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Title: Degradation of glycated bovine serum albumin in microglial cells
Authors: Stolzing, Alexandra
Widmer, Rebecca
Jung, Tobias
Voss, Peter
Grune, Tilman
Keywords: Advanced glycation end products
Free radicals
Primary microglia
Issue Date: 2006
Publisher: © Elsevier Inc
Citation: STOLZING, A. ... et al., 2006. Degradation of glycated bovine serum albumin in microglial cells. Free Radical Biology and Medicine, 40 (6), pp. 1017 - 1027.
Abstract: Glycated 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.
Description: Closed access
Sponsor: The work of T.G. was supported by DFG, GK 1033 and SFB575
Version: Published
DOI: 10.1016/j.freeradbiomed.2005.10.061
URI: https://dspace.lboro.ac.uk/2134/16872
Publisher Link: http://dx.doi.org/10.1016/j.freeradbiomed.2005.10.061
ISSN: 0891-5849
Appears in Collections:Closed Access (Mechanical, Electrical and Manufacturing Engineering)

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