Identification of AGE-modified proteins in SH-SY5Y and OLN-93 cells.
The formation of "Advanced Glycation End products" (AGEs) is an inevitable consequence of mammalian glucose metabolism. AGE-mediated protein-protein crosslinks lead to detergent-insoluble and protease-resistant protein aggregates, and in Alzheimer's disease (AD) extra cellular senile plaques (SPs) and intracellular neurofibrillary tangles (NFTs) have been shown to contain AGEs. However, to date little is known concerning the most prevalent protein-targets of AGE modification under normal, non-pathological conditions. Here, a combination of 2D-electrophoresis, Western blotting and mass spectrometry has been used to identify preferentially AGE-modified proteins in oligodendrocyte (OLN-93) and neuroblastoma cell lines (SH-SY5Y) in standard culture. Proteomics analysis identified a total of eight targets with structural, metabolic and regulatory function, three of which (beta-actin, beta-tubulin and eukaryotic Elongation Factor 1-alpha) were common to both cell lines. Based on results from prior studies, modification of these proteins may lead to a loss of function. Consequently, the identification of targets for these proteins is of particular interest for a better understanding of the consequences of AGE-modification in aging, neurodegenerative diseases and diabetes.
Langer
André K
AK
Nachwuchsgruppe 1, Interdisciplinary Centre of Clinical Research (IZKF), University of Leipzig, 04103 Leipzig, Germany. Andre.Langer@web.de
Poon
H Fai
HF
Münch
Gerald
G
Lynn
Bert C
BC
Arendt
Thomas
T
Butterfield
D Allan
DA
D000818:Animals; D045744:Cell Line, Tumor; D002682:Chinchilla; D017127:Glycation End Products, Advanced / Q000032:analysis* / Q000096:biosynthesis*; D006801:Humans; D009836:Oligodendroglia / Q000737:chemistry* / Q000378:metabolism; D011817:Rabbits; D051381:Rats
D017127:Glycation End Products, Advanced