journal_volume

31

pub_type

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