Source:http://linkedlifedata.com/resource/pubmed/id/16930554
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2006-9-11
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pubmed:abstractText |
The cell-cell adhesion molecule E-cadherin is stabilized by linking intracellularly with the actin cytoskeleton through PP2A-mediated recruitment of IQGAP1 to Rac1-bound E-cadherin-catenins complex in nonmalignant HME cells. However, little is known about the dysfunction of E-cadherin by loss or reduced expression of PP2A in human breast cancer cells. We report here that both human breast cancer MDA-MB-231 and MCF-7 cells were deficient in expression of the PP2A-A protein and lost the IQGAP1 recruitment to Rac1-bound catenins. In MDA-MB-231 cells, E-cadherin was also deficient. Immunohistochemical analysis of the normal-carcinoma matched human breast tissue arrays revealed that PP2A-A was expressed in 96% of normal tissue specimens but not in 57% of carcinoma specimens. Expression of E-cadherin in MCF-7 cells was 1.5-fold higher than that in HME cells, however, 80% of E-cadherin was endocytosed and incompletely anchored to F-actin. Therefore, we propose that the dysfunction of E-cadherin due to its endocytosis may occur in some proportion of human breast carcinomas in which the PP2A-A protein is lost or significantly reduced.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/IQ motif containing GTPase...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2,
http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
349
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
255-60
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16930554-Actins,
pubmed-meshheading:16930554-Biotinylation,
pubmed-meshheading:16930554-Breast Neoplasms,
pubmed-meshheading:16930554-Cadherins,
pubmed-meshheading:16930554-Carcinoma,
pubmed-meshheading:16930554-Cell Adhesion,
pubmed-meshheading:16930554-Cell Line, Tumor,
pubmed-meshheading:16930554-Cytoskeleton,
pubmed-meshheading:16930554-Endocytosis,
pubmed-meshheading:16930554-Female,
pubmed-meshheading:16930554-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:16930554-Humans,
pubmed-meshheading:16930554-Phosphoprotein Phosphatases,
pubmed-meshheading:16930554-Protein Phosphatase 2,
pubmed-meshheading:16930554-Tissue Distribution,
pubmed-meshheading:16930554-ras GTPase-Activating Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
Induction of E-cadherin endocytosis by loss of protein phosphatase 2A expression in human breast cancers.
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pubmed:affiliation |
Molecular Cell Biology Division, Kanagawa Cancer Center Research Institute, 1-1-2 Nakao, Asahi-ku, Yokohama 241-0815, Japan.
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pubmed:publicationType |
Journal Article
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