HISTOCHEMICAL AND IMMUNOHISTOCHEMICAL CHARACTERIZATION OF AMYLOID ASSOCIATED WITH CHRONIC-HEMODIALYSIS AS BETA-2-MICROGLOBULIN

  • 1 January 1985
    • journal article
    • research article
    • Vol. 53  (6) , 705-709
Abstract
The carpal tunnel syndrome has been associated with amyloid deposits and is now regarded as a major complication in patients undergoing chronic hemodialysis. The hemodialysis-associated amyloidosis appears to have systemic rather than local involvement, although its full extent is yet to be determined. In an attempt to examine the chemical and immunologic nature of the amyloid, the authors carried out a series of histochemical and immunohistochemical studies with the following results. The amyloid was "sensitive" to the "permanganate treatment", suggesting it was the AA (secondary) type. On immunohistochemistry, however, anti-human AA did not give positive reaction with the amyloid deposits, suggesting that this would be a new form of amyloid. As reported elsewhere, the author''s preliminary results on the amino acid sequence analysis in one specimen have revealed homology of its amino terminal sequence to .beta.2-microglobulin. In the present study, anti-.beta.2-microglobulin did indeed react positively (with appropriate controls) with the amyloid deposits in the tissues collected from five different patients, confirming the .beta.2-microglobulin-related nature of the amyloid. The present observations are significant in two points: (a) they confirm that hemodialysis-associated amyloid is of .beta.2-microglobulin origin since it shares same antigenic determinant(s) with it and since the amino acid sequence is homologous; and (b) it adds what many have suspected, i.e., "permanganate-sensitive" amyloid is not specific for the AA type but includes AA and .beta.2-microglobulin amyloid deposits at the minimum.