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Histochemical Evaluation of Enzymatic Activities in Human Squamous-Cell Cancer

( Department of Oral Surgery, Osaka University Dental School, Osaka, Japan)

Human squamous-cell cancer was studied histochemically for alkaline phosphatase, acid phosphatase, esterase, ß-glucuronidase, aminopeptidase, and various dehydrogenases.

Alkaline phosphatase activity was confined to the stromal elements, and there was usually a loss of activity in the malignant epithelium. Acid phosphatase activity was localized in the neoplastic epithelium and was particularly marked in the highly keratinized portion of central foci in epidermoid cancer. Esterase activity was considerably higher in neoplastic epithelial cells than in normal epithelial cells. It was high in the parakeratotic areas of epidermoid cancer and in the necrotic portion of squamous-cell cancer. ß-Glucuronidase activity in the neoplastic epithelium was similar to that of the homologous epithelium. Aminopeptidase activity was generally decreased in the tumor parenchyma, but in basal-cell carcinoma or anaplastic carcinoma the activity of this enzyme was present in the neoplastic cells. Aminopeptidase activity was occasionally present in the stromal elements, and its distribution was similar to that of alkaline phosphatase. Succinic dehydrogenase activity was localized in the peripheral cell layer and adjacent cells of epidermoid cancer and was found in most cells of basal cell cancers; however, the highly keratinized portion and necrotic areas showed a loss of this activity. Lactic, malic, glycerophosphate, glucose-6-phosphate, and isocitrate dehydrogenase were found to be similarly localized in the peripheral layer to the subhornified layer of squamous-cell cancer.

Received 9/13/62.