Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1987-2-19
pubmed:abstractText
Several heterologous antisera directed against either human or porcine von Willebrand factor (vWF), inhibited botrocetin-induced vWF-dependent agglutination at high concentrations but were found to enhance this reaction at low concentrations. Purified IgG from these immune sera also potentiated botrocetin-induced agglutination as did its F(ab)'2 fragments. However, monovalent Fab fragments of the purified IgG did not. The requirement for a divalent antigen combining region suggests that one possible mechanism of enhanced agglutination may involve intra or inter-molecular cross-linking of vWF multimers by the antibody. Another possible mechanism could be a conformational change in the vWF molecule induced by antibody binding. Such a conformational change may provide additional active sites on the vWF molecule that, in the presence of botrocetin, lead to enhancement of the agglutination reaction. Antisera to human vWF that showed this paradoxical inhibitory/enhancing effect on botrocetin-induced agglutination also inhibited ristocetin-induced platelet agglutination at high concentrations, but failed to enhance agglutination at any concentration. The different effects of these antisera on botrocetin and ristocetin-induced platelet agglutination suggest that no single mechanism can explain the action of both of these mediators.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
749-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
A paradoxical effect of antibody concentration on vWF-dependent platelet agglutination distinguishes between botrocetin and ristocetin-induced agglutination.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.