The von Willebrand Factor-Glycoprotein Ib/V/IX Interaction Induces Actin Polymerization and Cytoskeletal Reorganization in Rolling Platelets and Glycoprotein Ib/V/IX-transfected Cells Export

@article{citeulike:5105095, abstract = {Platelet adhesion to sites of vascular injury is initiated by the binding of the platelet glycoprotein (GP) Ib-V-IX complex to matrix-bound von Willebrand factor (vWf). This receptor-ligand interaction is characterized by a rapid on-off rate that enables efficient platelet tethering and rolling under conditions of rapid blood flow. We demonstrate here that platelets adhering to immobilized vWf under flow conditions undergo rapid morphological conversion from flat discs to spiny spheres during surface translocation. Studies of Glanzmann thrombasthenic platelets (lacking integrin [alpha]IIb[beta]3) and Chinese hamster ovary (CHO) cells transfected with GPIb/IX (CHO-Ib/IX) confirmed that vWf binding to GPIb/IX was sufficient to induce actin polymerization and cytoskeletal reorganization independent of integrin [alpha]IIb[beta]3. vWf-induced cytoskeletal reorganization occurred independently of several well characterized signaling processes linked to platelet activation, including calcium influx, prostaglandin metabolism, protein tyrosine phosphorylation, activation of protein kinase C or phosphatidylinositol 3-kinase but was critically dependent on the mobilization of intracellular calcium. Studies of Oregon Green 488 1,2-bis(o-amino-5-fluorophenoxy)ethane-N,N,N',N-tetraacetic acid tetraacetoxymethyl ester-loaded platelets and CHO-Ib/IX cells demonstrated that these cells mobilize intracellular calcium in a shear-dependent manner during surface translocation on vWf. Taken together, these studies suggest that the vWf-GPIb interaction stimulates actin polymerization and cytoskeletal reorganization in rolling platelets via a shear-sensitive signaling pathway linked to intracellular calcium mobilization. 10.1074/jbc.274.51.36241}, author = {Yuan, Yuping and Kulkarni, Suhasini and Ulsemer, Philippe and Cranmer, Susan L. and Yap, Cindy L. and Nesbitt, Warwick S. and Harper, Ian and Mistry, Nayna and Dopheide, Sacha M. and Hughan, Sascha C. and Williamson, David and de La Salle, Corinne and Salem, Hatem H. and Lanza, Francois and Jackson, Shaun P.}, citeulike-article-id = {5105095}, citeulike-linkout-0 = {http://dx.doi.org/10.1074/jbc.274.51.36241}, citeulike-linkout-1 = {http://www.jbc.org/cgi/content/abstract/274/51/36241}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/10593912}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=10593912}, day = {17}, doi = {10.1074/jbc.274.51.36241}, journal = {J. Biol. Chem.}, keywords = {adhesion, glycoprotein, glycoproteins, gpib, platelet, platelets, vwf}, month = {December}, number = {51}, pages = {36241--36251}, posted-at = {2009-07-10 12:22:29}, priority = {2}, title = {The von Willebrand Factor-Glycoprotein Ib/V/IX Interaction Induces Actin Polymerization and Cytoskeletal Reorganization in Rolling Platelets and Glycoprotein Ib/V/IX-transfected Cells}, url = {http://dx.doi.org/10.1074/jbc.274.51.36241}, volume = {274}, year = {1999} }

TY - JOUR ID - citeulike:5105095 L3 - citeulike-article-id:5105095 N2 - Platelet adhesion to sites of vascular injury is initiated by the binding of the platelet glycoprotein (GP) Ib-V-IX complex to matrix-bound von Willebrand factor (vWf). This receptor-ligand interaction is characterized by a rapid on-off rate that enables efficient platelet tethering and rolling under conditions of rapid blood flow. We demonstrate here that platelets adhering to immobilized vWf under flow conditions undergo rapid morphological conversion from flat discs to spiny spheres during surface translocation. Studies of Glanzmann thrombasthenic platelets (lacking integrin [alpha]IIb[beta]3) and Chinese hamster ovary (CHO) cells transfected with GPIb/IX (CHO-Ib/IX) confirmed that vWf binding to GPIb/IX was sufficient to induce actin polymerization and cytoskeletal reorganization independent of integrin [alpha]IIb[beta]3. vWf-induced cytoskeletal reorganization occurred independently of several well characterized signaling processes linked to platelet activation, including calcium influx, prostaglandin metabolism, protein tyrosine phosphorylation, activation of protein kinase C or phosphatidylinositol 3-kinase but was critically dependent on the mobilization of intracellular calcium. Studies of Oregon Green 488 1,2-bis(o-amino-5-fluorophenoxy)ethane-N,N,N',N-tetraacetic acid tetraacetoxymethyl ester-loaded platelets and CHO-Ib/IX cells demonstrated that these cells mobilize intracellular calcium in a shear-dependent manner during surface translocation on vWf. Taken together, these studies suggest that the vWf-GPIb interaction stimulates actin polymerization and cytoskeletal reorganization in rolling platelets via a shear-sensitive signaling pathway linked to intracellular calcium mobilization. 10.1074/jbc.274.51.36241 IS - 51 JF - J. Biol. Chem. EP - 36251 TI - The von Willebrand Factor-Glycoprotein Ib/V/IX Interaction Induces Actin Polymerization and Cytoskeletal Reorganization in Rolling Platelets and Glycoprotein Ib/V/IX-transfected Cells VL - 274 SP - 36241 KW - adhesion KW - glycoprotein KW - glycoproteins KW - gpib KW - platelet KW - platelets KW - vwf AU - Yuan, Yuping AU - Kulkarni, Suhasini AU - Ulsemer, Philippe AU - Cranmer, Susan AU - Yap, Cindy AU - Nesbitt, Warwick AU - Harper, Ian AU - Mistry, Nayna AU - Dopheide, Sacha AU - Hughan, Sascha AU - Williamson, David AU - de La Salle, Corinne AU - Salem, Hatem AU - Lanza, Francois AU - Jackson, Shaun PY - 1999/12/17/ UR - http://dx.doi.org/10.1074/jbc.274.51.36241 ER -