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Integrin alphaIIbbeta3 induces the adhesion and activation of mast cells through interaction with fibrinogen

Toshihiko Oki1, Jiro Kitaura, Koji Eto

  • 1Division of Cellular Therapy and Division of Hematopoietic Factors, Advanced Clinical Research Center, University of Tokyo, Japan.

Journal of Immunology (Baltimore, Md. : 1950)
|December 21, 2005
PubMed

Integrin alphaIIb, a well-known marker of megakaryocyte-platelet lineage, has been recently recognized on hemopoietic progenitors. We now demonstrate that integrin alphaIIbbeta3 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 FcepsilonRI and stem cell factor, mast cells adhered to extracellular matrix proteins such as fibrinogen and von Willebrand factor in an integrin alphaIIbbeta3-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 alphaIIbbeta3 in a variety of mast cell functions. In conclusion, mouse and human mast cells express functional integrin alphaIIbbeta3.

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