| pubmed-article:15606553 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15606553 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:15606553 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:15606553 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15606553 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:15606553 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15606553 | pubmed:dateCreated | 2004-12-20 | lld:pubmed |
| pubmed-article:15606553 | pubmed:abstractText | This study investigated the functional impact of O-linked glycosylation of von Willebrand Factor (VWF) A1 domains on the interaction with platelet receptors. Native or mutant VWF-A1-domains were transiently overexpressed on COS-7 cells as membrane glycosylphosphatidylinositol (GPI)-anchored FLAG-tagged fusion proteins. Cytofluometric analysis assured comparable levels of A1-domain expression among native and mutant homologues as well as for different culture conditions. Expressing native VWF-A1-domains under O-linked glycosylation blocking conditions increased the platelet aggregatory responses observed for fully glycosylated forms. Utilizing a neuronal network for prediction of O-linked glycosylation of mammalian proteins, threonine (T) and serine (S) residues located in the VWF-A1-loop flanking regions - not in the loop itself - were determined to be glycosylated n-terminal at amino acids T485, S490, T492 and T493 and c-terminal at T705. Simultaneous selective charge-to-alanine mutation of S490, T492 and T493 led to gain in aggregatory responses. When compared with native forms, equivalent alterations of T485 did not dictate functional differences. Any alanine-substitution for T705 revealed a substantial loss in aggregatory effects - possibly as a result of structural desintegration of the VWF-A1-binding site for glycoprotein (GP) Ib. These data suggest specific O-linked glycosylation of the amino-terminal VWF-A1-loop-flanking region to have a negative regulatory impact on the A1-domain affinity of non-activated human VWF for human platelet-GPIb. | lld:pubmed |
| pubmed-article:15606553 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15606553 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15606553 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15606553 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15606553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15606553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15606553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15606553 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15606553 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:15606553 | pubmed:issn | 0007-1048 | lld:pubmed |
| pubmed-article:15606553 | pubmed:author | pubmed-author:RogiersXavier... | lld:pubmed |
| pubmed-article:15606553 | pubmed:author | pubmed-author:RobsonSimon... | lld:pubmed |
| pubmed-article:15606553 | pubmed:author | pubmed-author:PeiperMatthia... | lld:pubmed |
| pubmed-article:15606553 | pubmed:author | pubmed-author:EisenbergerCl... | lld:pubmed |
| pubmed-article:15606553 | pubmed:author | pubmed-author:KnoefelWolfra... | lld:pubmed |
| pubmed-article:15606553 | pubmed:author | pubmed-author:Schulte am... | lld:pubmed |
| pubmed-article:15606553 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15606553 | pubmed:volume | 128 | lld:pubmed |
| pubmed-article:15606553 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15606553 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15606553 | pubmed:pagination | 82-90 | lld:pubmed |
| pubmed-article:15606553 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:meshHeading | pubmed-meshheading:15606553... | lld:pubmed |
| pubmed-article:15606553 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15606553 | pubmed:articleTitle | Impact of O-linked glycosylation of the VWF-A1-domain flanking regions on platelet interaction. | lld:pubmed |
| pubmed-article:15606553 | pubmed:affiliation | Clinic for General and Visceral Surgery, Heinrich Heine University Duesseldorf, Germany. jan.schulteamesch@uni-duesseldorf.de | lld:pubmed |
| pubmed-article:15606553 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15606553 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15606553 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15606553 | lld:pubmed |
