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MBC in Press, published online ahead of print January 5, 2005
Mol. Biol. Cell 10.1091/mbc.E04-07-0551

A more recent version of this article appeared on March 1, 2005
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Submitted on July 5, 2004
Revised on November 3, 2004
Accepted on December 16, 2004

Modulation of Epithelial Morphology, Monolayer Permeability, and Cell Migration by Gas3/PMP22

Kyle J. Roux, Stephanie A. Amici, Bradley S. Fletcher, and Lucia Notterpek*

Departments of Neuroscience, and Pharmacology and Therapeutics, College of Medicine, University of Florida, Gainesville, FL 32610

Monitoring Editor: Keith Yamamoto

Peripheral myelin protein 22 (PMP22) is associated with a subset of hereditary peripheral neuropathies. Although predominantly recognized as a transmembrane constituent of peripheral nerve myelin, PMP22 is localized to epithelial and endothelial cell-cell junctions, where its function remains unknown. In this report, we investigated the role of PMP22 in epithelial biology. Expression of human PMP22 (hPMP22) slows cell growth and induces a flattened morphology in Madin-Darby canine kidney (MDCK) cells. The transepithelial electrical resistance (TER) and paracellular flux of MDCK monolayers are elevated by hPMP22 expression. Following calcium switch, peptides corresponding to the second, but not the first, extracellular loop of PMP22 perturb the recovery of TER and paracellular flux. Finally, subsequent to wounding, epithelial monolayers expressing hPMP22 fail to migrate normally. These results indicate that PMP22 is capable of modulating several aspects of epithelial cell biology, including junctional permeability and wound closure.

*Corresponding author. E-mail: notterp{at}mbi.ufl.edu




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S. A. Amici, W. A. Dunn Jr, A. J. Murphy, N. C. Adams, N. W. Gale, D. M. Valenzuela, G. D. Yancopoulos, and L. Notterpek
Peripheral Myelin Protein 22 Is in Complex with {alpha}6beta4 Integrin, and Its Absence Alters the Schwann Cell Basal Lamina
J. Neurosci., January 25, 2006; 26(4): 1179 - 1189.
[Abstract] [Full Text] [PDF]


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