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Glycoprotein IIb-IIIa-liposomes bind fibrinogen but do not undergo fibrinogen-mediated aggregation

Platelet aggregation is mediated primarily by the binding of fibrinogen to its membrane receptor, GPIIb-IIIa, but such an interaction may not be sufficient to support aggregation. This question could potentially be resolved by reconstituting GPIIb-IIIa into a model membrane system. / A protocol was developed for the generation of liposomes containing purified GPIIb-IIIa. Flow cytometric techniques confirmed that the receptor was present in the lipid bilayer and were used to evaluate the characteristics of fibrinogen binding to the liposomes, which like fibrinogen-platelet interactions exhibited specificity, saturability, time-dependence, and calcium-dependence. / No fibrinogen-specific aggregation of GPIIb-IIIa-liposomes with stir or shear was observed, as determined by flow cytometric cell counting and microscopic examination of particles. In contrast, platelets rapidly formed large aggregates in the presence of fibrinogen. It thus appears that elements other than fibrinogen and GPIIb-IIIa play an important role in platelet aggregation.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.20865
Date January 1997
CreatorsSloan, Stephen Michael.
ContributorsFrojmovic, Mary M. (advisor)
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageMaster of Science (Department of Physiology.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 001604651, proquestno: MQ44281, Theses scanned by UMI/ProQuest.

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