Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1992-4-23
pubmed:abstractText
In this study, the ability of factor Xa to protect factor Va from proteolysis by activated protein C (APC) was verified. Interestingly, factor X was found to exert a similar effect with a dose-dependence identical to that of factor Xa. The effects of factor X and Xa were abrogated in the presence of protein S. To further assess the interactions of factor Va with factors Xa, X and APC, direct binding studies were performed. Factor X and Xa bound to factor Va with equal efficacy. Both proteins displaced APC from its factor Va binding site. These interactions were calcium-dependent. Although the binding of factor Xa devoid of its principal calcium binding site (the Gla-domain) to factor Va was identical to that observed using the native protein, its APC inhibitory effects were significantly reduced. These findings suggest that the Gla-domain of factor X (Xa) is pivotal in the protection of factor Va from APC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0957-5235
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
723-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Regulation of activated protein C by factor Xa.
pubmed:affiliation
Department of Medicine, Monash Medical School, Victoria, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't