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Fröhlich, E; Schaumburg-Lever, G; Klessen, C.
Immunocytochemical and immunoelectron microscopic demonstration of cathepsin B in human malignant melanoma.
Br J Dermatol. 1995; 132(6): 867-875. Doi: 10.1111/j.1365-2133.1995.tb16941.x
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Leading authors Med Uni Graz: Fröhlich Eleonore
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Abstract:: Proteases are known to enhance the spread of tumour cells. Possible sources of these proteases are the tumour cells themselves or fibroblasts in the tumour tissue. Immunological staining with anticathepsin B antibody indicates that the subcellular distribution of cathepsin B in tumour cell lines differs from that in normal liver. The aims of this study were: (i) to show whether different types of melanoma differ in their production of cathepsin B; (ii) to identify the cathepsin B-producing cells; and (iii) to determine the subcellular distribution of cathepsin B in melanoma cells. All types of melanomas contained cell regions stained with anticathepsin B antibody. The intensity of the stain and the number of cells reacting with anticathepsin B antibody depended on the size of the tumour but not on the type of melanoma. Epithelioid cells stained more intensely with anticathepsin B antibody than spindle-shaped cells. Cells staining with anticathepsin B antibody were almost exclusively tumour cells. Anticathepsin B stain was located mainly in vesicular structures which did not contain a filamentous matrix. Additional anticathepsin B stain was detected at the extracellular spaces. Hypomelanotic melanoma cells, mainly of the epithelioid type, produced most of the cathepsin B. Cathepsin B may be involved in both the degradation of possibly abnormal melanosomes and the focal degradation of the extracellular matrix.
Find related publications in this database (using NLM MeSH Indexing): Cathepsin B - analysis; Humans - analysis; Immunohistochemistry - analysis; Melanoma - chemistry; Microscopy, Immunoelectron - chemistry; Neoplasm Proteins - analysis; Skin Neoplasms - chemistry