Abstract
Mice bearing the Lewis lung carcinoma showed a high tumour glutaminase activity and significantly higher concentrations of most amino acids than in both the liver and the skeletal muscle of the host. Tumour tissue slices showed a marked preference for glutamine, especially for oxidation of its skeleton to CO2. It is proposed that the metabolism of this particular carcinoma is focused on amino acid degradation, glutamine being its preferred substrate.
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- Abou-Khalil W. H., Yunis A. A., Abou-Khalil S. Prominent glutamine oxidation activity in mitochondria of hematopoietic tumors. Cancer Res. 1983 May;43(5):1990–1993. [PubMed] [Google Scholar]
- Arola L., Palou A., Remesar X., Alemany M. Adenylate deaminase activity in the rat. Effect of 24 hours of fasting. Horm Metab Res. 1981 May;13(5):264–266. doi: 10.1055/s-2007-1019240. [DOI] [PubMed] [Google Scholar]
- Arola L., Palou A., Remesar X., Alemany M. Glutamine synthetase activity in the organs of fed and 24-hours fasted rats. Horm Metab Res. 1981 Apr;13(4):199–202. doi: 10.1055/s-2007-1019220. [DOI] [PubMed] [Google Scholar]
- Carrascosa J. M., Martínez P., Núez de Castro I. Nitrogen movement between host and tumor in mice inoculated with Ehrlich ascitic tumor cells. Cancer Res. 1984 Sep;44(9):3831–3835. [PubMed] [Google Scholar]
- Clark C. M., Goodlad G. A. Depletion of proteins of phasic and tonic muscles in tumour-bearing rats. Eur J Cancer. 1971 Feb;7(1):3–9. doi: 10.1016/0014-2964(71)90088-0. [DOI] [PubMed] [Google Scholar]
- Curthoys N. P., Lowry O. H. The distribution of glutaminase isoenzymes in the various structures of the nephron in normal, acidotic, and alkalotic rat kidney. J Biol Chem. 1973 Jan 10;248(1):162–168. [PubMed] [Google Scholar]
- Demetrakopoulos G. E., Linn B., Amos H. Rapid loss of ATP by tumor cells deprived of glucose: contrast to normal cells. Biochem Biophys Res Commun. 1978 Jun 14;82(3):787–794. doi: 10.1016/0006-291x(78)90851-3. [DOI] [PubMed] [Google Scholar]
- FAWCETT J. K., SCOTT J. E. A rapid and precise method for the determination of urea. J Clin Pathol. 1960 Mar;13:156–159. doi: 10.1136/jcp.13.2.156. [DOI] [PMC free article] [PubMed] [Google Scholar]
- FOLCH J., LEES M., SLOANE STANLEY G. H. A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem. 1957 May;226(1):497–509. [PubMed] [Google Scholar]
- HUGGETT A. S., NIXON D. A. Use of glucose oxidase, peroxidase, and O-dianisidine in determination of blood and urinary glucose. Lancet. 1957 Aug 24;273(6991):368–370. doi: 10.1016/s0140-6736(57)92595-3. [DOI] [PubMed] [Google Scholar]
- Hellmann K., Burrage K. Control of malignant metastases by ICRF l59. Nature. 1969 Oct 18;224(5216):273–275. doi: 10.1038/224273a0. [DOI] [PubMed] [Google Scholar]
- Henry N., van Lamsweerde A. L., Vaes G. Collagen degradation by metastatic variants of Lewis lung carcinoma: cooperation between tumor cells and macrophages. Cancer Res. 1983 Nov;43(11):5321–5327. [PubMed] [Google Scholar]
- Kovacevic Z., McGivan J. D. Mitochondrial metabolism of glutamine and glutamate and its physiological significance. Physiol Rev. 1983 Apr;63(2):547–605. doi: 10.1152/physrev.1983.63.2.547. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Landel A. M., Hammond W. G., Meguid M. M. Aspects of amino acid and protein metabolism in cancer-bearing states. Cancer. 1985 Jan 1;55(1 Suppl):230–237. doi: 10.1002/1097-0142(19850101)55:1+<230::aid-cncr2820551305>3.0.co;2-i. [DOI] [PubMed] [Google Scholar]
- Lazo P. A. Amino acids and glucose utilization by different metabolic pathways in ascites-tumour cells. Eur J Biochem. 1981 Jun;117(1):19–25. doi: 10.1111/j.1432-1033.1981.tb06297.x. [DOI] [PubMed] [Google Scholar]
- Levin L., Gevers W. Metabolic alterations in cancer. Part I. Carbohydrate metabolism. S Afr Med J. 1981 Apr 4;59(15):518–521. [PubMed] [Google Scholar]
- Linder-Horowitz M., Knox W. E., Morris H. P. Glutaminase activities and growth rates of rat hepatomas. Cancer Res. 1969 Jun;29(6):1195–1199. [PubMed] [Google Scholar]
- Lippman M. M., Laster W. R., Abbott B. J., Venditti J., Baratta M. Antitumor activity of macromomycin B (NSC 170105) against murine leukemias, melanoma, and lung carcinoma. Cancer Res. 1975 Apr;35(4):939–945. [PubMed] [Google Scholar]
- Lundholm K., Bylund A. C., Holm J., Scherstén T. Skeletal muscle metabolism in patients with malignant tumor. Eur J Cancer. 1976 Jun;12(6):465–473. doi: 10.1016/0014-2964(76)90036-0. [DOI] [PubMed] [Google Scholar]
- Lundholm K., Edström S., Ekman L., Karlberg I., Bylund A. C., Scherstén T. A comparative study of the influence of malignant tumor on host metabolism in mice and man: evaluation of an experimental model. Cancer. 1978 Aug;42(2):453–461. doi: 10.1002/1097-0142(197808)42:2<453::aid-cncr2820420212>3.0.co;2-t. [DOI] [PubMed] [Google Scholar]
- MIDER G. B. Some aspects of nitrogen and energy metabolism in cancerous subjects: a review. Cancer Res. 1951 Nov;11(11):821–829. [PubMed] [Google Scholar]
- Moreadith R. W., Lehninger A. L. The pathways of glutamate and glutamine oxidation by tumor cell mitochondria. Role of mitochondrial NAD(P)+-dependent malic enzyme. J Biol Chem. 1984 May 25;259(10):6215–6221. [PubMed] [Google Scholar]
- SUGIURA K., STOCK C. C. Studies in a tumor spectrum. III. The effect of phosphoramides on the growth of a variety of mouse and rat tumors. Cancer Res. 1955 Jan;15(1):38–51. [PubMed] [Google Scholar]
- Sauer L. A., Stayman J. W., 3rd, Dauchy R. T. Amino acid, glucose, and lactic acid utilization in vivo by rat tumors. Cancer Res. 1982 Oct;42(10):4090–4097. [PubMed] [Google Scholar]
- Schaur R. J., Semmelrock H. J., Schreibmayer W., Tillian H. M., Schauenstein E. Tumor host relations. V. Nitrogen metabolism in Yoshida sarcoma-bearing rats. Reduction of growth rate and increase of survival time by administration of physiological doses of branched-chain amino acids. J Cancer Res Clin Oncol. 1980;97(3):285–293. doi: 10.1007/BF00405780. [DOI] [PubMed] [Google Scholar]