Novel synthetic collagen fibers, poly(PHG), stimulate platelet aggregation through glycoprotein VI

Inoue, Osamu; Suzuki-Inoue, Katsue; Shinoda, Daisuke; Umeda, Yasuto; Uchino, Masazumi; Takasaki, Sin-ichi; Ozaki, Yukio

doi:10.1016/j.febslet.2008.11.026

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Volume 583, Issue 1 , Pages 81-87, 5 January 2009

Novel synthetic collagen fibers, poly(PHG), stimulate platelet aggregation through glycoprotein VI

Edited by Veli-Pekka Lehto

Osamu Inoue
- Department of Clinical and Laboratory Medicine, Faculty of Medicine, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi 409-3898, Japan
Katsue Suzuki-Inoue
- Department of Clinical and Laboratory Medicine, Faculty of Medicine, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi 409-3898, Japan
Daisuke Shinoda
- Department of Clinical and Laboratory Medicine, Faculty of Medicine, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi 409-3898, Japan
Yasuto Umeda
- Chisso Corporation Yokohama Research Center, 5-1, Ookawa, Kanazawa-ku, Yokohama 236-8605, Japan
Masazumi Uchino
- Chisso Corporation Yokohama Research Center, 5-1, Ookawa, Kanazawa-ku, Yokohama 236-8605, Japan
Sin-ichi Takasaki
- Chisso Corporation Yokohama Research Center, 5-1, Ookawa, Kanazawa-ku, Yokohama 236-8605, Japan
Yukio Ozaki
- Department of Clinical and Laboratory Medicine, Faculty of Medicine, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi 409-3898, Japan
- Corresponding author. Fax: +81 55 273 6713.

Received 5 September 2008; received in revised form 17 November 2008; accepted 21 November 2008. published online 05 December 2008.

Abstract

Novel synthetic collagen fibers, poly(PHG) made by polycondensation of Pro-Hyp-Gly, spontaneously assume polymeric structure with molecular weights greater than 10⁵. Its application for biomaterials has been explored, but that for a platelet agonist has not been investigated. Poly(PHG)-induced platelet aggregation independently of thromboxane A₂ and integrin α2β1. Poly(PHG)-induced tyrosine phosphorylation of glycoprotein VI (GPVI)-related molecules and failed to activate GPVI/FcRγ-deficient platelets. Binding of GPVI to poly(PHG) was confirmed by a surface plasmon resonance spectroscopy, suggesting that poly(PHG) activates platelets through GPVI. Poly(PHG) is an useful research tool to investigate GPVI-mediated signals and a substitute for collagen in platelet functional assays.

Abbreviations: GP, glycoprotein, LAT, linker for activation of T cells, SLP-76, SH2 domain-containing leukocyte protein of 76, PATI, platelet aggregation threshold index, PLCγ2, phospholipase Cγ2, TXA2, thromboxane A2