Endothelial cell (EC) junctions regulate in large part the integrity and barrier function of the vascular endothelium. Advanced glycation end-products (AGEs), the irreversibly formed reactive derivatives of non-enzymic glucose–protein condensation reactions, are strongly implicated in endothelial dysfunction that distinguishes diabetes- and aging-associated vascular complications. The aim of the present study was to determine whether AGEs affect EC lateral junction proteins, with particular regard to the vascular endothelial cadherin (VE-cadherin) complex. Our results indicate that AGE-modified BSA (AGE-BSA), a prototype of advanced glycated proteins, disrupts the VE-cadherin complex when administered to ECs. AGE-BSA, but not unmodified BSA, was found to induce decreases in the levels of VE-cadherin, β-catenin and γ-catenin in the complex and in total cell extracts, as well as a marked reduction in the amount of VE-cadherin present at the cell surface. In contrast, the level of platelet endothelial cell adhesion molecule-1 (PECAM-1), which is located at lateral junctions, was not altered. Supplementation of the cellular antioxidative defences abolished these effects. Finally, the loss of components of the VE-cadherin complex was correlated with increases in vascular permeability and in EC migration. These findings suggest that some of the AGE-induced biological effects on the endothelium could be mediated, at least in part, by the weakening of intercellular contacts caused by decreases in the amount of VE-cadherin present.
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November 2001
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Research Article|
October 25 2001
Albumin-derived advanced glycation end-products trigger the disruption of the vascular endothelial cadherin complex in cultured human and murine endothelial cells Available to Purchase
Karel OTERO;
Karel OTERO
1
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
1To whom correspondence should be addressed, at: IRF ‘Mario Negri’, Via Eritrea 62, 20157 Milan, Italy (e-mail [email protected]).
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Fernando MARTÍNEZ;
Fernando MARTÍNEZ
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
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Amada BELTRÁN;
Amada BELTRÁN
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
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Deyarina GONZÁLEZ;
Deyarina GONZÁLEZ
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
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Beatriz HERRERA;
Beatriz HERRERA
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
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Gypsy QUINTERO;
Gypsy QUINTERO
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
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René DELGADO;
René DELGADO
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
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Armando ROJAS
Armando ROJAS
Laboratorio de Farmacología, Centro de Química Farmacéutica, Apartado Postal 6990, La Habana, Cuba
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Publisher: Portland Press Ltd
Received:
May 14 2001
Revision Received:
July 27 2001
Accepted:
August 24 2001
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2001
2001
Biochem J (2001) 359 (3): 567–574.
Article history
Received:
May 14 2001
Revision Received:
July 27 2001
Accepted:
August 24 2001
Citation
Karel OTERO, Fernando MARTÍNEZ, Amada BELTRÁN, Deyarina GONZÁLEZ, Beatriz HERRERA, Gypsy QUINTERO, René DELGADO, Armando ROJAS; Albumin-derived advanced glycation end-products trigger the disruption of the vascular endothelial cadherin complex in cultured human and murine endothelial cells. Biochem J 1 November 2001; 359 (3): 567–574. doi: https://doi.org/10.1042/bj3590567
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