An immunohistochemical study of cytokeratins in skin-limited amyloidosis

The frequency of amyloid deposits in cases of seborrheic keratosis was investigated. In addition, the origin of amyloid protein(s) in lichen amyloidosis, macular amyloidosis and seborrheic keratosis was studied by immunohistochemical staining using a panel of anti-cytokeratin (CK) monoclonal antibodies. Amyloid deposits were found in 41 of 327 specimens (12.5%) from 301 cases of seborrheic keratosis. Amyloid deposits in seborrheic keratosis reacted with 6 of 12 CK antibodies and in lichen and macular amyloidosis (20 specimens) reacted with 5 of 12 CK antibodies. In seborrheic keratosis, antibody DE-K10 (labeling CK10) reacted with amyloid in 17 of 36 cases, antibody 34 beta E12 (labeling CK1, 5, 10, 14) reacted in 33 of 39 cases, and antibody MNF116 (labeling CK5, 6, 8, 17) reacted in 32 of 35 cases. Among 20 specimens from lichen and macular amyloidosis, the three antibodies reacted with amyloid in the following rates: 1 with antibody DE-K10, all 20 with antibody 34 beta E12, and 6 with antibody MNF116. These results suggest that amyloid deposits in seborrheic keratosis and lichen and macular amyloidosis may derive from epidermal cytokeratins.