Binding of radioiodinated human von Willebrand factor to Bernard-Soulier, thrombasthenic and von Willebrand's disease platelets

Moake, Joel L.; Olson, John D.; Troll, Joseph H.; Tang, S. S.; Funicella, Toni; Peterson, Dolores M.

doi:10.1016/0049-3848(80)90400-4

Cited by 97 publications

(31 citation statements)

References 8 publications

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“…On the other hand, in Glanzmann thrombasthenia, another congenital platelet abnormality, there is a marked decrease of the membrane GP complex Ilb/Illa but normal content of GPIb (9). The ristocetin-induced binding of vWF to thrombasthenic platelets has been reported to be normal (8). In contrast, we have recently shown that binding of vWF to thrombasthenic platelets stimulated by thrombin is severely deficient (4).…”

Section: Introductionmentioning

confidence: 89%

“…Platelet membrane glycoprotein (GP) lb is considered to function as the surface receptor for vWF (6). In the Bernard-Soulier syndrome, a congenital bleeding disorder, platelets lack GPIb (7) and the ristocetin-induced binding of vWF is decreased (8). On the other hand, in Glanzmann thrombasthenia, another congenital platelet abnormality, there is a marked decrease of the membrane GP complex Ilb/Illa but normal content of GPIb (9).…”

Section: Introductionmentioning

confidence: 96%

See 1 more Smart Citation

Platelets have more than one binding site for von Willebrand factor.

Ruggeri¹,

Marco²,

Gatti³

et al. 1983

J. Clin. Invest.

443

190

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A B ST R A CT The binding of '251-von Willebrand factor 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) lb had no effect on the binding of '251-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. Moreover, thrombin-induced binding of 1251-vWF was increased, rather than decreased, in two patients with the Bernard-Soulier syndrome whose platelets lacked GPIb. Conversely, monoclonal antibodies directed against the GPIIb/IIIa complex had no effect on ristocetininduced binding of (vWF)' is a large multimeric glycoprotein that circulates in blood complexed with the Factor VIII procoagulant activity protein (1). It plays an essential role in platelet function as shown by the prolonged bleeding time in von Willebrand disease (1). Specific binding sites for vWF are induced on the platelet membrane by the antibiotic ristocetin (2), a nonphysiologic agent, as well as by thrombin (3, 4) and ADP (5). Platelet membrane glycoprotein (GP) lb is considered to function as the surface receptor for vWF (6). In the Bernard-Soulier syndrome, a congenital bleeding disorder, platelets lack GPIb (7) and the ristocetin-induced binding of vWF is decreased (8). On the other hand, in Glanzmann thrombasthenia, another congenital platelet abnormality, there is a marked decrease of the membrane GP complex Ilb/Illa but normal content of GPIb (9). The ristocetin-induced binding of vWF to thrombasthenic platelets has been reported to be normal (8). In contrast, we have recently shown that binding of vWF to thrombasthenic platelets stimulated by thrombin is severely deficient (4). Therefore, we postulated that different sites are involved in ' Abbreviations used Marguerie et al. (12). The final platelet suspensions were all in modified calcium-free Tyrode buffer, containing 137 mM NaCI, 2 mM MgCI2, 0.42 mM NaH2PO4, 11.9 mM NaHCO3, 2.9 mM KCI, 5.5 mM glucose, 10 mM Hepes, pH 7.35, and 20 mg/ml bovine serum albumin (Fraction V, CalbiochemBehring Corp., American Hoechst Corp., San Diego, CA). When experiments of serotonin release were performed, PRP was labeled before washing by incubating 20 ml with 0. (3.3,M). However, ADG-washed platelets usually gave reversible aggregation to ADP and were unresponsive to epinephrine (EPI). On the contrary, gel-filtered platelets always gave irreversible aggregation to ADP, and responded to 20 MM EPI in the presence of fibrinogen (3.3 ,M) with a typical two-wave aggregation. Contamination of plasma vWF in all washed platelet preparations was below 5 X 10' U/dl (1 dl of a normal plasma pool contains ...

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Section: Introductionmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 96%

Platelets have more than one binding site for von Willebrand factor.

