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Journal of Biochemistry Advance Access published online on October 11, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn137
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© 2008 The Japanese Biochemical Society

Internalization of The Receptor for Advanced Glycation end Products (Rage) is Required to Mediate Intracellular Responses

Natalia Sevillano1, María D. Girón1, Mercedes Salido2, Alberto M. Vargas1, José Vilches2 and Rafael Salto1

1Department of Biochemistry and Molecular Biology II, School of Pharmacy, University of Granada. Campus de Cartuja sn, E-18071 Granada, Spain.
2Department of Histology. School of Medicine. University of Cádiz. Confocal Microscopy and Cell Culture Unit. Central Research Services in Health Sciences. Edificio Policlínico. C/ Dr Marañon 3, E-11002 Cádiz, Spain.

Corresponding author: R. Salto. Phone: (34)-958-246363. Fax: (34)-958-248960. E-mail address: rsalto{at}ugr.es

Received September 25, 2008; Accepted October 6, 2008


  Abstract

To dissect the rat receptor for advanced glycation end products (RAGE) subcellular distribution and trafficking in eukaryotic cells, an expression system coding for a fusion protein between the RAGE and an Enhanced Green Fluorescent Protein (EGFP) has been used. The RAGE-EGFP protein is expressed at the plasma membrane of CHO-k1 and Neuro-2a (N2a) cells and retains the capacity to bind Texas Red-labeled advanced glycation end products (AGEs). AGEs addition to the cell cultures induced a change in the subcellular distribution of the fluorescent RAGE-EGFP protein compatible with an internalization of the AGEs-RAGE complex. Furthermore, while N2a cells expressing the RAGE-EGFP showed an increase in ERK1/2 phosphorylation and NF-{kappa}B DNA binding in response to AGEs, preincubation with dansyl-cadaverine or phenylarsine oxide, inhibitors of receptors internalization, blocked the activation of ERKs and other intracellular responses mediated by AGEs. These results suggest that internalization plays a key role in the signal transduction mediated by RAGE.

Key Words: Enhanced green fluorescent protein, ERK1/2, NF-{kappa}B, Receptor for advanced glycation end products, Receptor internalization


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