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Ubiquitinated cytokeratin inclusions in lichen amyloidosus: An immunohistochemical analysis
Author(s) -
Akamatsu Mayumi,
Hori Sadaaki,
Tsutsumi Yutaka,
Osamura R. Yoshiyuki,
Ohkido Muneo
Publication year - 1995
Publication title -
pathology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
eISSN - 1440-1827
pISSN - 1320-5463
DOI - 10.1111/j.1440-1827.1995.tb03431.x
Subject(s) - cytokeratin , pathology , immunoelectron microscopy , biology , immunohistochemistry , intermediate filament , ubiquitin , antibody , desmosome , staining , chemistry , microbiology and biotechnology , cytoskeleton , cell , immunology , biochemistry , medicine , gene
Eosinophilic hyaline inclusions were consistently seen in the perinuclear cytoplasm of suprabasal keratinocytes in lichen amyiddosus. The inclusions, negative with amylold staining, were immunoreective for ubiquitin and cytokeratin, and uitrastructuraliy showed aggregations of fine filaments of two size (central thin and peripheral thick). The thin filaments were the main component in the upper epidermal layer. Four monoclonal antibodies (AE1, AE3, KL1 and CAM5.2) and om antiserum (WSS) were used for characterizing cytokeratin expression. The AE1 antibody normally stained the basal cells, but in lichen amyloidosus basal staining mostly disappeared. Instead, groups of suprabasal keratrnocytss were labeled, with AE1 ‐reactive inclusions disfributed therein. In contrast, the KL1 antibody, showing suprabasal staining, failed to react with the inclusions. The includms were weakly reactive with the AE3 and WSS antibodies, which stained all keratinocytes. The CAM5.2 antibody was unreactive. The subepidermal amyloid deposits were negative with all the antibodies. The inclusions were ubiquitinated especialty in the granular layer. Immuno‐electron microscopy disclosed that ubiquitin was more denseiy localized in the thin filaments than in the thick ones. This indicated that cytokeratin expression and metabolism are altered in the affected epidermis, and that ubiquitin functions in the process of degradation of abnormal cytokeratin filaments.