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Production But Not Histamine Release by SHP-1 in RBL-2H3 Mast Cells
Receptors and Signal Transduction Section, OIIB, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892
The SH2-containing protein tyrosine phosphatase1 (SHP-1) is
important for signaling from immune receptors. To investigate the role
of SHP-1 in mast cells we overexpressed the wild-type and the
phosphatase-inactive forms of SHP-1 in rat basophilic leukemia 2H3
(RBL-2H3) mast cell line. The phosphatase-inactive SHP-1 (C453S or
D419A) retains its ability to bind tyrosine phosphorylated substrates
and thereby competes with the endogenous wild-type enzyme.
Overexpression of wild-type SHP-1 decreased the Fc
RI
aggregation-induced tyrosine phosphorylation of the ß and 
subunits of the receptor whereas the dominant negative SHP-1 enhanced
phosphorylation. There were also similar changes in the tyrosine
phosphorylation of Syk. However, receptor-induced histamine release in
the cells expressing either wild-type or dominant negative SHP-1 was
similar to that in the parental control cells. In contrast, compared
with the parental RBL-2H3 cells, FcRI-induced c-Jun N-terminal
kinase phosphorylation and the level of TNF-
mRNA was increased in
the cells overexpressing wild-type SHP-1 whereas the dominant negative
SHP-1 had the opposite effect. The substrate-trapping mutant SHP1/D419A
identified pp25 and pp30 as two major potential substrates of SHP-1 in
RBL-2H3 cells. Therefore, SHP-1 may play a role in allergy and
inflammation by regulating mast cell cytokine
production.
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