Glycation and physiological mechanisms of its prevention in Alzheimer's disease

Abstract

Alzheimer's disease (AD) is a multifactorial disease that involves progressive synaptic loss and neuronal death. This neurodegeneration has been linked to the presence of extracellular plaques of amyloid beta (Aβ) peptide and to the occurrence of intracellular deposits (tangles) that are composed predominantly of microtubule-associated-protein tau (MAP-tau). It is noteworthy that the proteins in these deposits are frequently modified by Advanced Glycation Endproducts (AGEs). AGEs are found in many aging and pathological tissues but are particularly prevalent in AD. Evidence suggests that AGE-crosslinked aggregates may contribute to the pathophysiology of AD by a variety of mechanisms.