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The Journal of Immunology, 2006, 176: 52-60.
Copyright © 2006 by The American Association of Immunologists

Integrin {alpha}IIb{beta}3 Induces the Adhesion and Activation of Mast Cells through Interaction with Fibrinogen1

Toshihiko Oki*, Jiro Kitaura*, Koji Eto{dagger}, Yang Lu*, Mari Maeda-Yamamoto{ddagger}, Naoki Inagaki§, Hiroichi Nagai§, Yoshinori Yamanishi*, Hideaki Nakajina*, Hidetoshi Kumagai* and Toshio Kitamura2,*

* Division of Cellular Therapy and Division of Hematopoietic Factors, Advanced Clinical Research Center, and {dagger} Laboratory of Stem Cell Therapy, Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, Tokyo, Japan; {ddagger} National Institute of Vegetable and Tea Science, National Agriculture Research Organization, Shizuoka, Japan; and § Department of Pharmacology, Gifu Pharmaceutical University, Gifu, Japan

Integrin {alpha}IIb, a well-known marker of megakaryocyte-platelet lineage, has been recently recognized on hemopoietic progenitors. We now demonstrate that integrin {alpha}IIb{beta}3 is highly expressed on mouse and human mast cells including mouse bone marrow-derived mast cells, peritoneal mast cells, and human cord blood-derived mast cells, and that its binding to extracellular matrix proteins leads to enhancement of biological functions of mast cells in concert with various stimuli. With exposure to various stimuli, including cross-linking of Fc{epsilon}RI and stem cell factor, mast cells adhered to extracellular matrix proteins such as fibrinogen and von Willebrand factor in an integrin {alpha}IIb{beta}3-dependent manner. In addition, the binding of mast cells to fibrinogen enhanced proliferation, cytokine production, and migration and induced uptake of soluble fibrinogen in response to stem cell factor stimulation, implicating integrin {alpha}IIb{beta}3 in a variety of mast cell functions. In conclusion, mouse and human mast cells express functional integrin {alpha}IIb{beta}3.




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