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Blood, Vol. 92 No. 6 (September 15), 1998:
pp. 1852-1858
RAPID COMMUNICATION
Collagen Induces Tyrosine Phosphorylation of Wiskott-Aldrich Syndrome
Protein in Human Platelets
Atsushi Oda,
Hans D. Ochs,
Brian J. Druker,
Katsutoshi Ozaki,
Chiaki Watanabe,
Makoto Handa,
Yoshitaka Miyakawa, and
Yasuo Ikeda
From the Division of Hematology, Department of Internal Medicine, and
the Blood Center, Keio University, Tokyo, Japan; the Department of
Pediatrics, University of Washington, School of Medicine, Seattle, WA;
and the Division of Hematology and Medical Oncology, Oregon Health
Sciences University, Portland, OR.
Wiskott-Aldrich syndrome (WAS) and X-linked thrombocytopenia (XLT)
are caused by mutations of the WAS protein (WASP) gene. All
hematopoietic stem cell-derived lineages, including platelets, express
WASP. Platelets from WAS patients are smaller than their normal
counterparts and defects in platelet aggregation and actin polymerization have been reported. To determine if WASP is important for normal platelet function, we examined its role in signal
transduction. We found that collagen but not thrombopoietin or thrombin
induces a rapid and robust increase in tyrosine phosphorylation of
platelet-associated WASP. Collagen-induced tyrosine phosphorylation of
WASP was inhibited by cytochalasin D and wortmannin, respectively,
suggesting that actin polymerization and phosphatidylinositol 3-kinase
(PI3-kinase) play a role in the induction of tyrosine phosphorylation
of WASP. Binding of glutathion S-transferase (GST)-Grb2 to WASP was
seen in the lysate of resting platelets. The binding was reduced when lysates from collagen-stimulated platelets were incubated with GST-Grb2, suggesting that tyrosine phosphorylation of WASP may directly
or indirectly modulate the adapter function of WASP. Although thrombin-
and thrombopoietin-induced increase in tyrosine phosphorylation of WASP
is negligible or marginal, WASP from thrombin-activated platelets
became incorporated into the Triton X-100-insoluble 10,000g
sedimentable residue in an aggregation-dependent manner, suggesting
that it may have a regulatory role in platelet cytoskeletal processes
during aggregation. Lastly, we found that WASP is cleaved in response
to activation of calpain, a protease that may have a role in
postaggregation signaling processes. Our data suggest that collagen
specifically induces an increase in tyrosine phosphorylation of WASP
and that WASP is involved in signaling during thrombin-induced aggregation by its redistribution to the cytoskeleton and its cleavage
during aggregation.
© 1998 by The American Society of Hematology.
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