The role of bound lipid and transition metal in the formation of fluorescent advanced glycation endproducts by human serum albumin

Glycation is implicated in neurological disorders. In some cases it plays a key role in the pathogenesis, in others it plays a co-adjuvant role or it appears as a consequence of degenerative changes and protein accumulation stemming from other pathways. In this work, we attempt to provide a concise, updated review of the major recent findings concerning glycation in neurological diseases. After a short introduction covering advanced glycation endproducts (AGEs) and the receptor for AGEs (RAGE), we will discuss the impact of glycation in central nervous system disorders including Alzheimer's, Parkinson's and Creutzfeldt-Jakob disease, as well as peripheral diabetic polyneuropathies. Therapies directed at lowering the concentrations of RAGE ligands including AGEs, blocking RAGE signaling, preventing oxidative stress or lowering methylglyoxal (MGO) levels may significantly decrease the development of AGE-related pathologies in patients with neurological disorders. Many drugs are on the pipeline and the future clinical trials will reveal if the promising results translate into clinical application.

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Advanced glycation endproducts and their pathogenic roles in neurological disorders

Münch

et al. 2010

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Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease

Srikanth

Maczurek

Phan

et al. 2011

Neurobiology of Aging

442

285

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Tessier¹,

Birlouez‐Aragon²

1998

Glycoconjugate Journal

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Protein glycation is believed to play an important role in the development of long-term disorders associated with diabetes. Previous studies have shown that copper could activate this process; however, these experiments were performed under non-physiological conditions. In this study, in vitro experiments were carried out at near-physiological conditions to examine the catalytic activity of copper on the interaction of albumin with glucose. Changes in pH and phosphate buffering capacity were shown to affect albumin glycation. Under stable pH conditions, copper activates albumin glycation only at low protein concentrations (< 30 g l(-1)). Copper had no effect on albumin glycation at higher protein concentrations probably because the metal is chelated by the protein.

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The role of bound lipid and transition metal in the formation of fluorescent advanced glycation endproducts by human serum albumin

Cited by 4 publications

References 4 publications

Advanced glycation endproducts and their pathogenic roles in neurological disorders

Advanced glycation endproducts and their pathogenic roles in neurological disorders

Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease

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