|
|
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.
 Previous Article | Table of Contents | Next Article 
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.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
S. Matsuda, S. Yokozaki, H. Yoshida, Y. Kitagishi, N. Shirafuji, and N. Okumura
Insulin receptor substrate protein 53 (IRSp53) as a binding partner of antimetastasis molecule NESH, a member of Abelson interactor protein family
Ann. Onc.,
July 1, 2008;
19(7):
1356 - 1357.
[Full Text]
[PDF]
|
|
|
|
|
|
|
W. Abou-Kheir, B. Isaac, H. Yamaguchi, and D. Cox
Membrane targeting of WAVE2 is not sufficient for WAVE2-dependent actin polymerization: a role for IRSp53 in mediating the interaction between Rac and WAVE2
J. Cell Sci.,
February 1, 2008;
121(3):
379 - 390.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Eto, H. Nishikii, T. Ogaeri, S. Suetsugu, A. Kamiya, T. Kobayashi, D. Yamazaki, A. Oda, T. Takenawa, and H. Nakauchi
The WAVE2/Abi1 complex differentially regulates megakaryocyte development and spreading: implications for platelet biogenesis and spreading machinery
Blood,
November 15, 2007;
110(10):
3637 - 3647.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. Miki, Y. Takegami, K. Okawa, T. Muraguchi, M. Noda, and C. Takahashi
The Reversion-inducing Cysteine-rich Protein with Kazal Motifs (RECK) Interacts with Membrane Type 1 Matrix Metalloproteinase and CD13/Aminopeptidase N and Modulates Their Endocytic Pathways
J. Biol. Chem.,
April 20, 2007;
282(16):
12341 - 12352.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
H. Schulze, M. Korpal, J. Hurov, S.-W. Kim, J. Zhang, L. C. Cantley, T. Graf, and R. A. Shivdasani
Characterization of the megakaryocyte demarcation membrane system and its role in thrombopoiesis
Blood,
May 15, 2006;
107(10):
3868 - 3875.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Mitsushima, T. Sezaki, R. Akahane, K. Ueda, S. Suetsugu, T. Takenawa, and N. Kioka
Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin
Genes Cells,
March 1, 2006;
11(3):
281 - 292.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
B. J. Perrin, K. J. Amann, and A. Huttenlocher
Proteolysis of Cortactin by Calpain Regulates Membrane Protrusion during Cell Migration
Mol. Biol. Cell,
January 1, 2006;
17(1):
239 - 250.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
O. J. T. McCarty, M. K. Larson, J. M. Auger, N. Kalia, B. T. Atkinson, A. C. Pearce, S. Ruf, R. B. Henderson, V. L. J. Tybulewicz, L. M. Machesky, et al.
Rac1 Is Essential for Platelet Lamellipodia Formation and Aggregate Stability under Flow
J. Biol. Chem.,
November 25, 2005;
280(47):
39474 - 39484.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
H. Kashiwagi, M. Shiraga, H. Kato, T. Kamae, N. Yamamoto, S. Tadokoro, Y. Kurata, Y. Tomiyama, and Y. Kanakura
Negative regulation of platelet function by a secreted cell repulsive protein, semaphorin 3A
Blood,
August 1, 2005;
106(3):
913 - 921.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
