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rdf:type |
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lifeskim:mentions |
umls-concept:C0007102,
umls-concept:C0023884,
umls-concept:C0027108,
umls-concept:C0031715,
umls-concept:C0035647,
umls-concept:C0036525,
umls-concept:C0334227,
umls-concept:C0392756,
umls-concept:C0812204,
umls-concept:C1522484,
umls-concept:C1533691,
umls-concept:C1622501,
umls-concept:C1709130,
umls-concept:C1998811
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pubmed:issue |
2
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pubmed:dateCreated |
2003-11-25
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pubmed:abstractText |
The nm23-H1 gene is known as a potential metastasis suppressor gene in various types of carcinomas. However, the role of nm23-H1 in colorectal carcinoma still remains controversial and the cellular mechanisms by which its protein may modulate the metastatic phenotype are not yet known. We transfected nm23-H1 cDNA into the human colon cancer cell line, HT-29, to test the effects and cellular biological mechanism of nm23 protein in colon cancer. We found that nm23-H1 strongly inhibited the liver metastasis of HT-29 cells in nude mice and inhibited the epidermal growth factor (EGF)-induced cell migration in vitro. Furthermore, we clarified the regulation of the myosin light chain (MLC) phosphorylation by nm23-H1, which has been demonstrated as having potential role in cell migration.
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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/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase...,
http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Light Chains,
http://linkedlifedata.com/resource/pubmed/chemical/NM23 Nucleoside Diphosphate Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/NME1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nme1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Diphosphate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Markers, Biological
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0020-7136
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2003 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
108
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
207-11
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14639604-Animals,
pubmed-meshheading:14639604-Cell Movement,
pubmed-meshheading:14639604-Colonic Neoplasms,
pubmed-meshheading:14639604-Enzyme Activation,
pubmed-meshheading:14639604-Epidermal Growth Factor,
pubmed-meshheading:14639604-Humans,
pubmed-meshheading:14639604-Liver Neoplasms,
pubmed-meshheading:14639604-Mice,
pubmed-meshheading:14639604-Mice, Nude,
pubmed-meshheading:14639604-Mitogen-Activated Protein Kinase Kinases,
pubmed-meshheading:14639604-Monomeric GTP-Binding Proteins,
pubmed-meshheading:14639604-Myosin Light Chains,
pubmed-meshheading:14639604-NM23 Nucleoside Diphosphate Kinases,
pubmed-meshheading:14639604-Nucleoside-Diphosphate Kinase,
pubmed-meshheading:14639604-Phosphorylation,
pubmed-meshheading:14639604-Transcription Factors,
pubmed-meshheading:14639604-Transfection,
pubmed-meshheading:14639604-Tumor Cells, Cultured,
pubmed-meshheading:14639604-Tumor Markers, Biological
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pubmed:year |
2004
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pubmed:articleTitle |
nm23-H1 reduces in vitro cell migration and the liver metastatic potential of colon cancer cells by regulating myosin light chain phosphorylation.
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pubmed:affiliation |
Department of Cancer and Thoracic Surgery, Okayama University Graduate School of Medicine and Dentistry, Okayama, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro
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