Abstract
THE increased activity of pentose-shunt dehydrogenases, which had been demonstrated histochemically in cancers1, has been partly confirmed by biochemical investigations in carcinoma of the cervix in that the cells of the vaginal secretion gave high values for 6-phosphogluconate dehydrogenase2. Since this is said to be an oxidative pathway3, attempts were made to test if a concomitant rise in cytochrome oxidase activity could be demonstrated. This was done histochemically, to avoid dilution of active cancer tissue by inactive or necrotic tissue and by stroma. A more intense and permanent histochemical procedure for cytochrome oxidase4 was applied to sections from eight apparently normal cervices, three apparently normal endometria, ten primary carcinomata of the cervix and seven other carcinomata of the genital tract. The tissues were removed at operation and were frozen and sectioned by a controlled temperature freeze-sectioning method4,5. The cytochrome oxidase-levels were not elevated in the cancers; in some they seemed somewhat depressed.
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BUTCHER, R., CHAYEN, J. & LABRUM, A. Oxidation of L-Ascorbic Acid by Cells of Carcinoma of the Human Cervix. Nature 207, 992–993 (1965). https://doi.org/10.1038/207992a0
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DOI: https://doi.org/10.1038/207992a0
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