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- W2008337653 abstract "Chronic inflammation is known to play an important role in the heterogeneous pathogenesis of Alzheimer's disease (AD). Activated astrocytes expressing glial fibrillary acidic protein (GFAP) are closely associated with AD pathology, such as tangles, neuritic plaques and amyloid depositions. Altogether, 46 soluble isoforms of GFAP were separated and most of them quantified by two-dimensional immunoblotting in frontal cortices of AD patients and age-matched controls. A 60% increase in the amount of more acidic isoforms of GFAP was observed in AD and these isoforms were both phosphorylated and N-glycosylated, while more basic isoforms were O-glycosylated and exhibited no quantitative differences between post-mortem AD and control brains. These data highlight the importance of exploring isoform-specific levels of proteins in pathophysiological conditions since modifications of proteins determine their activity state, localization, turnover and interaction with other molecules. Mechanisms, structures and functional consequences of modification of GFAP isoforms remain to be clarified." @default.
- W2008337653 created "2016-06-24" @default.
- W2008337653 creator A5024592413 @default.
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- W2008337653 creator A5089275240 @default.
- W2008337653 creator A5091784289 @default.
- W2008337653 date "2005-12-01" @default.
- W2008337653 modified "2023-10-12" @default.
- W2008337653 title "Proteomic analysis of glial fibrillary acidic protein in Alzheimer's disease and aging brain" @default.
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