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The major platelet integrin
Volume 270,
Number 20,
Issue of May 19, pp. 11927-11934, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
through Cytoskeletal
Reorganization and Tyrosine Phosphorylation in Human Platelets
(glycoprotein IIb-IIIa) has been implicated in the regulation of
tyrosine phosphorylation and dephosphorylation in activated platelets.
To investigate the mechanisms of the
-dependent tyrosine
dephosphorylation, normal platelets or thrombasthenic platelets lacking
were stimulated with thrombin and
fractionated into Triton X-100-soluble or -insoluble subcellular
matrices. We then examined the kinetics of the tyrosine-phosphorylated
proteins and distribution of protein-tyrosine phosphatases in these
fractions and whole cell lysates. First,
-dependent tyrosine
dephosphorylation was recovered mainly in the cytoskeleton with similar
kinetics to the whole cell lysate. Second, protein-tyrosine phosphatase
(PTP) 1B and its cleaved 42-kDa form were associated with the
cytoskeleton in an aggregation-dependent manner, whereas association of
PTP1C with the cytoskeleton was regulated differentially both by
thrombin stimulation and by
-mediated aggregation. Several
calpain inhibitors did not affect either tyrosine phosphorylation and
dephosphorylation or relocation of PTP1B, but they did inhibit cleavage
of PTP1B. Cytochalasin D blocked relocation of both PTP1B and PTP1C but
not PTP1B cleavage. SH-PTP2 was distributed in the other fractions than
the cytoskeleton and showed no relocation on thrombin stimulation.
Finally, the cytoskeleton-associated PTP1C became
tyrosine-phosphorylated in an
-mediated aggregation-dependent
manner. Thus, integrin was
involved differentially in the regulation of PTP1B and PTP1C.
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