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
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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
منابع مشابه
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...
متن کاملPlatelet glycoprotein Ib-IX as a regulator of systemic inflammation.
OBJECTIVE The platelet glycoprotein Ib-IX (GP Ib-IX) receptor is a well-characterized adhesion receptor supporting hemostasis and thrombosis via interactions with von Willebrand factor. We examine the GP Ib-IX/von Willebrand factor axis in murine polymicrobial sepsis, as modeled by cecal ligation and puncture (CLP). APPROACH AND RESULTS Genetic absence of the GP Ib-IX ligand, von Willebrand f...
متن کاملHEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Ristocetin-dependent, but not botrocetin-dependent, binding of von Willebrand factor to the platelet glycoprotein Ib-IX-V complex correlates with shear-dependent interactions
Under conditions of high shear stress, both hemostasis and thrombosis are initiated by the interaction of the platelet membrane glycoprotein (GP) Ib-IX-V complex with its adhesive ligand, von Willebrand factor (vWF), in the subendothelial matrix or plasma. This interaction involves the A1 domain of vWF and the N-terminal extracellular region of GP Iba (His-1-Glu-282), and it can also be induced...
متن کاملHEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Requirement of leucine-rich repeats of glycoprotein (GP) Iba for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib–IX-V complex
The platelet glycoprotein (GP) Ib–IX-V complex mediates adhesion to von Willebrand factor (vWf) in (patho)physiologic thrombus formation. The vWf-binding site on GP Ib–IX-V is within the N-terminal 282 residues of GP Iba, which consist of an N-terminal flanking sequence (His-1– Ile-35), 7 leucine-rich repeats (Leu-36–Ala200), a C-terminal flank (Phe-201–Gly268), and a sulfated tyrosine sequence...
متن کاملHEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The 1 helix– 13 strand spanning Leu214 to Val229 of platelet glycoprotein Ib facilitates the interaction with von Willebrand factor: evidence from characterization of the epitope of monoclonal antibody AP1
The glycoprotein Ib-IX-V (GP Ib-IX-V) complex mediates platelet binding to von Willebrand factor (VWF) through its largest polypeptide, GP Ib . Of the many GP Ib monoclonal antibodies described, AP1 is of particular interest because it blocks static VWF binding induced by 2 modulators, ristocetin and botrocetin, and platelet adhesion to VWF surfaces under flow. We mapped the AP1 binding site to...
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تاریخ انتشار 2008