PLATELETS HAVE MORE THAN ONE BINDING-SITE FOR VONWILLEBRAND-FACTOR
PLATELETS HAVE MORE THAN ONE BINDING-SITE FOR VONWILLEBRAND-FACTOR
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DOI:
10.1172/jci110946
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发表时间:
1983-01-01
影响因子:
15.9
通讯作者:
MONTGOMERY, RR
中科院分区:
文献类型:
--
作者:
RUGGERI, ZM;DEMARCO, L;MONTGOMERY, RR
The binding of 125I-von Willebrand factor (125I-vWF) to platelets stimulated by thrombin, ADP and a combination of ADP + epinephrine (EPI) is specific, saturable and reversible. Active platelet metabolism and divalent cations are required for binding induced by these stimuli, but not by ristocetin, suggesting the existence of different mechanisms involved in the vWF-platelet interaction. A monoclonal antibody directed against an epitope of membrane glycoprotein (GP) Ib had no effect on the binding of 125I-vWF to normal platelets stimulated by thrombin or a combination of ADP + EPI, but completely blocked ristocetin-induced binding. Binding induced by thrombin to GPIb-blocked platelets was specific. Thrombin-induced binding of 125I-vWF was increased, rather than decreased, in 2 patients with the Bernard-Soulier syndrome whose platelets lacked GPIb. Monoclonal antibodies directed against the GPIIb/IIIa complex had no effect on ristocetin-induced binding of 125I-vWF to normal platelets, but blocked thrombin- and ADP + EPI-induced binding. To exclude effects mediated by the platelet Fc receptor, a monoclonal IgG directed against an epitope present on human B cells and monocytes, but not expressed on resting or stimulated platelets, was used. It did not affect 125I-vWF binding induced by any of the stimuli. Platelets have > 1 binding site for vWF, and they may be exposed by different stimuli.