Linked Life Data

21070595

Source:http://linkedlifedata.com/resource/pubmed/id/21070595

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-1-28
pubmed:abstractText
Endothelial von Willebrand factor (VWF) mediates platelet adhesion and acts as a protective chaperone to clotting factor VIII. Rapid release of highly multimerized VWF is particularly effective in promoting hemostasis. To produce this protein, an elaborate biogenesis is required, culminating at the trans-Golgi network (TGN) in storage within secretory granules called Weibel-Palade bodies (WPB). Failure to correctly form these organelles can lead to uncontrolled secretion of low-molecular-weight multimers of VWF. The TGN-associated adaptor AP-1 and its interactors clathrin, aftiphilin and ?-synergin are essential to initial WPB formation at the Golgi apparatus, and thus to VWF storage and secretion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1538-7836
pubmed:author
pubmed:copyrightInfo
© 2011 International Society on Thrombosis and Haemostasis.
pubmed:issnType
Electronic
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
392-401
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
A role for Rab10 in von Willebrand factor release discovered by an AP-1 interactor screen in C. elegans.
pubmed:affiliation
INSERM Avenir team Trafic intracellulaire et polarité chez C. elegans, Rennes, France. gmichaux@univ-rennes1.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't