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Volume 271, Number 33, Issue of August 16, 1996 pp. 20182-20186
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Negative Signaling via Fcgamma RIIB1 in B Cells Blocks Phospholipase Cgamma 2 Tyrosine Phosphorylation but Not Syk or Lyn Activation

(Received for publication, December 22, 1995, and in revised form, April 24, 1996)

Sujata Sarkar , Klaus Schlottmann , Damon Cooney and K. Mark Coggeshall

From the Ohio State University, Department of Microbiology, Columbus, Ohio 43210

Crosslinking of the B cell antigen receptor surface immunoglobulin induces tyrosine phosphorylation and activation of the Src family and Syk tyrosine protein kinases, tyrosine phosphorylation of phospholipase Cgamma 2 (PLCgamma 2) and increases in intracellular second messengers inositol phosphates and Ca2+. These activation events, in conjunction with other pathways, culminate in the induction of B cell proliferation and differentiation. In contrast, co-crosslinking surface Ig with the B cell IgG Fc receptor prevents many of these activation events, including B cell proliferation and differentiation. The precise nature of the negative signal(s) derived from Fc receptors that prevent B cell activation is not known. Here, early activation events were examined in B cells stimulated via the antigen receptor alone or under co-crosslinking conditions. The data indicated a selective block in the tyrosine phosphorylation and activation of PLCgamma 2 but not in activation of the upstream kinases, Syk and Lyn, under co-crosslinking conditions. We conclude that the negative signal acts directly on PLCgamma 2 and is consistent with recent studies describing an activation-induced association of a phosphotyrosine phosphatase with tyrosine-phosphorylated B cell Fc receptor.


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