Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor
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. Downregul...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | Dermatology Research and Practice |
| Online Access: | http://dx.doi.org/10.1155/2012/309587 |
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| author | Miquella G. Chavez Christian A. Buhr Whitney K. Petrie Angela Wandinger-Ness Donna F. Kusewitt Laurie G. Hudson |
| author_facet | Miquella G. Chavez Christian A. Buhr Whitney K. Petrie Angela Wandinger-Ness Donna F. Kusewitt Laurie G. Hudson |
| author_sort | Miquella G. Chavez |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-27a05f773d014fba81802fdab5dc4e5d |
| institution | Kabale University |
| issn | 1687-6105 1687-6113 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Dermatology Research and Practice |
| spelling | doaj-art-27a05f773d014fba81802fdab5dc4e5d2025-02-03T01:12:09ZengWileyDermatology Research and Practice1687-61051687-61132012-01-01201210.1155/2012/309587309587Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth FactorMiquella G. Chavez0Christian A. Buhr1Whitney K. Petrie2Angela Wandinger-Ness3Donna F. Kusewitt4Laurie G. Hudson5Division of Bioengineering, Department of Physiology, University of California San Francisco, San Francisco, CA 94158, USACollege of Pharmacy, University of New Mexico, MSC 09 5360, Albuquerque, NM 87131, USADepartment of Animal Science, University of California, Davis, CA 95616, USADepartment of Pathology, School of Medicine, University of New Mexico, MSC 08 4640, Albuquerque, NM 87131, USAScience Park Research Division, Department of Carcinogenesis, University of Texas, M.D. Anderson Cancer Center, Smithville, TX 78957, USACollege of Pharmacy, University of New Mexico, MSC 09 5360, Albuquerque, NM 87131, USAModulation 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.http://dx.doi.org/10.1155/2012/309587 |
| spellingShingle | Miquella G. Chavez Christian A. Buhr Whitney K. Petrie Angela Wandinger-Ness Donna F. Kusewitt Laurie G. Hudson Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor Dermatology Research and Practice |
| title | Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor |
| title_full | Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor |
| title_fullStr | Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor |
| title_full_unstemmed | Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor |
| title_short | Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor |
| title_sort | differential downregulation of e cadherin and desmoglein by epidermal growth factor |
| url | http://dx.doi.org/10.1155/2012/309587 |
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