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Vol. 9, Issue 2, 483-496, February 1998
1, but Not PLC2, in Antigen-stimulated RBL-2H3
Mast Cells
Department of Pathology and Cancer Research and Treatment Center,
University of New Mexico Health Sciences Center, Albuquerque, New
Mexico 87131
In RBL-2H3 tumor mast cells, cross-linking the high affinity IgE
receptor (Fc
RI) with antigen activates cytosolic tyrosine kinases
and stimulates Ins(1,4,5)P3 production. Using immune
complex phospholipase assays, we show that FcRI cross-linking
activates both PLC
1 and PLC2. Activation is accompanied by the
increased phosphorylation of both PLC isoforms on serine and
tyrosine in antigen-treated cells. We also show that the two PLC
isoforms have distinct subcellular localizations. PLC1 is primarily
cytosolic in resting RBL-2H3 cells, with low levels of plasma membrane
association. After antigen stimulation, PLC1 translocates to the
plasma membrane where it associates preferentially with membrane
ruffles. In contrast, PLC2 is concentrated in a perinuclear region
near the Golgi and adjacent to the plasma membrane in resting cells and
does not redistribute appreciably after FcRI cross-linking. The
activation of PLC1, but not of PLC2, is blocked by wortmannin, a
PI 3-kinase inhibitor previously shown to block antigen-stimulated
ruffling and to inhibit Ins(1,4,5)P3 synthesis. In
addition, wortmannin strongly inhibits the antigen-stimulated
phosphorylation of both serine and tyrosine residues on PLC1 with
little inhibition of PLC2 phosphorylation. Wortmannin also blocks
the antigen-stimulated translocation of PLC1 to the plasma membrane.
Our results implicate PI 3-kinase in the phosphorylation,
translocation, and activation of PLC1. Although less abundant than
PLC2, activated PLC1 may be responsible for the bulk of
antigen-stimulated Ins(1,4,5)P3 production in RBL-2H3
cells.
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