Shinji Taneda

TL;DR: In this article, the authors present evidence that the characteristic pathological structures associated with Alzheimer disease contain modifications typical of advanced Maillard reaction end products, which are initiated by the condensation between amino groups of proteins and reducing sugars.

TL;DR: Evidence is presented that the seminal features of Alzheimer’s disease, including amyloid-P deposition, neurofibrillary tangle formation, degeneration of specific neuronal populations, and the persistence of the pathological lesions in vivo and their relative insolubility in vitro may all be related to specific oxidative stress-type mechanisms.

TL;DR: This ELISA provides a new tool for assessing the role of the advanced Maillard reaction in aging and age-related diseases and pentosidine values in digested human plasma correlating with those measured by HPLC.

TL;DR: The LG-derived protein-bound pyrrole may be a useful marker of oxidative lipid damage, and an immunoassay for this post-translational protein modification can be exploited as a mild, sensitive method for detecting and quantifying the generation of LGs in chronic inflammatory states.