Linked Life Data

2010538

Source:http://linkedlifedata.com/resource/pubmed/id/2010538

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-5-7
pubmed:abstractText
Many variants of von Willebrand disease (vWD) with qualitatively abnormal von Willebrand factor (vWF) are recognized. In vWD type IIB, the abnormal protein displays enhanced affinity for a platelet vWF receptor, the glycoprotein Ib-IX complex. 14 patients from 7 unrelated families with vWD type IIB were studied to determine the molecular basis for this phenotype. Specific oligonucleotide primers were used to amplify portions of vWF exon 28 encoding a domain that interacts with the platelet glycoprotein Ib-IX complex. Candidate missense mutations were identified for all 14 patients by DNA sequencing, allele specific oligonucleotide hybridization, and restriction endonuclease digestion. These sequence changes occur in an 11 amino acid segment within a single disulfide loop bounded by Cys(509) and Cys(695). All of these sequence changes are C----T transitions within CG dinucleotides. Six patients from two unrelated families were heterozygous for the encoded sequence Arg(543)----Trp. Seven patients from four unrelated families were heterozygous for the encoded sequence Arg(545)----Cys; this sequence change appears to have occurred independently three times, once as a new spontaneous mutation. One patient with apparently sporadic vWD type IIB was heterozygous for the encoded sequence Val(553)----Met, and this appears to be a new mutation. None of these sequence changes was found in 100 normal alleles. These findings suggest that vWD type IIB may be caused by relatively few distinct mutations, that these mutations may cluster within a specific region of one disulfide loop in vWF domain A1, and that this region can modulate the affinity of vWF for the platelet glycoprotein Ib-IX complex.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-1988024, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2293764, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2377450, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2448875, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2461363, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2477370, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2584182, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2657729, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2690940, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2783833, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2786201, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2864688, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2932740, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-2934387, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3028536, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3033024, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3097553, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3491540, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3497666, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3500738, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3502076, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-355893, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-3856838, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6253938, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6286015, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6325506, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6412139, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6767976, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6773982, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6798442, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6805532, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6855599, http://linkedlifedata.com/resource/pubmed/commentcorrection/2010538-6982737
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9738
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1220-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Molecular basis of von Willebrand disease type IIB. Candidate mutations cluster in one disulfide loop between proposed platelet glycoprotein Ib binding sequences.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't