| pubmed-article:10793144 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10793144 | lifeskim:mentions | umls-concept:C1521816 | lld:lifeskim |
| pubmed-article:10793144 | lifeskim:mentions | umls-concept:C1182610 | lld:lifeskim |
| pubmed-article:10793144 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:10793144 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
| pubmed-article:10793144 | lifeskim:mentions | umls-concept:C1420744 | lld:lifeskim |
| pubmed-article:10793144 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10793144 | pubmed:dateCreated | 2000-8-3 | lld:pubmed |
| pubmed-article:10793144 | pubmed:abstractText | The tight junction is the most apical intercellular junction of epithelial cells and regulates transepithelial permeability through the paracellular pathway. To examine possible functions for the tight junction-associated protein ZO-1, C-terminally truncated mutants and a deletion mutant of ZO-1 were epitope tagged and stably expressed in corneal epithelial cell lines. Only full-length ZO-1 and one N-terminal truncation mutant targeted to cell borders; other mutants showed variable cytoplasmic distributions. None of the mutants initially disrupted the localization of endogenous ZO-1. However, long-term stable expression of two of the N-terminal mutants resulted in a dramatic change in cell shape and patterns of gene expression. An elongated fibroblast-like shape replaced characteristic epithelial cobblestone morphology. In addition, vimentin and smooth muscle actin expression were up-regulated, although variable cytokeratin expression remained, suggesting a partial transformation to a mesenchymal cell type. Concomitant with the morphological change, the expression of the integral membrane tight junction protein occludin was significantly down-regulated. The localizations of endogenous ZO-1 and another family member, ZO-2, were disrupted. These findings suggest that ZO-1 may participate in regulation of cellular differentiation. | lld:pubmed |
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| pubmed-article:10793144 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10793144 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10793144 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10793144 | pubmed:month | May | lld:pubmed |
| pubmed-article:10793144 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:10793144 | pubmed:author | pubmed-author:PaulDD | lld:pubmed |
| pubmed-article:10793144 | pubmed:author | pubmed-author:GoodenoughD... | lld:pubmed |
| pubmed-article:10793144 | pubmed:author | pubmed-author:RyeomS WSW | lld:pubmed |
| pubmed-article:10793144 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10793144 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:10793144 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10793144 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10793144 | pubmed:pagination | 1687-96 | lld:pubmed |
| pubmed-article:10793144 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10793144 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10793144 | pubmed:articleTitle | Truncation mutants of the tight junction protein ZO-1 disrupt corneal epithelial cell morphology. | lld:pubmed |
| pubmed-article:10793144 | pubmed:affiliation | Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:10793144 | pubmed:publicationType | Journal Article | lld:pubmed |
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