The role of ADP secretion and thromboxane synthesis in factor VIII binding to platelets

G. Di Minno, S. S. Shapiro, P. M. Catalano, L. De Marco, S. Murphy

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Following stimulation with arachidonic acid, collagen, U-46619 (a stable analogue of prostaglandin endoperoxide/thromboxane-A2), thrombin, or adenosine diphosphate (ADP), unstirred human platelet suspensions bound labeled factor VIII in a reaction that reached equilibrium within 10 min. Apyrase inhibited binding induced by arachidonic acid, collagen, U-46619, and thrombin by less than 40%, but inhibited ADP-induced binding by 95%. Binding to aspirin-treated platelets was normal in response to U-46619, reduced by 60%-70% in response to ADP, collagen, and thrombin, and absent in response to arachidonic acid. Binding in response to U-46619 was not altered by the combination of apyrase and aspirin. Binding of factor VIII was decreased by 90% when 10 mM EDTA was added before each agonist, but is was inhibited less than 30% when EDTA was added following platelet stimulation. We conclude that arachidonic acid, collagen, and thrombin can expose binding sites for factor VIII independently of released ADP; that Ca++ is required for activation but probably not for binding of factor VIII to platelets; and that platelet thromboxane synthesis plays a major role in the binding of factor VIII to platelets induced by thrombin, ADP, or collagen.

Original languageEnglish
Pages (from-to)186-190
Number of pages5
JournalBlood
Volume62
Issue number1
Publication statusPublished - 1983

Fingerprint

Thromboxanes
Factor VIII
Platelets
Adenosine Diphosphate
15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid
Thrombin
Blood Platelets
Collagen
Arachidonic Acid
Apyrase
Edetic Acid
Aspirin
Synthetic Prostaglandin Endoperoxides
Thromboxane A2
Suspensions
Chemical activation
Binding Sites

ASJC Scopus subject areas

  • Hematology

Cite this

Di Minno, G., Shapiro, S. S., Catalano, P. M., De Marco, L., & Murphy, S. (1983). The role of ADP secretion and thromboxane synthesis in factor VIII binding to platelets. Blood, 62(1), 186-190.

The role of ADP secretion and thromboxane synthesis in factor VIII binding to platelets. / Di Minno, G.; Shapiro, S. S.; Catalano, P. M.; De Marco, L.; Murphy, S.

In: Blood, Vol. 62, No. 1, 1983, p. 186-190.

Research output: Contribution to journalArticle

Di Minno, G, Shapiro, SS, Catalano, PM, De Marco, L & Murphy, S 1983, 'The role of ADP secretion and thromboxane synthesis in factor VIII binding to platelets', Blood, vol. 62, no. 1, pp. 186-190.
Di Minno G, Shapiro SS, Catalano PM, De Marco L, Murphy S. The role of ADP secretion and thromboxane synthesis in factor VIII binding to platelets. Blood. 1983;62(1):186-190.
Di Minno, G. ; Shapiro, S. S. ; Catalano, P. M. ; De Marco, L. ; Murphy, S. / The role of ADP secretion and thromboxane synthesis in factor VIII binding to platelets. In: Blood. 1983 ; Vol. 62, No. 1. pp. 186-190.
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AB - Following stimulation with arachidonic acid, collagen, U-46619 (a stable analogue of prostaglandin endoperoxide/thromboxane-A2), thrombin, or adenosine diphosphate (ADP), unstirred human platelet suspensions bound labeled factor VIII in a reaction that reached equilibrium within 10 min. Apyrase inhibited binding induced by arachidonic acid, collagen, U-46619, and thrombin by less than 40%, but inhibited ADP-induced binding by 95%. Binding to aspirin-treated platelets was normal in response to U-46619, reduced by 60%-70% in response to ADP, collagen, and thrombin, and absent in response to arachidonic acid. Binding in response to U-46619 was not altered by the combination of apyrase and aspirin. Binding of factor VIII was decreased by 90% when 10 mM EDTA was added before each agonist, but is was inhibited less than 30% when EDTA was added following platelet stimulation. We conclude that arachidonic acid, collagen, and thrombin can expose binding sites for factor VIII independently of released ADP; that Ca++ is required for activation but probably not for binding of factor VIII to platelets; and that platelet thromboxane synthesis plays a major role in the binding of factor VIII to platelets induced by thrombin, ADP, or collagen.

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