Abstract
The specificity of tetrafibricin was examined by comparing its activities on GPIIb/IIIa and on the vitronectin receptor (alpha v beta 3) with those of Arg-Gly-Asp-Ser (RGDS) on the same receptors. Tetrafibricin, which inhibited fibrinogen-GPIIb/IIIa binding 10 times more potently than RGDS, was three orders of magnitude less potent compared to RGDS on the inhibition of fibrinogen binding to alpha v beta 3. Furthermore, tetrafibricin potently inhibited platelet adhesion to both fibrinogen and von Willebrand factor. Whereas, there was no significant inhibition observed in the GPIIb/IIIa-independent cellular adhesions. These results suggest that tetrafibricin is highly selective for GPIIb/IIIa.
MeSH terms
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Amino Acid Sequence
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Animals
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Anti-Bacterial Agents / pharmacology*
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Aorta
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Blood Platelets / metabolism
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Cattle
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Cells, Cultured
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Endothelium, Vascular / drug effects
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Endothelium, Vascular / physiology*
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Fibrinogen / metabolism
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Glycoproteins / metabolism
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Humans
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Integrins / drug effects*
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Integrins / isolation & purification
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Integrins / metabolism
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Kinetics
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Macrolides*
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Molecular Sequence Data
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Oligopeptides / pharmacology*
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Platelet Adhesiveness / drug effects
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Platelet Adhesiveness / physiology
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Platelet Aggregation Inhibitors / pharmacology*
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Platelet Membrane Glycoproteins / drug effects*
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Platelet Membrane Glycoproteins / isolation & purification
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Platelet Membrane Glycoproteins / metabolism
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Receptors, Cytoadhesin / drug effects*
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Receptors, Cytoadhesin / isolation & purification
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Receptors, Cytoadhesin / metabolism
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Receptors, Vitronectin
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Vitronectin
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von Willebrand Factor / metabolism
Substances
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Anti-Bacterial Agents
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Glycoproteins
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Integrins
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Macrolides
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Oligopeptides
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Platelet Aggregation Inhibitors
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Platelet Membrane Glycoproteins
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Receptors, Cytoadhesin
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Receptors, Vitronectin
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Vitronectin
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von Willebrand Factor
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tetrafibricin
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Fibrinogen
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arginyl-glycyl-aspartyl-serine