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The role of ligand-ligand interactions in competition by fibrinogen and fibrin degradation products for fibrinogen binding to human platelets.

Publication ,  Journal Article
Pasqua, JJ; Pizzo, SV
Published in: Biochim Biophys Acta
June 9, 1983

Binding to human platelets of radioiodinated human fibrinogen and fragments X, Y, D, D1 dimer and E was studied to determine the domain of the fibrinogen molecule responsible for binding to the platelet receptor. Although the fragments did not bind, some were able to compete for the binding of fibrinogen to platelets. It was postulated that the fragments bound to fibrinogen and subsequently interfered with its binding to the receptor. Two approaches were developed to test this hypothesis. In the first technique, molecular exclusion on Sephacryl S-200 superfine was utilized to examine the interaction of radiolabeled fragments with fibrinogen. In the second series of studies, fibrinogen-Sepharose was prepared and the binding of degradation products directly determined. A spin dialysis apparatus was employed in each case to achieve rapid separation of bound and free radioligand. These studies demonstrated that fragments D and E bind to fibrinogen. Therefore, the mechanism by which degradation products interfere with fibrinogen binding to the platelet receptor is ligand-ligand interaction rather than binding of the fragments to the receptor. Since none of the radiolabeled degradation products bound to platelets, it appears that receptor recognition requires the intact molecule.

Duke Scholars

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

June 9, 1983

Volume

757

Issue

3

Start / End Page

282 / 287

Location

Netherlands

Related Subject Headings

  • Serum Albumin, Bovine
  • Protein Binding
  • Ligands
  • In Vitro Techniques
  • Humans
  • Fibrinogen
  • Fibrin Fibrinogen Degradation Products
  • Blood Platelets
  • Binding, Competitive
  • Binding Sites
 

Citation

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Pasqua, J. J., & Pizzo, S. V. (1983). The role of ligand-ligand interactions in competition by fibrinogen and fibrin degradation products for fibrinogen binding to human platelets. Biochim Biophys Acta, 757(3), 282–287. https://doi.org/10.1016/0304-4165(83)90052-1
Pasqua, J. J., and S. V. Pizzo. “The role of ligand-ligand interactions in competition by fibrinogen and fibrin degradation products for fibrinogen binding to human platelets.Biochim Biophys Acta 757, no. 3 (June 9, 1983): 282–87. https://doi.org/10.1016/0304-4165(83)90052-1.
Pasqua, J. J., and S. V. Pizzo. “The role of ligand-ligand interactions in competition by fibrinogen and fibrin degradation products for fibrinogen binding to human platelets.Biochim Biophys Acta, vol. 757, no. 3, June 1983, pp. 282–87. Pubmed, doi:10.1016/0304-4165(83)90052-1.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

June 9, 1983

Volume

757

Issue

3

Start / End Page

282 / 287

Location

Netherlands

Related Subject Headings

  • Serum Albumin, Bovine
  • Protein Binding
  • Ligands
  • In Vitro Techniques
  • Humans
  • Fibrinogen
  • Fibrin Fibrinogen Degradation Products
  • Blood Platelets
  • Binding, Competitive
  • Binding Sites