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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2007-2-13
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pubmed:abstractText |
Interactions between E-cadherin, beta-catenin and PTP1B (protein tyrosine phosphatase 1B) are crucial for the organization of AJs (adherens junctions) and epithelial cell-cell adhesion. In the present study, the effect of acetaldehyde on the AJs and on the interactions between E-cadherin, beta-catenin and PTP1B was determined in Caco-2 cell monolayers. Treatment of cell monolayers with acetaldehyde induced redistribution of E-cadherin and beta-catenin from the intercellular junctions by a tyrosine phosphorylation-dependent mechanism. The PTPase activity associated with E-cadherin and beta-catenin was significantly reduced and the interaction of PTP1B with E-cadherin and beta-catenin was attenuated by acetaldehyde. Acetaldehyde treatment resulted in phosphorylation of beta-catenin on tyrosine residues, and abolished the interaction of beta-catenin with E-cadherin by a tyrosine kinase-dependent mechanism. Protein binding studies showed that the treatment of cells with acetaldehyde reduced the binding of beta-catenin to the C-terminal region of E-cadherin. Pairwise binding studies using purified proteins indicated that the direct interaction between E-cadherin and beta-catenin was reduced by tyrosine phosphorylation of beta-catenin, but was unaffected by tyrosine phosphorylation of E-cadherin-C. Treatment of cells with acetaldehyde also reduced the binding of E-cadherin to GST (glutathione S-transferase)-PTP1B. The pairwise binding study showed that GST-E-cadherin-C binds to recombinant PTP1B, but this binding was significantly reduced by tyrosine phosphorylation of E-cadherin. Acetaldehyde increased the phosphorylation of beta-catenin on Tyr-331, Tyr-333, Tyr-654 and Tyr-670. These results show that acetaldehyde induces disruption of interactions between E-cadherin, beta-catenin and PTP1B by a phosphorylation-dependent mechanism.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-10187801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-10593980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-10753201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-10798595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-11279024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-11710913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-11984870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-12107032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-12169098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-12377785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-12604349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-12755455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-12824418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-12841864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-14675348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-15082451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-15161014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-15166657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-2914637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-3049625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-7542250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-7642713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-8135747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-8185635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-8707857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-8727253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-8811162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-9786960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17087658-9835287
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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/Acetaldehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/occludin,
http://linkedlifedata.com/resource/pubmed/chemical/zonula occludens-1 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
402
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
291-300
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17087658-Acetaldehyde,
pubmed-meshheading:17087658-Adherens Junctions,
pubmed-meshheading:17087658-Amino Acid Sequence,
pubmed-meshheading:17087658-Caco-2 Cells,
pubmed-meshheading:17087658-Cadherins,
pubmed-meshheading:17087658-Humans,
pubmed-meshheading:17087658-Membrane Proteins,
pubmed-meshheading:17087658-Molecular Sequence Data,
pubmed-meshheading:17087658-Phosphoproteins,
pubmed-meshheading:17087658-Phosphorylation,
pubmed-meshheading:17087658-Phosphotyrosine,
pubmed-meshheading:17087658-Protein Binding,
pubmed-meshheading:17087658-Protein Tyrosine Phosphatase, Non-Receptor Type 1,
pubmed-meshheading:17087658-Protein Tyrosine Phosphatases,
pubmed-meshheading:17087658-Protein-Tyrosine Kinases,
pubmed-meshheading:17087658-Tight Junctions,
pubmed-meshheading:17087658-beta Catenin
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pubmed:year |
2007
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pubmed:articleTitle |
Acetaldehyde dissociates the PTP1B-E-cadherin-beta-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism.
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pubmed:affiliation |
Department of Physiology, University of Tennessee Health Science Center, University of Memphis, Memphis, TN 38163, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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