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Degradation of oxidized extracellular proteins by microglia
journal contribution
posted on 2015-03-06, 13:44 authored by Alexandra StolzingAlexandra Stolzing, Antje Wengner, Tilman GruneIn 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 BiophysicsVolume
400Issue
2Pages
171 - 179Citation
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 ScienceVersion
- 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
2002Notes
This article is closed access.ISSN
0003-9861Publisher version
Language
- en