Tetrafibricin Has a High Selectivity for GPIIb/IIIa: Comparison of the Effects of Tetrafibricin and RGDS on GPIIb/IIIa and the Vitronectin Receptor

The specificity of tetrafibricin was examined by comparing its activities on GPIIb/IIIa and on the vitronectin receptor (αvβ3) 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 o...

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Veröffentlicht in:	Biochemical and biophysical research communications 1994-10, Vol.204 (1), p.325-332
Hauptverfasser:	Satoh, T., Kouns, W.C., Yamashita, Y., Kamiyama, T., Steiner, B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Anti-Bacterial Agents - pharmacology Aorta Blood Platelets - metabolism Cattle Cells, Cultured Endothelium, Vascular - drug effects Endothelium, Vascular - physiology Fibrinogen - metabolism Glycoproteins - metabolism Humans Integrins - drug effects Integrins - isolation & purification Integrins - metabolism Kinetics Macrolides Molecular Sequence Data Oligopeptides - pharmacology Platelet Adhesiveness - drug effects Platelet Adhesiveness - physiology Platelet Aggregation Inhibitors - pharmacology Platelet Membrane Glycoproteins - drug effects Platelet Membrane Glycoproteins - isolation & purification Platelet Membrane Glycoproteins - metabolism Receptors, Cytoadhesin - drug effects Receptors, Cytoadhesin - isolation & purification Receptors, Cytoadhesin - metabolism Receptors, Vitronectin Vitronectin von Willebrand Factor - metabolism
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Zusammenfassung:	The specificity of tetrafibricin was examined by comparing its activities on GPIIb/IIIa and on the vitronectin receptor (αvβ3) 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 αvβ3. 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.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1994.2463