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Degradation of oxidized extracellular proteins by microglia

journal contribution
posted on 06.03.2015, 13:44 by Alexandra Stolzing, Antje Wengner, Tilman Grune
In living organisms a permanent oxidation of protein oxidation occurs. The degradation of intracellular oxidized proteins is intensively studied, but knowledge about the fate of oxidatively modified extracellular proteins is still limited. We studied the fate of exogenously added oxidized proteins in microglial cells. Both primary microglial cells and RAW cells are able to remove added oxidized laminin and myelin basic protein from the extracellular environment. Moderately oxidized proteins are degraded most efficiently, whereas strongly oxidized proteins are taken up by the microglial cells without an efficient degradation. Activation of microglial cells enhances the selective recognition and degradation of moderately oxidized protein substrates by proteases. Inhibitor studies also revealed an involvement of the lysosomal and the proteasomal system in the degradation of extracellular proteins. These studies let us conclude that microglial cells are able to remove oxidized proteins from the extracellular environment in the brain. © 2002 Elsevier Science (USA). All rights reserved.

Funding

This study was supported by the Deutsche Forschungsgemeinschaft (DFG Gr 1240/9-1).

History

School

  • Mechanical, Electrical and Manufacturing Engineering

Published in

Archives of Biochemistry and Biophysics

Volume

400

Issue

2

Pages

171 - 179

Citation

Stolzing, A., WENGNER, A. and GRUNE, T., 2002. Degradation of oxidized extracellular proteins by microglia. Archives of Biochemistry and Biophysics, 400 (2), pp. 171 - 179.

Publisher

© Elsevier Science

Version

VoR (Version of Record)

Publisher statement

This work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/

Publication date

2002

Notes

This article is closed access.

ISSN

0003-9861

Language

en

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