Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-8-29
pubmed:abstractText
Vitamin K-dependent protein S and complement regulator C4b-binding protein (C4BP) form a high-affinity complex in plasma. We have previously shown that both free protein S and the C4BP-protein S complex can bind to apoptotic Jurkat cells. It has been demonstrated in the past that protein S and C4BP can bind to neutrophils. We now show that it is only the apoptotic neutrophil population that binds these proteins. In addition, we also show that binding is mediated through the Gla domain on protein S, which binds negatively charged phospholipids, since a monoclonal antibody directed against this domain blocks the binding. Thus, we conclude that binding of protein S and the C4BP-protein S complex to neutrophils is not cell specific, but rather apoptosis dependent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0957-5235
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
355-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The binding of protein S and the protein S-C4BP complex to neutrophils is apoptosis dependent.
pubmed:affiliation
Division of Clinical Chemistry, Department of Laboratory Medicine, Lund University, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't