Immunocytochemical identification of amyloid in formalin-fixed paraffin sections |
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Authors: | T. Shirahama M. Skinner A. S. Cohen |
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Affiliation: | (1) The Arthritis Center of Boston University, Boston City Hospital, Boston, Massachusetts, USA;(2) the Arthritis and Connective Tissue Disease Section, Boston City Hospital, Boston, Massachusetts, USA;(3) the Thorndike Memorial Laboratory and Division of Medicine, Boston City Hospital, Boston, Massachusetts, USA;(4) the Evans Memorial Department of Clinical Research, University Hospital, Boston, Massachusetts, USA;(5) the Department of Medicine, Boston University School of Medicine, Boston, Massachusetts, USA |
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Abstract: | Summary Formalin-fixed paraffin sections of livers, spleens and kidneys from patients with primary, secondary and familial amyloidosis as well as from a casein-induced murine amyloid model were analysed by an immunocy-tochemical (unlabeled antibody enzyme) method utilizing antisera to amyloid-related proteins. All amyloid deposits of all amyloid types showed positive reactions with anti-AP of the respective species. Positive reaction of anti-human AA to human secondary amyloid deposits and of anti-mouse AA to the deposits of casein-induced murine amyloid was also observed, but there was no species cross reactivity. No significant deposition of the reaction products was produced by anti-immunoglobulin light chains on deposits of any amyloid type, or by anti-AA in the tissues from primary or familial amyloidosis. The results indicate that amyloid proteins AA and AP can survive as antigens through routine histologic preparation, that anti-AP can be a universal marker for deposits of any amyloid type within the same species, and that AA-type amyloid can be identified by this method while there may as yet be no feasible universal marker for the AL-type at present.Presented in part at the 64th Annual Meeting of the Federation of American Societies for Experimental Biology, Anaheim, California, April, 1980 |
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