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Functional differences between two Fc receptor ITAM signaling motifs
IE Van den Herik-Oudijk, MW Ter Bekke, MJ Tempelman, PJ Capel and JG Van de Winkel
Department of Immunology, University Hospital, Utrecht, The Netherlands.
Most Ig receptors exist as multi-subunit complexes with a unique ligand
binding alpha chain and a common signaling FcR gamma-chain. The myeloid Fc
gamma RIIa (CD32) appears unique among FcR because both ligand- binding and
signaling capacity are found in the alpha chain. Within the cytoplasmic
tails of Fc gamma RIIa and FcR gamma-chain similar, but not identical,
activatory motifs (ITAMs) have been defined, in which tyrosines play an
important role. Previously, Fc gamma RIIa-ITAM was shown to be critical for
both proximal and distal activatory functions in IIA1.6 B-cell
transfectants. Triggering of interleukin-2 (IL-2) release and antigen
presentation was absent in Fc gamma RIIa, but not in FcR gamma-chain
receptor complexes. We now assessed the capacity of Fc gamma RIIa wild-type
and Fc gamma RIIa/gamma chimeric molecules to trigger IL-2 production and
antigen presentation by B cells. Both of these functions could solely be
triggered by receptors containing the FcRIIa was capable of functional
interaction with FcR gamma-chain, thus reconstituting the capacity to
trigger IL-2 release and antigen presentation. These data document
qualitative differences between Fc receptor ITAMs.
Volume 86,
Issue 9,
pp. 3302-3307,
11/01/1995
Copyright © 1995 by The American Society of Hematology
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