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rdf:type |
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lifeskim:mentions |
umls-concept:C0007600,
umls-concept:C0085862,
umls-concept:C0086418,
umls-concept:C0205263,
umls-concept:C0392747,
umls-concept:C0443172,
umls-concept:C0600139,
umls-concept:C1299583,
umls-concept:C1518174,
umls-concept:C1521991,
umls-concept:C1549571,
umls-concept:C1608386,
umls-concept:C2677316,
umls-concept:C2745880
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pubmed:issue |
7
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pubmed:dateCreated |
2007-6-18
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pubmed:abstractText |
Expression of prostasin in the PC-3 human prostate carcinoma cells inhibited in vitro invasion, but the molecular mechanisms are unknown. Wild-type human prostasin or a serine active-site mutant prostasin was expressed in the PC-3 cells. Molecular changes were measured at the mRNA and the protein levels. Cell signaling changes were evaluated by measuring phosphorylation of the extracellular signal-regulated kinases (Erk1/2) following epidermal growth factor (EGF) treatment of the cells. Protein expression of the EGF receptor (EGFR) was differentially down-regulated by the wild-type and the active-site mutant prostasin. The mRNA expression of EGFR and the transcription repressor SLUG was reduced in cells expressing wild-type prostasin but not the active-site mutant. Phosphorylation of Erk1/2 in response to EGF was greatly reduced by the wild-type prostasin but not by the active-site mutant. The mRNA expression of the urokinase-type plasminogen activator (uPA), the uPA receptor (uPAR), cyclooxygenase-2 (COX-2), and the inducible nitric oxide synthase (iNOS) was decreased by the wild-type and the active-site mutant prostasin. The mRNA or protein expression of granulocyte-macrophage colony-stimulating factor (GM-CSF), matriptase, and E-cadherin was greatly increased by the active-site mutant prostasin. In conclusion, prostasin expression elicits both protease-dependent and independent molecular changes in the PC-3 cells.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-10360641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-10688036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-11433419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-11597399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-11774283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-12882393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-14701705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-14991861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-15720812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-15800053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16011659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16061697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16499663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16541421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16638913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16706607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16804520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-16980306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-17018611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-17228523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-304450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-7479394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-7508078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-8339265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17532063-9465939
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Granulocyte-Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II,
http://linkedlifedata.com/resource/pubmed/chemical/PTGS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Urokinase-Type Plasminogen Activator,
http://linkedlifedata.com/resource/pubmed/chemical/matriptase,
http://linkedlifedata.com/resource/pubmed/chemical/prostasin,
http://linkedlifedata.com/resource/pubmed/chemical/snail family transcription factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1773
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1133-40
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17532063-Binding Sites,
pubmed-meshheading:17532063-Cadherins,
pubmed-meshheading:17532063-Cell Line, Tumor,
pubmed-meshheading:17532063-Cyclooxygenase 2,
pubmed-meshheading:17532063-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:17532063-Granulocyte-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:17532063-Humans,
pubmed-meshheading:17532063-Male,
pubmed-meshheading:17532063-Membrane Proteins,
pubmed-meshheading:17532063-Mutation,
pubmed-meshheading:17532063-Nitric Oxide Synthase Type II,
pubmed-meshheading:17532063-Prostatic Neoplasms,
pubmed-meshheading:17532063-Receptor, Epidermal Growth Factor,
pubmed-meshheading:17532063-Serine Endopeptidases,
pubmed-meshheading:17532063-Signal Transduction,
pubmed-meshheading:17532063-Transcription Factors,
pubmed-meshheading:17532063-Urokinase-Type Plasminogen Activator
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pubmed:year |
2007
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pubmed:articleTitle |
Prostasin induces protease-dependent and independent molecular changes in the human prostate carcinoma cell line PC-3.
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pubmed:affiliation |
Biomolecular Science Center, Burnett College of Biomedical Sciences, University of Central Florida, Orlando, FL 32816-2364, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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