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Blood, 15 April 2005, Vol. 105, No. 8, pp. 3141-3148.
Prepublished online as a Blood First Edition Paper on August 3, 2004; DOI 10.1182/blood-2003-04-1319.
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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
WAVE/Scars in platelets
Atsushi Oda,
Hiroaki Miki,
Ikuo Wada,
Hideki Yamaguchi,
Daisuke Yamazaki,
Shiro Suetsugu,
Mineba Nakajima,
Akira Nakayama,
Katsuya Okawa,
Hiroshi Miyazaki,
Kazuhiko Matsuno,
Hans D. Ochs,
Laura M. Machesky,
Hiroyoshi Fujita, and
Tadaomi Takenawa
From the Laboratory of Environmental Biology, Department of Preventive Medicine, Hokkaido University School of Medicine, Sapporo, Japan; the Department of Biochemistry, Institute of Medical Science, University of Tokyo, Tokyo, Japan; the Department of Cell Science, Institute of Biomedical Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan; the Horizontal Medical Research Organization, Kyoto University Faculty of Medicine, Kyoto, Japan; the Pharmaceutical Research Laboratories, Pharmaceutical Division, KIRIN BREWERY CO, LTD, Gunma, Japan; the College of Medical Technology, School of Medicine, Hokkaido University, Sapporo, Japan; the Division of Immunology, Infectious Diseases, and Rheumatology, Department of Pediatrics, School of Medicine, University of Washington, Seattle; the School of Biosciences, Division of Molecular Cell Biology, University of Birmingham, Birmingham, England; and PRESTO, JST, Tokyo, Japan.
Using specific antibodies against isoforms of WAVE (WASP [Wiskott-Aldrich syndrome protein] family Verprolin-homologous protein, also called Scar), we demonstrated that human platelets express all 3 isoforms. With the use of an in vitro pull-down technique, the src homology 3 (SH3) domain of insulin receptor substrate p53 (IRSp53) precipitated WAVE2 from platelet lysates more efficiently than did profilin I. The opposite was true for WAVE1, and neither precipitated WAVE3, suggesting that WAVE isoforms have different affinities to these ligands, while the SH3 domain of abl binds to all 3 isoforms. The 3 WAVE isoforms were distributed in the actin-rich Triton X-100–insoluble pellets following platelet aggregation induced by thrombin receptor–activating peptide. We also found that all 3 WAVE isoforms are substrates for calpain in vivo and in vitro. Although portions of these 3 isoforms were commonly distributed in the actin- and actin-related protein 2 and 3 (Arp2/3)–rich edge of the lamellipodia in spreading platelets, only WAVE2 remained in the cell fringe following detergent extraction or fixation of the cells. Finally, by mass spectrometry, we found that the proteins, which reportedly interact with WAVE/Scars, are present in platelets. These data suggest that the 3 WAVE isoforms exhibit common and distinct features and may potentially be involved in the regulation of actin cytoskeleton in platelets.
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