Phospholipase Cgamma2 contributes to stable thrombus formation on VWF.
Though phospholipase C PLCgamma2 is known to play an important role in platelet activation by collagen and fibrinogen, its importance in GPIb-mediated platelet activation is less well understood. To better understand the role of PLCgamma2 in GPIb-mediated adhesion and thrombus formation, we examined the ability of wild-type and PLCgamma2- deficient murine platelets to spread on immobilized von Willebrand factor (VWF) under static conditions, and to attach to and form thrombi on VWF under conditions of arterial shear. While absence of PLCgamma2 had only a minimal effect on platelet adhesion to immobilized VWF, its absence impaired spreading and profoundly affected thrombus growth and stability on VWF.
Blood Research Institute The Blood Center of Southeastern Wisconsin, P.O. Box 2178, 638 N. 18th St., Milwaukee, WI 53201, USA.
Vipul
V
Rathore
Demin
D
Wang
Debra K
DK
Newman
Peter J
PJ
Newman
D000818:Animals; D001792:Blood Platelets / Q000201:enzymology / Q000502:physiology*; D017353:Gene Deletion; D018056:Hemorheology; D051379:Mice; D051966:Phospholipase C gamma; D010973:Platelet Adhesiveness; D013927:Thrombosis / Q000201:enzymology / Q000378:metabolism*; D010738:Type C Phospholipases / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D014841:von Willebrand Factor / Q000378:metabolism*
D014841:von Willebrand Factor; D010738:Type C Phospholipases; D051966:Phospholipase C gamma