pubmed-article:15070682 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C0221464 | lld:lifeskim |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C0040038 | lld:lifeskim |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C0015982 | lld:lifeskim |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C0302148 | lld:lifeskim |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C0525038 | lld:lifeskim |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C0040371 | lld:lifeskim |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:15070682 | lifeskim:mentions | umls-concept:C2347946 | lld:lifeskim |
pubmed-article:15070682 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:15070682 | pubmed:dateCreated | 2004-4-8 | lld:pubmed |
pubmed-article:15070682 | pubmed:abstractText | Thrombophilic dysfibrinogen Tokyo V was identified in a 43-year-old man with recurrent thromboembolism. Based on analyses of the patient fibrinogen genes, the amino acid sequence of the aberrant fibrinogen peptide, and deglycosylation experiments, fibrinogen Tokyo V was shown to have an amino acid substitution of gamma Ala327Thr and possibly extra glycosylation at gamma Asn325 because the mutation confers the N-linked glycosylation consensus sequence Asn-X-Thr. The mutation resulted in impaired function and hypofibrinogenemia (hypodysfibrinogen). Polymerization of fibrin monomers derived from patient fibrinogen was severely impaired with a partial correction in the presence of calcium, resulting in very low clottability. Additionally, a large amount of soluble cross-linked fibrin was formed upon thrombin treatment in the presence of factor XIII and calcium. However, Tokyo V-derived fibrin was resistant to degradation by tissue plasminogen activator (tPA)-catalyzed plasmin digestion. The structure of Tokyo V fibrin appeared severely perturbed, since there are large pores inside the tangled fibrin networks and fiber ends at the boundaries. Taken together, these data suggest that Tokyo V fibrin clots are fragile, so that fibrinolysis-resistant insoluble fibrin and soluble fibrin polymers may be released to the circulation, partly accounting for the recurrent embolic episodes in the patient. | lld:pubmed |
pubmed-article:15070682 | pubmed:language | eng | lld:pubmed |
pubmed-article:15070682 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070682 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:15070682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070682 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15070682 | pubmed:month | Apr | lld:pubmed |
pubmed-article:15070682 | pubmed:issn | 0006-4971 | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:KitamuraNobor... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:SugoTerukoT | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:KashiwakuraYu... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:HamanoAkieiA | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:SakataYoichiY | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:ItohTakeyoshi... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:OnoTomokoT | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:MatsudaMichio... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:MadoiwaSeijiS | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:MimuroJunJ | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:NishinaritaSu... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:AoshimaMotono... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:TakanoKatsuhi... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:IshiwataAkira... | lld:pubmed |
pubmed-article:15070682 | pubmed:author | pubmed-author:NiwaKazukiK | lld:pubmed |
pubmed-article:15070682 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15070682 | pubmed:day | 15 | lld:pubmed |
pubmed-article:15070682 | pubmed:volume | 103 | lld:pubmed |
pubmed-article:15070682 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15070682 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15070682 | pubmed:pagination | 3045-50 | lld:pubmed |
pubmed-article:15070682 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:15070682 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15070682 | pubmed:articleTitle | Thrombophilic dysfibrinogen Tokyo V with the amino acid substitution of gammaAla327Thr: formation of fragile but fibrinolysis-resistant fibrin clots and its relevance to arterial thromboembolism. | lld:pubmed |
pubmed-article:15070682 | pubmed:affiliation | Division of Cell and Molecular Medicine, Center for Molecular Medicine, Jichi Medical School, Tochigi-ken, Japan. | lld:pubmed |
pubmed-article:15070682 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15070682 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:15070682 | pubmed:publicationType | Case Reports | lld:pubmed |
pubmed-article:15070682 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15070682 | lld:pubmed |