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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1990-3-1
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pubmed:abstractText |
In order to analyze the interaction of platelets with von Willebrand factor (vWF) and collagen, we studied the binding of glycocalicin (GC) and formalin-fixed platelets to vWF adsorbed onto uncoated or collagen-coated polystyrene surfaces. These studies show that three-fold more vWF binds to collagen-coated polystyrene than to polystyrene coated with fibrin monomer or fibrinogen. At saturation, 37 +/- 2.9 ng vWF bound to the collagen-coated wells, compared to 12.8 +/- 5.4 ng, and 10.9 +/- 2.7 ng of vWF bound to wells coated with fibrin monomer and fibrinogen, respectively. GC also bound significantly more to collagen-coated wells than to wells coated with fibrinogen, and this binding was increased approximately two-fold (from 7 +/- 0.65 ng to 14 +/- 1.1 ng) in the presence of vWF adsorbed to the collagen-coated surface. Only 2 ng of GC was bound to 3000 ng of vWF when the latter was adsorbed directly onto a polystyrene surface. In contrast, GC binding to vWF adsorbed onto a collagen-coated surface was enhanced 600-fold with 7.0 ng of GC bound to 18 ng of immobilized vWF. Formalin-fixed platelets showed little binding to vWF adsorbed onto the microtiter wells. At saturation, 7 x 10(4) platelets bound to 3000 ng of vWF; a 6-fold increase in platelet binding was observed using collagen-coated wells and this binding was increased even further in the presence of vWF, resulting in 250-fold increase in platelet binding to vWF when the latter was adsorbed onto a collagen surface. These studies suggest that (1) GC is involved in platelet binding to collagen and this binding is increased by vWF; (2) GC binding to vWF is enhanced by the collagen-coated surface; (3) the adsorption of vWF onto a collagen surface may induce conformational changes in vWF that promote its interaction with GC or glycoprotein Ib.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrin,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Fixatives,
http://linkedlifedata.com/resource/pubmed/chemical/Formaldehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIb-IX...,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Polystyrenes,
http://linkedlifedata.com/resource/pubmed/chemical/glycocalicin,
http://linkedlifedata.com/resource/pubmed/chemical/von Willebrand Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0049-3848
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
347-57
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2617474-Adsorption,
pubmed-meshheading:2617474-Blood Platelets,
pubmed-meshheading:2617474-Collagen,
pubmed-meshheading:2617474-Fibrin,
pubmed-meshheading:2617474-Fibrinogen,
pubmed-meshheading:2617474-Fixatives,
pubmed-meshheading:2617474-Formaldehyde,
pubmed-meshheading:2617474-Humans,
pubmed-meshheading:2617474-Microchemistry,
pubmed-meshheading:2617474-Platelet Adhesiveness,
pubmed-meshheading:2617474-Platelet Glycoprotein GPIb-IX Complex,
pubmed-meshheading:2617474-Platelet Membrane Glycoproteins,
pubmed-meshheading:2617474-Polystyrenes,
pubmed-meshheading:2617474-Protein Conformation,
pubmed-meshheading:2617474-von Willebrand Factor
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pubmed:year |
1989
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pubmed:articleTitle |
Glycocalicin binding to von Willebrand factor adsorbed onto collagen-coated or polystyrene surfaces.
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pubmed:affiliation |
Hematology Division, Brigham and Women's Hospital, Boston, MA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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