Kidney and Metabolic Bone Diseases Vol.14 No.1(5)

Theme Dialysis -- related amyloidosis -- update
Title Advanced glycation on proteins and clinical profile of dialysis related amyloidosis
Publish Date 2001/01
Author Yoshihiro Motomiya Suiyukai Clinic
Author Hisahiko Iwamoto R&D for Diagnostics, A&T Corporation
Author Haruyoshi Yoshida Department of Clinical Laboraroty, Faculty of Medicine, Kagoshima University
[ Summary ] It has been no less than 15 years since an essential involvement of beta2-m in dialysis related amyloidosis (DRA) was reported. However, the details of neither pathomechanism nor monitoring markers, for DRA, are yet understood. However, in relation to both of these factors advanced glycation of proteins is considered to be the most important. Advanced glycation end products (AGEs) are formed in vivo, via Maillard reaction and/or non-Maillard reactions, but the latter process is most dominant in clinical dialysis settings. Car boxymethylation of lysine residue on proteins is one of the typical modifications in that process. No links between AGEs, including carboxymethyllysine with amyloidogenesis have so far been found, though current investigations are providing new links to the in volvement of AGEs in other Amyloid diseases, such as Alzheimer disease and AA amyloidosis.
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