Linked Life Data

1342292

Source:http://linkedlifedata.com/resource/pubmed/id/1342292

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-2-10
pubmed:abstractText
Traditionally, plasmin generation has been conceptualized as a process oriented on the surface of a fibrin-containing thrombus. Recent work, however, indicated that plasminogen and its activators, tissue plasminogen activator (t-PA) and urokinase, can assemble on the surface of cultured human umbilical vein endothelial cells (HUVECs). On binding to HUVECs, plasminogen is activated by t-PA approximately 12-fold more efficiently than fluid-phase plasminogen, and is converted to a plasmin-modified form, possibly unique to cell surfaces. In addition, t-PA interacts with HUVECs at two sites. The major binding site preserves its activity and represents a true (relative molecular weight 40,000) membrane-associated exoreceptor. The low-density lipoprotein (LDL)-like lipoprotein, lipoprotein(a), is highly associated with atherosclerosis, bears striking sequence homology to plasminogen, and competes with plasminogen for cell surface binding. In summary, functional assembly of plasminogen and t-PA may represent an important thromboregulatory system.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1047-2797
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
419-26
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Assembly of plasmin-generating proteins on the surface of human endothelial cells.
pubmed:affiliation
Department of Medicine, Cornell University Medical College, New York, NY 10021.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't