Pathogenesis of dialysis-related amyloidosis

T. Miyata, K. Maeda

Research output: Contribution to journalReview articlepeer-review

14 Citations (Scopus)

Abstract

Beta2-microglobulin has been demonstrated to be a major constituent of amyloid fibrils in dialysis-related amyloidosis. However, the molecular pathogenesis of this complication remains unknown. Several lines of evidence suggest that β2-microglobulin is not an innocent bystander, but plays an active role in the development of dialysis-related amyloidosis. The evidence remains inconclusive, however, as to whether it is intact or modified β2-microglobulin which is amyloidogenic and contributes to bone and joint destruction. Recent biochemical and immunohistological studies have revealed a new modification of β2-microglobulin in amyloid fibrils, the advanced glycation end products formed nonenzymatically between aldoses and proteins. Further study has suggested that the interaction of advanced glycation end product-modified β2-microglobulin with monocytes/macrophages gives a plausible, albeit incomplete, explanation for the mechanism of bone and joint destruction in dialysis-related amyloidosis. This review focuses on new aspects of the pathogenesis of dialysis-related amyloidosis.

Original languageEnglish
Pages (from-to)493-497
Number of pages5
JournalCurrent Opinion in Nephrology and Hypertension
Volume4
Issue number6
DOIs
Publication statusPublished - 1995 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Internal Medicine
  • Nephrology

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