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pubmed-article:2470544pubmed:abstractText1. 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.lld:pubmed
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pubmed-article:2470544pubmed:dateRevised2004-11-17lld:pubmed
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pubmed-article:2470544pubmed:year1989lld:pubmed
pubmed-article:2470544pubmed:articleTitleHigh-molecular-mass proteins in haemodialysis-associated amyloidosis.lld:pubmed
pubmed-article:2470544pubmed:affiliationINSERM Unit 249, Centre de Recherche Biochimie Macromoléculaire, CNRS, Montpellier, France.lld:pubmed
pubmed-article:2470544pubmed:publicationTypeJournal Articlelld:pubmed