Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor
Autor: | Miquella G. Chavez, Christian A. Buhr, Whitney K. Petrie, Angela Wandinger-Ness, Donna F. Kusewitt, Laurie G. Hudson |
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Jazyk: | angličtina |
Rok vydání: | 2012 |
Předmět: | |
Zdroj: | Dermatology Research and Practice, Vol 2012 (2012) |
Druh dokumentu: | article |
ISSN: | 1687-6105 1687-6113 |
DOI: | 10.1155/2012/309587 |
Popis: | 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. |
Databáze: | Directory of Open Access Journals |
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