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Degradation of glycated bovine serum albumin in microglial cells
journal contribution
posted on 2015-03-04, 12:22 authored by Alexandra StolzingAlexandra Stolzing, Rebecca Widmer, Tobias Jung, Peter Voss, Tilman GruneGlycated protein products are formed upon binding of sugars to lysine and arginine residues and have been shown to accumulate during aging and in pathologies such as Alzheimer disease and diabetes. Often these glycated proteins are transformed into advanced glycation end products (AGEs) by a series of intramolecular rearrangements. In the study presented here we tested the ability of microglial cells to degrade BSA-AGE formed by glycation reactions of bovine serum albumin (BSA) with glucose and fructose. Microglial cells are able to degrade BSA-AGEs to a certain degree by proteasomal and lysosomal pathways. However, the proteasome and lysosomal proteases are severely inhibited by cross-linked BSA-AGEs. BSA-AGEs are furthermore able to activate microglial cells. This activation is accompanied by an enhanced degradation of BSA-AGE. Therefore, we conclude that microglial cells are able to degrade glycated proteins, although cross-linked protein-AGEs have an inhibitory effect on proteolytic systems in microglial cells. © 2005 Elsevier Inc. All rights reserved.
Funding
The work of T.G. was supported by DFG, GK 1033 and SFB575
History
School
- Mechanical, Electrical and Manufacturing Engineering
Published in
Free Radical Biology and MedicineVolume
40Issue
6Pages
1017 - 1027Citation
STOLZING, A. ... et al., 2006. Degradation of glycated bovine serum albumin in microglial cells. Free Radical Biology and Medicine, 40 (6), pp. 1017 - 1027.Publisher
© Elsevier IncVersion
- 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
2006Notes
Closed accessISSN
0891-5849Publisher version
Other identifier
S0891584905006659Language
- en