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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2003-5-12
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pubmed:abstractText |
The plasminogen/plasmin system, urokinase-type plasminogen activator (uPA), its receptor (uPAR), and its inhibitor (PAI-1), influence extracellular proteolysis and cell migration in lung injury or neoplasia. In this study, we sought to determine whether tcuPA (two chain uPA) alters expression of its major inhibitor PAI-1 in lung epithelial cells. The expression of PAI-1 was evaluated at the protein and mRNA level by Western blot, immunoprecipitation, and Northern blot analyses. We found that tcuPA treatment enhanced PAI-1 protein and mRNA expression in Beas2B lung epithelial cells in a time- and concentration-dependent manner. The tcuPA-mediated induction of PAI-1 involves post-transcriptional control involving stabilization of PAI-1 mRNA. Inactivation of the catalytic activity of tcuPA had little effect on PAI-1 induction and the activity of the isolated amino-terminal fragment was comparable with full-length single- or two-chain uPA. In contrast, deletion of either the uPA receptor binding growth factor domain or kringle domain (kringle) from full-length single chain uPA markedly attenuated the induction of PAI-1. Induction of PAI-1 by exposure of lung epithelial cells to uPA is a newly recognized pathway by which PAI-1 could regulate local fibrinolysis and urokinase-dependent cellular responses in the setting of lung inflammation or neoplasia.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18124-31
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12642587-Blotting, Northern,
pubmed-meshheading:12642587-Blotting, Western,
pubmed-meshheading:12642587-Catalysis,
pubmed-meshheading:12642587-Catalytic Domain,
pubmed-meshheading:12642587-Cell Division,
pubmed-meshheading:12642587-Cell Nucleus,
pubmed-meshheading:12642587-Cells, Cultured,
pubmed-meshheading:12642587-DNA, Complementary,
pubmed-meshheading:12642587-Dose-Response Relationship, Drug,
pubmed-meshheading:12642587-Epithelial Cells,
pubmed-meshheading:12642587-Humans,
pubmed-meshheading:12642587-Ligands,
pubmed-meshheading:12642587-Lung,
pubmed-meshheading:12642587-Plasmids,
pubmed-meshheading:12642587-Plasminogen Activator Inhibitor 1,
pubmed-meshheading:12642587-Precipitin Tests,
pubmed-meshheading:12642587-Protein Structure, Tertiary,
pubmed-meshheading:12642587-Protein-Tyrosine Kinases,
pubmed-meshheading:12642587-RNA, Messenger,
pubmed-meshheading:12642587-Time Factors,
pubmed-meshheading:12642587-Transcription, Genetic,
pubmed-meshheading:12642587-Transfection,
pubmed-meshheading:12642587-Urokinase-Type Plasminogen Activator
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pubmed:year |
2003
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pubmed:articleTitle |
Induction of plasminogen activator inhibitor-1 by urokinase in lung epithelial cells.
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pubmed:affiliation |
Department of Specialty Care Services, University of Texas Health Center, Tyler, Texas 75708, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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