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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-11-23
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoadhesin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Vitronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Vitronectin,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartyl-serine,
http://linkedlifedata.com/resource/pubmed/chemical/tetrafibricin,
http://linkedlifedata.com/resource/pubmed/chemical/von Willebrand Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
204
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
325-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7524499-Amino Acid Sequence,
pubmed-meshheading:7524499-Animals,
pubmed-meshheading:7524499-Anti-Bacterial Agents,
pubmed-meshheading:7524499-Aorta,
pubmed-meshheading:7524499-Blood Platelets,
pubmed-meshheading:7524499-Cattle,
pubmed-meshheading:7524499-Cells, Cultured,
pubmed-meshheading:7524499-Endothelium, Vascular,
pubmed-meshheading:7524499-Fibrinogen,
pubmed-meshheading:7524499-Glycoproteins,
pubmed-meshheading:7524499-Humans,
pubmed-meshheading:7524499-Integrins,
pubmed-meshheading:7524499-Kinetics,
pubmed-meshheading:7524499-Macrolides,
pubmed-meshheading:7524499-Molecular Sequence Data,
pubmed-meshheading:7524499-Oligopeptides,
pubmed-meshheading:7524499-Platelet Adhesiveness,
pubmed-meshheading:7524499-Platelet Aggregation Inhibitors,
pubmed-meshheading:7524499-Platelet Membrane Glycoproteins,
pubmed-meshheading:7524499-Receptors, Cytoadhesin,
pubmed-meshheading:7524499-Receptors, Vitronectin,
pubmed-meshheading:7524499-Vitronectin,
pubmed-meshheading:7524499-von Willebrand Factor
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pubmed:year |
1994
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pubmed:articleTitle |
Tetrafibricin has a high selectivity for GPIIb/IIIa: comparison of the effects of tetrafibricin and RGDS on GPIIb/IIIa and the vitronectin receptor.
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pubmed:affiliation |
Nippon Roche Research Center, Kanagawa, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study
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