دورية أكاديمية
The p.R1819_C1948delinsS mutation makes von Willebrand factor ADAMTS13-resistant and reduces its collagen-binding capacity
| العنوان: | The p.R1819_C1948delinsS mutation makes von Willebrand factor ADAMTS13-resistant and reduces its collagen-binding capacity |
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| المؤلفون: | DAIDONE, VIVIANA, SAGA, GIORGIA, BARBON, GIOVANNI, PONTARA, ELENA, PELOSO CATTINI, MARIA GRAZIA, MORPURGO, MARGHERITA, ZANOTTI, GIUSEPPE, CASONATO, SANDRA |
| المساهمون: | Daidone, Viviana, Saga, Giorgia, Barbon, Giovanni, Pontara, Elena, PELOSO CATTINI, MARIA GRAZIA, Morpurgo, Margherita, Zanotti, Giuseppe, Casonato, Sandra |
| بيانات النشر: | Blackwell Publishing Ltd |
| سنة النشر: | 2015 |
| المجموعة: | Padua Research Archive (IRIS - Università degli Studi di Padova) |
| مصطلحات موضوعية: | ADAMTS13, Von Willebrand disease, VWF gene mutation, VWF resistance to ADAMTS13 proteolysi, VWF-ADAMTS13 binding, ADAM Protein, Collagen, Female, Hemorrhage, Human, Male, Protein Binding, von Willebrand Factor, INDEL Mutation, Hematology, Medicine (all) |
| الوصف: | Most circulating von Willebrand factor (VWF) is normally inactive and incapable of binding platelets, but numerous disorders may modify the proportion of active VWF. We explored active VWF levels in patients with von Willebrand disease (VWD) whose VWF had a higher affinity for platelet glycoprotein (GP)Ib, but different susceptibilities to ADAMTS13 and multimer patterns (9 patients lacking large multimers, 10 with a normal pattern); 12 patients with VWF C2362F and R1819_C1948delinsS mutations, which make VWF resistant to ADAMTS13 were also studied. Type 2B patients with abnormal or normal multimers had significantly more active VWF (3·33 ± 1·6 and 3·74 ± 0·74, respectively; normal 0·99 ± 0·23). The type of VWF mutation influenced VWF activation: V1316M was associated with the highest levels in patients with abnormal multimers, and R1341W in those with normal multimers. Pregnancy induced gradually rising active VWF levels and declining platelet counts in one type 2B VWD patient without large multimers. Active VWF levels dropped significantly in patients homozygous for the C2362F mutation or heterozygous for R1819_C1948delinsS mutations (0·2 ± 0·03 and 0·23 ± 0·1, respectively), and less in cases heterozygous for the VWF C2362F mutation (0·55 ± 0·17). We demonstrate that VWF may be more or less activated, with or without any direct involvement of the A1 domain, and regardless of ADAMTS13. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | STAMPA |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/25904363; info:eu-repo/semantics/altIdentifier/wos/WOS:000359259900016; volume:170; issue:4; firstpage:564; lastpage:573; numberofpages:10; journal:BRITISH JOURNAL OF HAEMATOLOGY; http://hdl.handle.net/11577/3174399Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84938555700 |
| DOI: | 10.1111/bjh.13472 |
| DOI: | 10.1111/bjh.13785/epdf |
| الإتاحة: | https://doi.org/10.1111/bjh.13472Test http://hdl.handle.net/11577/3174399Test |
| رقم الانضمام: | edsbas.5F559CE9 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1111/bjh.13472 |
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