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Blood, Vol. 95 No. 5 (March 1), 2000:
pp. 1663-1670
Rapid tyrosine phosphorylation and activation of Bruton's
tyrosine/Tec kinases in platelets induced by
collagen binding or CD32 cross-linking
Atsushi Oda,
Yasuo Ikeda,
Hans D. Ochs,
Brian J. Druker,
Katsutsohi Ozaki,
Makoto Handa,
Tadashi Ariga,
Yukio Sakiyama,
Owen N. Witte, and
Matthew I. Wahl
From the Division of Hematology, Department of Internal Medicine,
and the Blood Center, Keio University, Keio, Japan; the Department of
Microbiology, Immunology, and Molecular Genetics, University of
California at Los Angeles, Los Angeles, CA; the Howard Hughes Medical
Institute; the Department of Pediatrics, University of Washington
School of Medicine, Seattle, WA; the Division of Hematology and Medical
Oncology, Oregon Health Sciences University, Portland, OR; and the
Department of Human Gene Therapy, Hokkaido University School of
Medicine, Sapporo, Japan.
Stimulation of the platelet nonintegrin collagen receptor,
glycoprotein VI, evokes a signaling response similar to that induced by
antigen receptor activation in B and T lymphocytes. A key transducer of
the lymphocyte signaling pathways is the Bruton's tyrosine kinase
(Btk)/Tec kinase family, which connects receptors to the elevation of
intracellular-free calcium levels. An important signaling function for
Btk in collagen-induced platelet activation in vitro was recently
demonstrated by other researchers using Btk-deficient platelets from
patients with X-linked agammaglobulinemia (XLA). Since Btk-deficiency
does not induce an overt platelet-based bleeding disorder in vivo,
collagen receptor responses may include other Btk/Tec kinase family
members in normal platelets. Both Btk and Tec had increased tyrosine
following stimulation of collagen receptors or CD32 cross-linking. Data
from kinetic analyses and inhibitor studies and the use of
phosphopeptide-specific antibodies recognizing 2 Btk regulatory
phosphorylated tyrosine residues suggest a mechanism for coordinate
recruitment of Btk and Tec through the immunoreceptor tyrosine-based
activation motif, Src family kinases, and phosphatidylinositol 3-kinase. In XLA platelets, collagen treatment increased tyrosine phosphorylation of Tec and several other signaling proteins, including Lyn, Fyb, Slp-76, and the Wiskott-Aldrich syndrome protein. This indicates that important elements of the collagen signaling pathway proximal and distal to Btk and Tec are preserved despite the lack of
functional Btk. The results are consistent with the conclusion that
activation of Tec may sustain XLA platelet function in vivo, while some
in vitro assays of nonintegrin collagen receptor signaling through the
Btk/Tec kinase family reflect the additive dosage of the transducers.
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