| pubmed-article:11150026 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11150026 | lifeskim:mentions | umls-concept:C0042971 | lld:lifeskim |
| pubmed-article:11150026 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:11150026 | lifeskim:mentions | umls-concept:C0205161 | lld:lifeskim |
| pubmed-article:11150026 | lifeskim:mentions | umls-concept:C1282974 | lld:lifeskim |
| pubmed-article:11150026 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:11150026 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11150026 | pubmed:dateCreated | 2001-1-26 | lld:pubmed |
| pubmed-article:11150026 | pubmed:abstractText | We describe a von Willebrand disease (VWD) variant characterized by low plasma and platelet von Willebrand factor (VWF), impaired ristocetin-induced VWF binding to platelet glycoprotein Ib (GPIb), and abnormal VWF multimer pattern not associated with the absence of large forms. A C-to-T transition at nucleotide 4120 in exon 28 of the VWF gene was found; this mutation introduces a cysteine at the codon for Arg 611 of mature VWF. In addition to the decreased factor VIII (FVIII) and VWF levels, ristocetin-induced platelet aggregation (RIPA) was almost absent, and VWF ristocetin cofactor activity (VWF:RCo) was significantly more decreased than VWF antigen. The patients (mother and son) also showed a defect in VWF collagen-binding activity. Plasma VWF multimers were decreased, with no limit in the size of large forms, and the normal discontinuous multimer organization was replaced by a diffuse smear, especially detectable in the large forms. This picture was emphasized by 1-deamino-8-D -arginine vasopressin (DDAVP) infusion, so that the abnormal VWF multimers appeared to have a molecular weight higher than those present in, or released by, human umbilical vein endothelial cells. DDAVP also increased FVIII and VWF levels but did not normalize the GPIb-dependent VWF functions expressed as RIPA and VWF:RCo. We include this variant in type 2M VWD, focusing on the abnormality in GPIb-dependent VWF function. We advance that this defect depends on the mutation in the GPIb binding domain of VWF rather than the abnormal VWF multimer pattern. | lld:pubmed |
| pubmed-article:11150026 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11150026 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11150026 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11150026 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11150026 | pubmed:issn | 0022-2143 | lld:pubmed |
| pubmed-article:11150026 | pubmed:author | pubmed-author:GirolamiAA | lld:pubmed |
| pubmed-article:11150026 | pubmed:author | pubmed-author:CasonatoAA | lld:pubmed |
| pubmed-article:11150026 | pubmed:author | pubmed-author:SartorelliLL | lld:pubmed |
| pubmed-article:11150026 | pubmed:author | pubmed-author:PontaraEE | lld:pubmed |
| pubmed-article:11150026 | pubmed:author | pubmed-author:BertomoroAA | lld:pubmed |
| pubmed-article:11150026 | pubmed:author | pubmed-author:DuranteCC | lld:pubmed |
| pubmed-article:11150026 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11150026 | pubmed:volume | 137 | lld:pubmed |
| pubmed-article:11150026 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11150026 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11150026 | pubmed:pagination | 70-6 | lld:pubmed |
| pubmed-article:11150026 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:11150026 | pubmed:meshHeading | pubmed-meshheading:11150026... | lld:pubmed |
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| pubmed-article:11150026 | pubmed:meshHeading | pubmed-meshheading:11150026... | lld:pubmed |
| pubmed-article:11150026 | pubmed:meshHeading | pubmed-meshheading:11150026... | lld:pubmed |
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| pubmed-article:11150026 | pubmed:meshHeading | pubmed-meshheading:11150026... | lld:pubmed |
| pubmed-article:11150026 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11150026 | pubmed:articleTitle | Type 2M von Willebrand disease variant characterized by abnormal von willebrand factor multimerization. | lld:pubmed |
| pubmed-article:11150026 | pubmed:affiliation | Department of Medical and Surgical Sciences and the Second Chair of Internal Medicine, University of Padua Medical School, Italy. | lld:pubmed |
| pubmed-article:11150026 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11150026 | pubmed:publicationType | Case Reports | lld:pubmed |
| pubmed-article:11150026 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
