Neurotoxicity Research

, Volume 4, Issue 3, pp 191–209 | Cite as

Involvement of maillard reactions in Alzheimer disease

  • V. Prakash Reddy
  • Mark E. Obrenovich
  • Craig S. Atwood
  • George Perry
  • Mark A. Smith
Article

Abstract

Maillard reactions have been explored by food chemists for many years. It is only recently that the advanced glycation end products (AGEs), the end products of the Maillard reaction, have been detected in a wide variety of diseases such as diabetes, atherosclerosis, cataractogenesis, Parkinson disease and Alzheimer disease (AD). In this review, we discuss the chemistry and biochemistry of AGE-related crosslinks such as pyrraline, pentosidine, carboxymethyllysine (CML), crosslines, imidazolidinones, and dilysine crosslinks (GOLD and MOLD), as well as their possible involvement in neurodegenerative conditions. Pentosidine and CML are found in elevated amounts in the major lesions of the AD brain. Glycation is also implicated in the formation of the paired helical filaments (PHF), a component of the neurofibrillary tangles (NFTs). Amyloid-β peptide and proteins of the cerebrospinal fluid are also glycated in patients with AD. In order to ameliorate the effects of AGEs on AD pathology, various inhibitors of AGEs have been increasingly explored. It is hoped that understanding of the mechanism of the AGEs formation and their role in the neurodegeneration will result in vovel therapeutics for neuroprotection.

Keywords

Advanced glycation end products Alzheimer disease Amyloid-β Glycation Maillard reaction Neurodegeneration 

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Copyright information

© Springer 2002

Authors and Affiliations

  • V. Prakash Reddy
    • 1
  • Mark E. Obrenovich
    • 2
  • Craig S. Atwood
    • 2
  • George Perry
    • 2
  • Mark A. Smith
    • 2
  1. 1.Department of ChemistryUniversity of Missouri-RollaRollaUSA
  2. 2.Institute of PathologyCase Western Reserve UniversityClevelandUSA

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