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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1990-6-8
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pubmed:abstractText |
Platelets from patients with platelet-type von Willebrand disease (vWD) were used as immunogens for the production of murine monoclonal antibodies (MoAbs). One such MoAb, C-34, inhibited ristocetin-induced aggregation of patient or normal platelets, but not aggregation induced by other aggregating agents. As demonstrated by crossed-immunoelectrophoresis, C-34 recognized an epitope within the GPIb/IX complex. In indirect immunofluorescence studies on fresh platelets, the ratio of any of four different anti-GPIb MoAbs to one another was near unity (0.88-1.14) both for normals and for patients. In contrast, the ratio of the binding of C-34 to such a MoAb (AP-1) was 0.31 +/- 0.02 (means +/- SE) for normal platelets and significantly increased to 0.54 +/- 0.01 for patient platelets (P less than 0.001). In NP-40 lysates of 3H-labelled platelets, saturating concentrations of C-34 produced much fainter bands than did AS-2 or other anti-GPIb MoAbs in the GPIb and GPIX regions. In contrast to the other anti-GPIb MoAbs, C-34 did not bind to the purified 125I-labelled glycocalicin fragment of GPIb, to the glycocalicin derivative identified by crossed-immunoelectrophoresis, or to the amino-terminal approximately 40 kDa portion of GPIb alpha cleaved from 3H-labelled platelets by trypsin. C-34 appears to be the first MoAb that is quantitatively informative in identifying the abnormal platelets in platelet-type vWD. The observed differences between the patient and normal platelets may reflect an abnormality in the primary structure of the GPIb/IX complex. Alternatively, patient platelets may have an abnormality of other structures near this region that impose less of a steric hindrance upon binding of antibody to the C-34 epitope.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0007-1048
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
313-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1692230-Animals,
pubmed-meshheading:1692230-Antibodies, Monoclonal,
pubmed-meshheading:1692230-Blood Platelets,
pubmed-meshheading:1692230-Epitopes,
pubmed-meshheading:1692230-Humans,
pubmed-meshheading:1692230-Immunoelectrophoresis, Two-Dimensional,
pubmed-meshheading:1692230-Mice,
pubmed-meshheading:1692230-Mice, Inbred BALB C,
pubmed-meshheading:1692230-Platelet Aggregation,
pubmed-meshheading:1692230-Platelet Membrane Glycoproteins,
pubmed-meshheading:1692230-Ristocetin,
pubmed-meshheading:1692230-von Willebrand Diseases
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pubmed:year |
1990
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pubmed:articleTitle |
Increased platelet sensitivity to ristocetin is predicted by the binding characteristics of a GPIb/IX determinant.
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pubmed:affiliation |
Department of Pathology, SUNY Health Science Center, Syracuse, N.Y.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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