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      Electron-Microscopic and Inimunohistochemical Study of Beta-2-Microglobulin-Related Amyloidosis

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          Abstract

          β<sub>2</sub>-Microglobulin (β<sub>2</sub>-MG)-related amyloidosis has been reported as a complication in long-term hemodialysis patients. We observed β<sub>2</sub>-MG amyloid deposits in synovial sheaths, bone cysts and gastric mucosa. They showed unique ultrastructural features, that is bundles or nodules consisting of curved or linear amyloid fibrils, associated with various cell reactions. The electron-microscopic histochemical study showed that they strongly stained with periodic acid-silver methenamine stain. A similar phenomenon was noticed in the spicules or bundles of amyloid fibrils in primary and secondary renal amyloidosis. With the cationic reagent toluidine blue 0, proteoglycanlike structures were observed around amyloid bundles and nodules, but not on each fibrils. Based on these results, we postulate that there is a close relationship between ultrastructural features and histochemical characteristics in β<sub>2</sub>-MG amyloid fibrils.

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          Author and article information

          Journal
          NEF
          Nephron
          10.1159/issn.1660-8151
          Nephron
          S. Karger AG
          1660-8151
          2235-3186
          1990
          1990
          10 December 2008
          : 56
          : 4
          : 357-363
          Affiliations
          aDepartment of Medicine II, Niigata University Medical School and bDivision of Pathology, Shinrakuen Hospital, Niigata, Japan
          Article
          186175 Nephron 1990;56:357–363
          10.1159/000186175
          1706823
          © 1990 S. Karger AG, Basel

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          Page count
          Pages: 7
          Categories
          Original Paper

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