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      Formation of Amyloid-Like Substance from Beta-2-Microglobulin in vitro

      a , b

      Nephron

      S. Karger AG

      β2-Microglobulin, Amyloid, Glycosaminoglycan, Amyloid P component, serum

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          Abstract

          Although the pathogenesis has yet to be fully understood, β<sub>2</sub>-microglobulin (β<sub>2</sub>m) related amyloidosis is a frequent complication in long-term hemodialysis (HD) patients. In an attempt to clarify the association of two potential candidates with amyloidogenesis from β<sub>2</sub>m in HD patients, human urine-derived β<sub>2</sub>m solution alone or combined with glycosaminoglycans: hyaluronic acid, heparan sulfate, or serum amyloid P component (SAP) were dialyzed against physiological buffered solution (pH 7.4) using a microdialyzer in vitro for 72 h at 4°C. This study demonstrates for the first time that SAP can play a crucial role in the formation of amyloid-like fibrils from β<sub>2</sub>m. This occurs by a direct influence on either the processing of a precursor protein, or protein folding, in vitro, by a short-period dialysis against a physiological buffered solution.

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          Author and article information

          Journal
          NEF
          Nephron
          10.1159/issn.1660-8151
          Nephron
          S. Karger AG
          1660-8151
          2235-3186
          1994
          1994
          16 December 2008
          : 66
          : 4
          : 404-407
          Affiliations
          aOno Geka Clinic, Fukuoka, and bFirst Department of Pathology, Yamaguchi University School of Medicine, Ube, Japan
          Article
          187854 Nephron 1994;66:404–407
          10.1159/000187854
          8015642
          © 1994 S. Karger AG, Basel

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          Page count
          Pages: 4
          Categories
          Original Paper

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