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Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor

Article Abstract:

Hemodynamic properties governing platelet adhesion to immobilized fibrinogen and von Willebrand factor (vWf) show that the two substrates rely on the action of glycoproteins (GP) to promote cell adhesion in thrombogenesis. Fibrinogen uses the binding to GP IIb-IIIa receptor, also known as integrin alpha(sub IIb) beta(sub 3), while vWf interacts with GP Ib alpha as well as with integrin. Integrin attracts cells at low shear stress while GP Ib is able to attract cells at high shear stress. The action of GP Ib allows integrin to bind platelets to vWf under conditions that do not permit binding to fibrinogen.

Author: Ruggeri, Zaverio M., Savage, Brian, Saldivar, Enrique
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Cell aggregation, Blood clotting, Blood coagulation, Fibrinogen

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Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow

Article Abstract:

A study was conducted on two biologically relevant substrates to determine the adhesion pathways involved in the platelet thrombus formation. The type I collagen fibrils and subendothelial matrix were examined in real time using confocal videomicroscopy. Results showed the initial glycoprotein Ibalpha-mediated function of von Willerbrand factor causes irreversible platelet adhesion and aggregation, indicating that hemodynamic forces and substrate characteristics determine platelet adhesion routes leading to thrombogenesis.

Author: Ruggeri, Zaverio M., Savage, Brian, Amus-Jacobs, Fanny
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Blood flow, Thrombosis, Blood clot, Platelet-derived growth factor receptors

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Mvwf, a dominant modifier of murine von Willebrand factor, results from altered lineage-specific expression of a glycosyltransferase

Article Abstract:

A study was conducted to analyze altered lineage-specific expression of an N-acetylgalactosaminyltarnsferase gene, Galgt2, as the gain-of-function mechanism influencing the action of a major modifier of plasma von Willebrand factor level in RIIIS/J mice. Experimental results indicated that the posttranslational modification of von Willebran factor by the gene correlates with clearance increases from plasma.

Author: Lowe, John B., Ginsburg, David, Smith, Peter L., Mohlke, Karen L., Purkayastha, Anjali A., Westrick, Randal J., Petryniak, Bronia
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
Mice, Mice (Rodents)

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Subjects list: Research, Blood platelets, Von Willebrand factor
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