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Integrin _IIb3 Induces the Adhesion and Activation of Mast Cells through Interaction with Fibrinogen¹

Toshihiko Oki^*, Jiro Kitaura^*, Koji Eto, Yang Lu^*, Mari Maeda-Yamamoto, Naoki Inagaki, Hiroichi Nagai, Yoshinori Yamanishi^*, Hideaki Nakajina^*, Hidetoshi Kumagai^* and Toshio Kitamura^2,*

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

Integrin _IIb, a well-known marker of megakaryocyte-platelet lineage, has been recently recognized on hemopoietic progenitors. We now demonstrate that integrin _IIb3 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 FcRI and stem cell factor, mast cells adhered to extracellular matrix proteins such as fibrinogen and von Willebrand factor in an integrin _IIb3-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 _IIb3 in a variety of mast cell functions. In conclusion, mouse and human mast cells express functional integrin _IIb3.

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