Differential downregulation of e-cadherin and desmoglein by epidermal growth factor.
Repository Usage Stats
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 cell : 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.
Published Version (Please cite this version)10.1155/2012/309587
Publication InfoChavez, Miquella G; Buhr, Christian A; Petrie, Whitney K; Wandinger-Ness, Angela; Kusewitt, Donna F; & Hudson, Laurie G (2012). Differential downregulation of e-cadherin and desmoglein by epidermal growth factor. Dermatol Res Pract, 2012. pp. 309587. 10.1155/2012/309587. Retrieved from https://hdl.handle.net/10161/12074.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
More InfoShow full item record