| pubmed-article:16176977 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16176977 | lifeskim:mentions | umls-concept:C0221908 | lld:lifeskim |
| pubmed-article:16176977 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:16176977 | lifeskim:mentions | umls-concept:C0332464 | lld:lifeskim |
| pubmed-article:16176977 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:16176977 | lifeskim:mentions | umls-concept:C1514721 | lld:lifeskim |
| pubmed-article:16176977 | lifeskim:mentions | umls-concept:C0173022 | lld:lifeskim |
| pubmed-article:16176977 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:16176977 | pubmed:dateCreated | 2005-11-24 | lld:pubmed |
| pubmed-article:16176977 | pubmed:abstractText | Although ras mutations have been shown to affect epithelial architecture and polarity, their role in altering tight junctions remains unclear. Transfection of a valine-12 mutated ras construct into LLC-PK1 renal epithelia produces leakiness of tight junctions to certain types of solutes. Transepithelial permeability of D-mannitol increases sixfold but transepithelial electrical resistance increases >40%. This indicates decreased paracellular permeability to NaCl but increased permeability to nonelectrolytes. Permeability increases to D-mannitol (Mr 182), polyethylene glycol (Mr 4000), and 10,000-Mr methylated dextran but not to 2,000,000-Mr methylated dextran. This implies a "ceiling" on the size of solutes that can cross a ras-mutated epithelial barrier and therefore that the increased permeability is not due to loss of cells or junctions. Although the abundance of claudin-2 declined to undetectable levels in the ras-overexpressing cells compared with vector controls, levels of occludin and claudins 1, 4, and 7 increased. The abundance of claudins-3 and -5 remained unchanged. An increase in extracellular signal-regulated kinase-2 phosphorylation suggests that the downstream effects on the tight junction may be due to changes in the mitogen-activated protein kinase signaling pathway. These selective changes in permeability may influence tumorigenesis by the types of solutes now able to cross the epithelial barrier. | lld:pubmed |
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| pubmed-article:16176977 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16176977 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16176977 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16176977 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16176977 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:AndrianovaE... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:SellChristian... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:SmithDavid... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:FrancisMary... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:ValenzanoMary... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:MullinJames... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:LeathermanJam... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:VerrechioJonJ | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:SnetselaarKar... | lld:pubmed |
| pubmed-article:16176977 | pubmed:author | pubmed-author:LiuMantaoM | lld:pubmed |
| pubmed-article:16176977 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16176977 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:16176977 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16176977 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16176977 | pubmed:pagination | 5538-50 | lld:pubmed |
| pubmed-article:16176977 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16176977 | pubmed:meshHeading | pubmed-meshheading:16176977... | lld:pubmed |
| pubmed-article:16176977 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16176977 | pubmed:articleTitle | Ras mutation impairs epithelial barrier function to a wide range of nonelectrolytes. | lld:pubmed |
| pubmed-article:16176977 | pubmed:affiliation | The Lankenau Institute for Medical Research, Wynnewood, PA 19096, USA. mullinj@mlhs.org | lld:pubmed |
