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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1993-6-29
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pubmed:abstractText |
Cyclic RGD-containing peptides caused a dose-dependent inhibition of binding of human embryonic kidney cells transfected with recombinant GpIIb/IIIa (r293 clone B) to human fibrinogen coated on to non-tissue culture plates. The inhibitory activity, IC50, of a panel of seventeen RGD-containing peptides ranged from 0.12 to 89.2 microM. These IC50 values correlated with those determined by the inhibition of platelet aggregation (r = 0.99). Even though there was a correlation, there were differences between the platelet aggregation and the bioadhesion assay. The binding of r293 clone B to fibrinogen was not increased by ADP suggesting that GpIIb/IIIa expressed on the surface of r293 clone B cells may be in the 'activated' form. Moreover, preincubation of r293 clone B cells with a monoclonal antibody (mAb) specific for GpIIIa (4B12) resulted in a dose-dependent decrease of binding to fibrinogen while a mAb specific for GPIIb (2D2) had no effect. Neither of these mAbs inhibited platelet aggregation. The binding of r293 clone B cells to fibrinogen required Ca2+ or Mg2+. This cell-based bioadhesion method can provide a tool for screening potential GpIIb/IIIa antagonists and investigating the interaction of GpIIb/IIIa and fibrinogen not possible with platelet aggregation.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
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/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0957-5235
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
255-62
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:8499563-Adenosine Diphosphate,
pubmed-meshheading:8499563-Antibodies, Monoclonal,
pubmed-meshheading:8499563-Biological Assay,
pubmed-meshheading:8499563-Calcium,
pubmed-meshheading:8499563-Cell Adhesion,
pubmed-meshheading:8499563-Clone Cells,
pubmed-meshheading:8499563-Edetic Acid,
pubmed-meshheading:8499563-Egtazic Acid,
pubmed-meshheading:8499563-Fibrinogen,
pubmed-meshheading:8499563-Humans,
pubmed-meshheading:8499563-Magnesium,
pubmed-meshheading:8499563-Models, Biological,
pubmed-meshheading:8499563-Oligopeptides,
pubmed-meshheading:8499563-Platelet Aggregation,
pubmed-meshheading:8499563-Platelet Aggregation Inhibitors,
pubmed-meshheading:8499563-Platelet Membrane Glycoproteins,
pubmed-meshheading:8499563-Recombinant Proteins,
pubmed-meshheading:8499563-Transfection
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pubmed:year |
1993
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pubmed:articleTitle |
RGD-containing peptides inhibit adhesion of 293 cells transfected with GpIIb/IIIa to fibrinogen: comparison to inhibition of platelet aggregation.
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pubmed:affiliation |
Department of Medicinal and Analytical Chemistry, Genentech Inc., South San Francisco, CA 94080.
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pubmed:publicationType |
Journal Article
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