Pathophysiology of advanced glycation end-products in renal failure

T. Miyata, Y. Iida, K. Horie, Z. Cai, S. Sugiyama, K. Maeda

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

β2-Microglobulin is a major constituent of amyloid fibrils in dialysis-related amyloidosis, a serious complication leading to bone and joint destruction in long-term haemodialysis patients. However, the molecular pathogenesis of this complication remains unknown. Intact β2-microglobulin per se seems an unlikely contributor to the pathogenesis, because no difference in the plasma levels of intact β2-microglobulin has yet been found between haemodialysis patients with and without this complication. Some investigators have therefore focused on the modification of this molecule. Recent studies have revealed a new modification of β2-microglobulin in amyloid fibrils-the advanced glycation end-products (AGEs) formed by a non-enzymatic reaction between sugar aldose and protein. Further studies have suggested that the interaction of AGE-modified β2-microglobulin with monocyte/macrophage and osteoclast/osteoblast gives a plausible albeit partial explanation for the mechanism of bone and joint destruction in dialysis-related amyloidosis. This article discusses the pathophysiology of AGEs in renal failure and the modification of β2-microglobulin with AGEs, especially focusing on their structure and pathological role in dialysis-related amyloidosis.

Original languageEnglish
Pages (from-to)27-30
Number of pages4
JournalNephrology Dialysis Transplantation
Volume11
Issue numberSUPPL. 5
DOIs
Publication statusPublished - 1996
Externally publishedYes

Keywords

  • AGEs
  • Pathophysiology
  • Renal failure
  • β-microglobulin

ASJC Scopus subject areas

  • Nephrology
  • Transplantation

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