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Department of Pediatric Oncology, Dana-Farber Cancer Institute, and Department of Pediatrics, Harvard Medical School, Boston, MA 02115
Jurkat T cells activated by the phosphotyrosine phosphatase
inhibitors H2O2 or vanadate were found to have
a similar pattern of tyrosine phosphorylation when compared with T
cells stimulated by anti-CD3 Ab cross-linking, suggesting that
protein tyrosine phosphatase (PTP) inhibitors affect the early steps of
TCR signaling. To study the role of PTPs in the most proximal membrane
events of tyrosine phosphorylation, subcellular fractions of T cells
were treated with the PTP inhibitors in the presence of ATP. In the
membrane fraction, tyrosine phosphorylation of Lck, Fyn, and CD3
can
be induced by PTP inhibitors, but not by anti-CD3. Detailed
characterization of this cell-free system showed that the pattern and
the order of induced tyrosine phosphorylation is similar to that
induced in intact cells. Upon removal of the PTP inhibitor, the
tyrosine-phosphorylated proteins, including Lck, Fyn, Syk, Zap70, and
CD3, are rapidly dephosphorylated. Preliminary characterizations
indicate that a PTP distinct from CD45, SHP1, and SHP2 is present in T
cell membranes and the inhibition of this yet unidentified PTP is most
likely responsible for the Lck-dependent tyrosine phosphorylation
triggered by PTP inhibitors.
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