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B-cell antigen receptor-induced apoptosis requires both Ig alpha and Ig
beta
J Tseng, BJ Eisfelder and MR Clark
Department of Medicine, University of Chicago, IL 60637, USA.
The response of a B cell to antigen is dependent on the surface expression
of a clonotypic B-cell receptor complex (BCR) consisting of membrane-bound
Ig and disulfide-linked heterodimers of Ig alpha/beta. Studies of Ig alpha
or Ig beta have shown that the immunoreceptor tyrosine-based activation
motif (ITAM) found in each cytoplasmic tail is capable of inducing most
receptor signaling events. However, Ig alpha, Ig beta, and most of the
other receptor chains that contain ITAMs, including CD3 epsilon, CD3 gamma,
TCR zeta, and Fc epsilon Rl gamma, are found as components of multimeric
and heterogeneous complexes. In such a complex it is possible that
cooperativity between individual chains imparts functional capacities to
the intact receptor that are not predicted from the properties of its
constituents. Therefore, we developed a novel system in which we could form
and then aggregate dimers, representative of partial receptor complexes,
which contained either Ig alpha alone, Ig beta alone, or the two chains
together and then examine their ability to induce apoptosis in the immature
B-cell line, WEHI-231. Here we present evidence that heterodimers of Ig
alpha and Ig beta efficiently induced apoptosis while homodimers of either
chain did not. Apoptosis was associated with the inductive tyrosine
phosphorylation of a very restricted set of proteins including the tyrosine
kinase Syk. These findings may provide insight into the mechanisms by which
the BCR, and other such multimeric receptor complexes, initiate both
apoptotic and proliferative responses to antigen.
Volume 89,
Issue 5,
pp. 1513-1520,
03/01/1997
Copyright © 1997 by The American Society of Hematology
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