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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
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|
pubmed:dateCreated |
2000-3-7
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|
pubmed:abstractText |
The annexins constitute a family of calcium-dependent membrane binding proteins. Recently, annexin II has been shown to accelerate the activation of the clot-dissolving protease plasmin by complexing with the plasmin precursor plasminogen and with tissue plasminogen activator. Binding of plasminogen to annexin II is inhibited by the atherogenic lipoprotein, lipoprotein(a), while binding of tissue plasminogen activator to annexin II is blocked by the thiol amino acid homocysteine. Formation of the plasminogen/tissue plasminogen activator/annexin II complex may represent a key regulatory mechanism in fibrinolytic surveillance.
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pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
1050-1738
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
9
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
128-38
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|
pubmed:dateRevised |
2009-11-19
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|
pubmed:meshHeading |
pubmed-meshheading:10639727-Amino Acid Sequence,
pubmed-meshheading:10639727-Animals,
pubmed-meshheading:10639727-Annexin A2,
pubmed-meshheading:10639727-Endothelium, Vascular,
pubmed-meshheading:10639727-Fibrinolysin,
pubmed-meshheading:10639727-Fibrinolysis,
pubmed-meshheading:10639727-Humans,
pubmed-meshheading:10639727-Molecular Sequence Data,
pubmed-meshheading:10639727-Plasminogen,
pubmed-meshheading:10639727-Receptors, Cell Surface,
pubmed-meshheading:10639727-Structure-Activity Relationship,
pubmed-meshheading:10639727-Tissue Plasminogen Activator
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|
pubmed:year |
1999
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|
pubmed:articleTitle |
Annexin II: a mediator of the plasmin/plasminogen activator system.
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|
pubmed:affiliation |
Department of Pediatrics, Weill Medical College of Cornell University, New York, New York 10021, USA.
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|
pubmed:publicationType |
Journal Article,
Review
|
