1) Lung tumors induced in mice and rats with 4-nitroquinoline 1-oxide were examined histochemically for alkaline phosphatase, acid phosphatase, adenosine triphosphatase, glucose-6-phosphatase, 5-nucleotidase, non-specific esterase, cholinesterase, lipase, β-glucuronidase, leucine aminopeptidase, cytochrome oxidase, monoamine oxidase, succinic dehydrogenase, diphosphopyridine nucleotide (DPN) diaphorase, triphosphopyridine nucleotide (TPN) diaphorase, lactic dehydrogenase, glutamic dehydrogenase, malic dehydrogenase, ethanol dehydrogenase, and glucose 6-phosphate dehydrogenase, and in some of the animals the serum levels of leucine aminopeptidase and lactic dehydrogenase were also determined.
2) β-Glucuronidase, DPN-diaphorase, TPN-diaphorase, lactic dehydrogenase, and glucose 6-phosphate dehydrogenase activities were consistently higher in lung tumors of both animals than in normal lung tissues.
3) Leucine aminopeptidase activity in the tumor cells was seen only in the adenomas and adenocacinomas in both animals.
4) In mice, monoamine oxidase, glutamic dehydrogenase, and ethanol dehydrogenase activities were higher in tumors originating in the bronchioles than in tumors originating in the alveoli. They were also higher in the bronchioles than in the alveoli of normal lungs.
5) In rats, alkaline phosphatase and succinic dehydrogenase activities were higher in adenocarcinomas than in adenomas, and in mice, stromal alkaline phosphatase activity was seen only in adenocarcinomas.
6) In squamous cell carcinomas of rats enzymatic activity was lower than in adenomas and adenocarcinomas.
7) Leucine aminopeptidase and β-glucuronidase activities were localized to the stroma of the tumors, but the former was weaker than in human lung cancers,
8) The serum values of leucine aminopeptidase and lactic dehydrogenase in mice with lung tumors induced by 4-nitroquinoline 1-oxide were normal.
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