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Journal of Amino Acids
Volume 2011 (2011), Article ID 461216, 9 pages
http://dx.doi.org/10.4061/2011/461216
Review Article

Protein Modification by Dicarbonyl Molecular Species in Neurodegenerative Diseases

1Department of Biological Sciences, Case Western Reserve University, Cleveland, OH 44106, USA
2Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA

Received 3 November 2010; Accepted 10 January 2011

Academic Editor: Jackob Moskovitz

Copyright © 2011 Wesley M. Williams et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Neurodegeneration results from abnormalities in cerebral metabolism and energy balance within neurons, astrocytes, microglia, or microvascular endothelial cells of the blood-brain barrier. In Alzheimer's disease, 𝛽 -amyloid is considered the primary contributor to neuropathology and neurodegeneration. It now is believed that certain systemic diseases, such as diabetes mellitus, can contribute to neurodegeneration through the effects of chronic hyperglycemia/insulin resistance resulting in protein glycation, oxidative stress and inflammation within susceptible brain regions. Here, we present an overview of research focusing on the role of protein glycation, oxidative stress, and inflammation in the neurodegenerative process. Of special interest in this paper is the effect of methylglyoxal (MGO), a cytotoxic byproduct of glucose metabolism, elevated in neurodegenerative disease, and diabetes mellitus, on cerebral protein function and oxidative stress. How MGO interacts with amino acid residues within -amyloid, and small peptides within the brain, is also discussed in terms of the affect on protein function.