New aspects in the pathogenesis of dialysis-related amyloidosis: Pathophysiology of advanced glycation end products in renal failure

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6 Citations (Scopus)

Abstract

It has been demonstrated that 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 hemodialysis patients. However, the molecular pathogenesis of this complication remains unknown. Several lines of evidence suggest that β2-microglobulin plays an active role in the development of dialysis-related amyloidosis. It is unlikely that intact β2-microglobulin per se contributes to the pathogenesis, because no difference in the plasma levels of intact β2-microglobulin has yet been found between hemodialysis patients with and without this complication. Some investigators, therefore, have focused on the modification of this molecule. Recent studies have revealed a new modification of β2-microglobulin in amyloid fibrils: advanced glycation end products (AGEs) formed by a non-enzymatic reaction between aldoses and proteins. 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 focuses on the modification of β2-microglobulin with AGEs, especially on their structure and pathological role in dialysis-related amyloidosis. Furthermore, the implication of renal failure in the pathophysiology of AGEs is also discussed.

Original languageEnglish
Pages (from-to)191-197
Number of pages7
JournalJapanese Journal of Nephrology
Volume38
Issue number5
Publication statusPublished - 1996 Dec 1
Externally publishedYes

Keywords

  • Advanced glycation end products
  • Dialysis-related amyloidosis
  • Glycoxidation
  • Redox imbalance
  • β2-microglobulin

ASJC Scopus subject areas

  • Nephrology

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