A functional 14-3-3 –independent association of PI3-kinase with glycoprotein Ib , the major ligand-binding subunit of the platelet glycoprotein Ib-IX-V complex

نویسندگان

  • Fi-Tjen Mu
  • Robert K. Andrews
  • Jane F. Arthur
  • Adam D. Munday
  • Susan L. Cranmer
  • Shaun P. Jackson
  • Frank C. Stomski
  • Angel F. Lopez
  • Michael C. Berndt
چکیده

1Department of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Australia; 2Puget Sound Blood Center and Division of Hematology, University of Washington, Seattle; 3Australian Centre for Blood Diseases, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Australia; and 4Department of Human Immunology, Institute of Medical and Veterinary Science, Hanson Institute, Adelaide, Australia

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منابع مشابه

HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY A functional 14-3-3 –independent association of PI3-kinase with glycoprotein Ib , the major ligand-binding subunit of the platelet glycoprotein Ib-IX-V complex

1Department of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Australia; 2Puget Sound Blood Center and Division of Hematology, University of Washington, Seattle; 3Australian Centre for Blood Diseases, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Australia; and 4Department of Human Immunology, Institute of Medical and Ve...

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A functional 14-3-3ζ-independent association of PI3-kinase with glycoprotein Ibα, the major ligand-binding subunit of the platelet glycoprotein Ib-IX-V complex Running Title: The interaction of PI3-kinase and GPIbα Scientific Category: Hemostasis, Thrombosis, and Vascular Biology

From the Department of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Victoria, Australia; Puget Sound Blood Center and Division of Hematology, University of Washington, Seattle; Australian Centre for Blood Diseases, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Victoria Australia; Department of Human Immunology, Institu...

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Molecular characterization of quinine/quinidine drug-dependent antibody platelet interaction using monoclonal antibodies.

Two murine monoclonal antibodies, FMC 25 and AN 51, directed against distinct epitopes on the glycoprotein Ib complex, have been used to further define the mechanism of quinine/quinidine drug-dependent antibody interaction with platelets. FMC 25, directed against an epitope on glycoprotein IX, had no effect on platelet aggregation induced by collagen or adenosine diphosphate and little, if any,...

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Localization of the Adhesion Receptor Glycoprotein Ib-IX-V Complex to Lipid Rafts Is Required for Platelet Adhesion and Activation

The platelet glycoprotein (GP) Ib-IX-V complex mediates the attachment of platelets to the blood vessel wall by binding von Willebrand factor (VWF), an interaction that also transmits signals for platelet activation and aggregation. Because the complex is extensively palmitoylated, a modification known to target proteins to lipid rafts, we investigated the role of raft localization in GP Ib-IX-...

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Aggregation of mammalian cells expressing the platelet glycoprotein (GP) Ib-IX complex and the requirement for tyrosine sulfation of GP Ib alpha.

The glycoprotein (GP) Ib-IX complex mediates platelet aggregation in response to high shear forces by binding von Willebrand factor (vWF) in the plasma. We investigated the possibility that the complex could mediate a similar phenomenon if expressed in nonhematopoietic cells. When agitated on a tabletop shaker, CHO and L cells expressing the full complex formed large aggregates in the presence ...

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تاریخ انتشار 2008