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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1994-3-4
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pubmed:abstractText |
Tetrafibricin is a novel nonpeptidic fibrinogen receptor inhibitor isolated from Streptomyces neyagawaensis NR0577. Its competitive and selective fibrinogen receptor blockage was demonstrated in this study. Tetrafibricin competitively inhibited (Ki = 9.9 nM) the binding of biotinylated fibrinogen to purified active glycoprotein (GP) IIb/IIIa immobilized on plastic plate. When RGDS and tetrafibricin were added in combination, the inhibition was additive. The binding of other RGD-containing proteins, fibronectin and von Willebrand factor, to active GPIIb/IIIa were also completely inhibited by tetrafibricin. The fact that tetrafibricin did not inhibit the binding of von Willebrand factor to GPIb/IX indicates the specific blockage of tetrafibricin for GPIIb/IIIa. Fibrinogen receptor inhibition of tetrafibricin was also confirmed by its ability to inhibit 125I-fibrinogen binding to platelets stimulated with ADP. Because of its competitiveness and specificity, tetrafibricin can be used in a new structural model for the design of fibrinogen receptor inhibitors.
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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/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartic acid,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartyl-serine,
http://linkedlifedata.com/resource/pubmed/chemical/fibrinopeptides gamma,
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 |
Dec
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pubmed:issn |
0049-3848
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
389-400
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8303682-Adenosine Diphosphate,
pubmed-meshheading:8303682-Amino Acid Sequence,
pubmed-meshheading:8303682-Anti-Bacterial Agents,
pubmed-meshheading:8303682-Binding, Competitive,
pubmed-meshheading:8303682-Blood Platelets,
pubmed-meshheading:8303682-Fibrinogen,
pubmed-meshheading:8303682-Humans,
pubmed-meshheading:8303682-Macrolides,
pubmed-meshheading:8303682-Molecular Sequence Data,
pubmed-meshheading:8303682-Oligopeptides,
pubmed-meshheading:8303682-Platelet Membrane Glycoproteins,
pubmed-meshheading:8303682-Streptomyces,
pubmed-meshheading:8303682-von Willebrand Factor
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pubmed:year |
1993
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pubmed:articleTitle |
Tetrafibricin: a nonpeptidic fibrinogen receptor inhibitor from Streptomyces neyagawaensis (I). Its GPIIb/IIIa blockage on solid phase binding assay.
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pubmed:affiliation |
Nippon Roche Research Center, Kanagawa, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro
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