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Dermatology Research and Practice
Volume 2012 (2012), Article ID 309587, 14 pages
Research Article

Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor

1Division of Bioengineering, Department of Physiology, University of California San Francisco, San Francisco, CA 94158, USA
2College of Pharmacy, University of New Mexico, MSC 09 5360, Albuquerque, NM 87131, USA
3Department of Animal Science, University of California, Davis, CA 95616, USA
4Department of Pathology, School of Medicine, University of New Mexico, MSC 08 4640, Albuquerque, NM 87131, USA
5Science Park Research Division, Department of Carcinogenesis, University of Texas, M.D. Anderson Cancer Center, Smithville, TX 78957, USA

Received 13 July 2011; Revised 1 October 2011; Accepted 2 October 2011

Academic Editor: Aziz Ghahary

Copyright © 2012 Miquella G. Chavez et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Modulation of cell : cell junctions is a key event in cutaneous wound repair. In this study we report that activation of the epidermal growth factor (EGF) receptor disrupts cel : cell adhesion, but with different kinetics and fates for the desmosomal cadherin desmoglein and for E-cadherin. Downregulation of desmoglein preceded that of E-cadherin in vivo and in an EGF-stimulated in vitro wound reepithelialization model. Dual immunofluorescence staining revealed that neither E-cadherin nor desmoglein-2 internalized with the EGF receptor, or with one another. In response to EGF, desmoglein-2 entered a recycling compartment based on predominant colocalization with the recycling marker Rab11. In contrast, E-cadherin downregulation was accompanied by cleavage of the extracellular domain. A broad-spectrum matrix metalloproteinase inhibitor protected E-cadherin but not the desmosomal cadherin, desmoglein-2, from EGF-stimulated disruption. These findings demonstrate that although activation of the EGF receptor regulates adherens junction and desmosomal components, this stimulus downregulates associated cadherins through different mechanisms.