High-molecular-mass proteins in haemodialysis-associated amyloidosis

Clin Sci (Lond). 1989 May;76(5):547-52. doi: 10.1042/cs0760547.

Abstract

1. Protein constituents were determined in eight amyloid deposits from eight patients (five male and three female), 53 +/- 4 years of age, treated by haemodialysis for 9-20 years using only cuprophane membranes and operated for carpal tunnel syndrome. 2. Soluble proteins were removed by solubilization in phosphate-buffered saline after osmotic lysis. The proteins of the insoluble fibrils were characterized by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and two-dimensional gel electrophoresis, and immunologically identified by Western blotting. 3. In addition to beta 2-microglobulin, alpha 2-macroglobulin was identified in the fibrillar material. The presence of these two proteins in amyloid deposits was confirmed by immunofluorescent microscopic studies. 4. Our data confirm the presence of beta 2-microglobulin in haemodialysis-associated amyloidosis, and also suggest a possible role for alpha 2-microglobulin: it may protect beta 2-microglobulin from proteolytic digestion, leading to its accumulation in intact form and to amyloid fibril formation.

MeSH terms

  • Amyloid / analysis*
  • Amyloidosis / etiology
  • Amyloidosis / metabolism*
  • Blotting, Western
  • Carpal Tunnel Syndrome / etiology
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Middle Aged
  • Molecular Weight
  • Proteins / analysis*
  • Renal Dialysis / adverse effects*
  • alpha-Macroglobulins / analysis
  • beta 2-Microglobulin / analysis

Substances

  • Amyloid
  • Proteins
  • alpha-Macroglobulins
  • beta 2-Microglobulin