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Nuclear factor of activated T-cells (NFAT) is a transcriptional
activator that binds to the interleukin-2 promoter and is believed to
be responsible for T-cell-specific interleukin-2 gene expression. Here
we demonstrate using electrophoretic mobility shift assays that nuclear
NFAT can be induced in the rat basophilic leukemia (RBL-2H3) mast cell
line and rat bone marrow-derived mast cells upon cross-linkage of the
high affinity receptor (Fc
Volume 270,
Number 27,
Issue of July 07, pp. 16333-16338, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
RI-mediated
Induction of Nuclear Factor of Activated T-cells
RI) for immunoglobulin E (IgE).
Receptor-dependent activation of NFAT was mimicked by the combination
of the protein kinase C activator phorbol myristate acetate and the
calcium ionophore ionomycin. The induced binding activity was specific
for the NFAT recognition motif because competition with nonradioactive
NFAT oligonucleotide abolished the DNA binding activity, whereas
nonradioactive oligonucleotides recognized by the transcription factors
NF
B, glucocorticoid receptors, and TFIID did not. An
oligonucleotide representing the AP-1 recognition sequence also blocked
the NFAT DNA binding activity, as did a combination of anti-Fos and
anti-Jun antibodies. Using electrophoretic mobility shift assays,
AP-1-binding proteins were found to be induced in RBL-2H3 cells under
the same conditions as was the NFAT binding activity. Together these
data suggest that the NFAT complex in mast cells contains Fos and Jun
proteins as does NFAT in T-cells. The appearance of nuclear NFAT
binding activity was dependent in part upon calcium mobilization, as
buffering the antigen-induced calcium rise with intracellular BAPTA
strongly inhibited NFAT activation. Prevention of calcium influx with
external EGTA also inhibited NFAT activation, indicating that release
of calcium from internal stores was insufficient for sustained
activation of mast cell NFAT. Cyclosporin A, a potent inhibitor of the
calmodulin-dependent phosphatase calcineurin, blocked the induction of
NFAT-DNA binding activity, implicating calcineurin as a key signaling
enzyme in this pathway. These results suggest that NFAT is present in
the mast cell line RBL-2H3 and in primary bone marrow-derived mast
cells, is similar in subunit composition to the T-cell NFAT, and may
play a role in calcium-dependent signal transduction in mast cells.
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