Role of methylglyoxal in Alzheimer's disease

Biomed Res Int. 2014:2014:238485. doi: 10.1155/2014/238485. Epub 2014 Mar 9.

Abstract

Alzheimer's disease is the most common and lethal neurodegenerative disorder. The major hallmarks of Alzheimer's disease are extracellular aggregation of amyloid β peptides and, the presence of intracellular neurofibrillary tangles formed by precipitation/aggregation of hyperphosphorylated tau protein. The etiology of Alzheimer's disease is multifactorial and a full understanding of its pathogenesis remains elusive. Some years ago, it has been suggested that glycation may contribute to both extensive protein cross-linking and oxidative stress in Alzheimer's disease. Glycation is an endogenous process that leads to the production of a class of compounds known as advanced glycation end products (AGEs). Interestingly, increased levels of AGEs have been observed in brains of Alzheimer's disease patients. Methylglyoxal, a reactive intermediate of cellular metabolism, is the most potent precursor of AGEs and is strictly correlated with an increase of oxidative stress in Alzheimer's disease. Many studies are showing that methylglyoxal and methylglyoxal-derived AGEs play a key role in the etiopathogenesis of Alzheimer's disease.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alzheimer Disease / metabolism*
  • Amyloid beta-Peptides / metabolism
  • Animals
  • Antioxidants / metabolism
  • Glycation End Products, Advanced / metabolism
  • Glycogen Synthase Kinase 3 / metabolism
  • Glycogen Synthase Kinase 3 beta
  • Humans
  • Oxidation-Reduction
  • Oxidative Stress
  • PC12 Cells
  • Phosphorylation
  • Pyruvaldehyde / metabolism*
  • Rats
  • Risk Factors
  • p38 Mitogen-Activated Protein Kinases / metabolism
  • tau Proteins / metabolism

Substances

  • Amyloid beta-Peptides
  • Antioxidants
  • Glycation End Products, Advanced
  • tau Proteins
  • Pyruvaldehyde
  • Glycogen Synthase Kinase 3 beta
  • p38 Mitogen-Activated Protein Kinases
  • Glycogen Synthase Kinase 3