| pubmed-article:11717414 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11717414 | lifeskim:mentions | umls-concept:C2700453 | lld:lifeskim |
| pubmed-article:11717414 | lifeskim:mentions | umls-concept:C0014609 | lld:lifeskim |
| pubmed-article:11717414 | lifeskim:mentions | umls-concept:C0021721 | lld:lifeskim |
| pubmed-article:11717414 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:11717414 | pubmed:dateCreated | 2001-12-5 | lld:pubmed |
| pubmed-article:11717414 | pubmed:abstractText | Alterations in peripheral myelin protein 22 (PMP22) gene expression are associated with a host of heritable demyelinating peripheral neuropathies, yet the function of the protein remains unknown. PMP22 expression is highest in myelinating Schwann cells of peripheral nerves; however, significant levels of PMP22 mRNAs can be detected in a variety of non-neural tissue, including epithelia. To date, PMP22 protein expression and localization in non-neural tissues have not been studied in detail. In adult rat liver and intestine, and cultured epithelial cells, we detected PMP22-like immunoreactivity associated with markers of the tight junctional complex, including zonula occludens 1 (ZO-1) and occludin. Upon disruption of intercellular contacts, PMP22 was internalized into vesicles that were immunoreactive for both anti-occludin and anti-PMP22 antibodies. Nonionic detergent extraction of cultured epithelial cells did not solubilize PMP22, as the majority of the protein remained in the detergent insoluble fraction, as did ZO-1 and occludin. We also observed the targeting of exogenous myc-tagged PMP22 to apical cell junctions in polarized epithelia and to anti-ZO-1 antibody immunoreactive cell contacts of L fibroblasts. These studies support a role for PMP22 at intercellular junctions of epithelia and may indicate a similar function in myelinating Schwann cells. Furthermore, our findings could provide an explanation for certain phenotypes of PMP22 neuropathy mice that cannot be accounted for by dysmyelination. | lld:pubmed |
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| pubmed-article:11717414 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11717414 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11717414 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11717414 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11717414 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11717414 | pubmed:author | pubmed-author:FletcherB SBS | lld:pubmed |
| pubmed-article:11717414 | pubmed:author | pubmed-author:RahnerCC | lld:pubmed |
| pubmed-article:11717414 | pubmed:author | pubmed-author:NotterpekLL | lld:pubmed |
| pubmed-article:11717414 | pubmed:author | pubmed-author:RouxK JKJ | lld:pubmed |
| pubmed-article:11717414 | pubmed:author | pubmed-author:AmiciS ASA | lld:pubmed |
| pubmed-article:11717414 | pubmed:author | pubmed-author:YazdanpourAA | lld:pubmed |
| pubmed-article:11717414 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11717414 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:11717414 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:11717414 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11717414 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11717414 | pubmed:pagination | 14404-9 | lld:pubmed |
| pubmed-article:11717414 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11717414 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11717414 | pubmed:articleTitle | Peripheral myelin protein 22 is a constituent of intercellular junctions in epithelia. | lld:pubmed |
| pubmed-article:11717414 | pubmed:affiliation | Department of Neuroscience, McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA. notterp@ufbi.ufl.edu | lld:pubmed |
| pubmed-article:11717414 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11717414 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11717414 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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