Ruggeri¹,

Marco²,

Gatti³

et al. 1983

J. Clin. Invest.

443

190

View full text Add to dashboard Cite

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“…Although vWF is multifunctional and binds to platelet GpIb (5,6,25,26), GpIIb-IIIa (30)(31)(32), components of the subendothelium such as collagen (7)(8)(9)16) and Factor VIII:C (28,33), the domain on native vWF polymer that binds to each of these receptors or proteins has not been localized. One our studies indicate (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Abbreviations used in this paper: GpIb, glycoprotein Ib vessel wall (1)(2)(3). Although the mechanism by which vWF promotes adhesion has not been fully delineated, there is evidence that vWF links platelets to the vessel wall by binding to platelet glycoprotein Ib (GpIb), as well as to exposed subendothelial collagen (4)(5)(6)(7)(8)(9). In previous studies, we, and others, have demonstrated vWF binding to GpIb and competition for binding by a soluble proteolytic fragment of GpIb, glycocalicin (10, 1 1).…”

Section: Introductionmentioning

confidence: 99%

Structural basis of von Willebrand factor binding to platelet glycoprotein Ib and collagen. Effects of disulfide reduction and limited proteolysis of polymeric von Willebrand factor.

1986

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“…Of the platelet surface membrane proteins, GPIb at 26,000±10,000 copies per platelet (10) and glycoprotein IIb/IIIa (GPIIb/IIIa) at 40,000-50,000 copies per platelet (1 1, 12) are potential candidates for plasminogen binding sites on resting platelets. Since agonists alter the function of both of these membrane proteins as evidenced by ristocetin-supported binding of von Willebrand Factor to GPIb (10,13) and the role of GPIIb/IIIa in thrombinstimulated binding of fibrinogen (12,(14)(15)(16), fibronectin (17), and von Willebrand Factor (18), their alteration may also contribute to the increase in plasminogen binding to stimulated platelets. Thrombin stimulation also results in the expression of new species on the surface ofactivated platelets.…”

Section: Introductionmentioning

confidence: 99%

Plasminogen interacts with human platelets through two distinct mechanisms.

Miles¹,

Ginsberg²,

White³

et al. 1986

J. Clin. Invest.

125

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Glu-plasminogen, the native form of plasminogen, interacts in a specific and saturable manner with unstimulated human platelets, and the binding is enhanced fivefold by thrombin stimulation (Miles and Plow, 1985. J. Biol. Chem. 260:4303). This study characterizes the nature of the Glu-plasminogen binding sites by analyzing platelets deficient in selected proteins and functions. Platelets from patients with afibrinogenemia, Gray platelet syndrome, and the Cam Variant of thrombasthenia, a form of thrombasthenia with near normal levels of glycoprotein HIb/IIIa (GPIIb/IIIa), showed minimal augmentation of plasminogen binding to thrombin-stimulated platelets but normal binding to unstimulated platelets. This selective deficiency indicates that two distinct mechanisms are involved in the interaction of plasminogen with platelets. These abnormal platelets share a deficiency in fibrinogen. Surface expression of platelet fibrinogen, however, was not sufficient for enhanced plasminogen binding to stimulated platelets, and experiments with alpha-thrombin and gamma-thrombin indicated that fibrin formation on the platelet surface is necessary for the augmented plasminogen binding. Unstimulated and stimulated thrombasthenic platelets deficient in GPIIb/IIIa bound markedly reduced levels of plasminogen, which suggests a role for GPIIb/IIIa in plasminogen binding to unstimulated platelets. Treatment of platelets to dissociate the heterodimeric complex of GPIIb/IIIa did not significantly perturb plasminogen binding to unstimulated platelets, but the complex may be necessary for thrombin-stimulated plasminogen binding via its interaction with platelet fibrin.

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Binding of radioiodinated human von Willebrand factor to Bernard-Soulier, thrombasthenic and von Willebrand's disease platelets

Cited by 97 publications

References 8 publications

Platelets have more than one binding site for von Willebrand factor.

Platelets have more than one binding site for von Willebrand factor.

Structural basis of von Willebrand factor binding to platelet glycoprotein Ib and collagen. Effects of disulfide reduction and limited proteolysis of polymeric von Willebrand factor.

Plasminogen interacts with human platelets through two distinct mechanisms.

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