Suppression of Dimethylhydrazine-induced Carcinogenesis in Mice by Dietary Addition of the Bowman-Birk Protease Inhibitor

Cancer Research

Volumn 50, Issue 3, 1990, Pages 580-586

  Clair, William H St ^a,b   Billings, Paul C ^a,c   Carew, Josephine A ^a,d   Keller McGandy, Christine ^a   Newberne, Paul ^a   Kennedy, Ann R ^a,c  

^a HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

^b WAKE FOREST SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d DANA FARBER CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMETHYLHYDRAZINE; PROTEINASE INHIBITOR; SUPPRESSOR FACTOR;

ANIMAL; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CARCINOGENESIS; MAMMAL; MOUSE; NONHUMAN; PRIORITY JOURNAL;

ADENOCARCINOMA; ANIMAL; BODY WEIGHT; CARCINOMA, SQUAMOUS CELL; DIMETHYLHYDRAZINES; GASTROINTESTINAL NEOPLASMS; LIVER NEOPLASMS; LIVER NEOPLASMS, EXPERIMENTAL; METHYLHYDRAZINES; MICE; MICE, INBRED STRAINS; NEOPLASMS, EXPERIMENTAL; ORGAN WEIGHT; PANCREAS; SUPPORT, U.S. GOV'T, P.H.S.; TRYPSIN INHIBITOR, BOWMAN-BIRK SOYBEAN; TRYPSIN INHIBITORS;

EID: 0025166613     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article

References (50)

1. Wattenberg, L. W. Chemoprevention of cancer. Cancer Res., 45: 1–8, 1985.
2. Troll, W., Frenkel, K., and Wiesner, R. Protease inhibitors as anticarcinogens. J. Natl. Cancer Inst., 73: 1245–1250, 1984.
3. Kennedy, A. R., and Billings, P. C. Anticarcinogenic actions of protease inhibitors. In: P. A. Cerutti, O. F. Nygaard, and M. G. Simic (eds.), Anticar-cinogenesis and Radiation Protection, pp. 285–295. New York: Plenum Press, 1987.
4. Birk, Y. Structure-activity relationships of several trypsin and chymotrypsin inhibitors from legume seeds. In: N. Fritz, H. Tschesche, L. J. Green, and E. Truscheit (eds.), Proteinase Inhibitors, pp. 355–361. Berlin: Springer-Verlag, 1974.
5. Kennedy, A. R. Promotion and other interactions between agents in the induction of transformation in vitro in fibroblasts. In: T. J. Slaga (ed.), Mechanisms of Tumor Promotion, Vol III, Tumor Promotion and Carcinogenesis In Vitro, pp. 13–55, 1984. CRC Press Inc., 1984.
6. Doll, R., and Peto, R. Causes of cancer: quantitative estimates of avoidable risks of cancer in the United States today. J. Natl. Cancer Inst., 66: 1193–1308, 1981.
7. Correa, P. Epidemiologic correlations between diet and cancer frequency. Cancer Res., 41: 3685–3690, 1981.
8. Philips, R. L. Role of life-style and dietary habits in risk of cancer among Seventh Day Adventists. Cancer Res., 35: 3513–3522, 1975.
9. Kennedy, A. R., and Little, J. B. Protease inhibitors suppress radiation induced malignant transformation in vitro. Nature (Lond.), 276: 825–826, 1978.
10. Baturay, N. Z., and Kennedy, A. R. Pyrene acts as a cocarcinogen with the carcinogens benzo(a)pyrene, B-propiolactone and radiation in the induction of malignant transformation of cultured mouse fibroblasts; soybean extract containing the Bow man-Birk inhibitor acts as an anticarcinogen. Cell Biol. Toxicol., 2: 21–32, 1986.
11. Kennedy, A. R. The conditions for the modification of radiation transformation in vitro by a tumor promoter and protease inhibitors. Carcinogenesis (Lond.), 6: 1441–1446, 1985.
12. Billings, P. C., St. Clair, W. H., Ryan, C. A., and Kennedy, A. R. Inhibition of radiation-induced transformation of C3H/10T1/2 cells by chymotrypsin inhibitor 1 from potatoes. Carcinogenesis (Lond.), 8: 809–812, 1987.
13. Chang, J. D., Billings, P. C., and Kennedy, A. R. C-myc expression is reduced in antipain treated proliferating C3H/10T1/2 cells. Biochem. Biophys. Res. Commun., 133: 830–835, 1985.
14. Chang, J. D., and Kennedy, A. R. Cell cycle progression of C3H/10T1/2 and 3T3 cells in the absence of an increase in c-myc RNA levels. Carcinogenesis (Lond.), 9: 17–20, 1988.
15. Garte, S. J., Currie, D. D., and Troll, W. Inhibition of H-ras oncogene transformation of NIH3T3 cells by protease inhibitors. Cancer Res., 47: 3159–3162, 1987.
16. Kennedy, A. R., Radner, B., and Nagasawa, H. Protease inhibitors reduce the frequency of spontaneous chromosome abnormalities in cells from patients with Bloom syndrome. Proc. Natl. Acad. Sci. USA, 81: 1827–1830, 1984.
17. Troll, W., Klassen, A., and Janoff, A. Tumorigenesis in mouse skin: inhibition by synthetic inhibitors of proteases. Science (Wash. DC), 169: 1211–1213, 1970.
18. Troll, W., Wiesner, R., Shellabarger, C. J., Holtzman, S., and Stone, J. P. Soybean diet lowers breast tumor incidence in irradiated rats. Carcinogenesis (Lond.), 7: 469–472, 1980.
19. Becker, F. F. Inhibition of spontaneous hepatocarcinogenesis in C3H/HeN mice by Edi Pro A, an isolated soy protein. Carcinogenesis (Lond.), 2: 1213–1214, 1981.
20. Corasanti, J. G., Hobika, G. H., and Markus, G. Interference with dimethyl-hydrazine induction of colon tumors in mice by c-aminocaproic acid. Science (Wash. DC), 216: 1020–1021, 1982.
21. Weed, H. G., McGandy, R. B., and Kennedy, A. R. Protection against dimethylhydrazine-induced adenomatous tumors of the mouse colon by the dietary addition of an extract of soybeans containing the Bowman-Birk protease inhibitor. Carcinogenesis (Lond.), 6: 1239–1241, 1985.
22. Messadi, D. V., Billings, P. C., Shklar, G., and Kennedy, A. R. Inhibition of oral carcinogenesis by a protease inhibitor. J. Natl. Cancer Inst., 76: 447–452, 1986.
23. Birk, Y. Proteinase inhibitors from plant sources. Methods Enzymol., 45: 695–751, 1976.
24. Birk, Y. The Bowman-Birk inhibitor. Int. J. Peptide Protein Res., 25: 113–131, 1985.
25. Hwang, D. L. R., Davis-Lin, K. T., Yang, W. K., and Foard, D. T. Purification, partial characterization and immunological relationships of multiple low molecular weight proteinase inhibitors of soybean. Biochem. Biophys. Acta, 495: 369–382, 1977.
26. Yavelow, J., Collins, J., Birk, Y., Troll, W., and Kennedy, A. R. Nanomolar concentrations of Bowman-Birk soybean protease inhibitor suppress X-ray-induced transformation in vitro. Proc. Natl. Acad. Sci. USA, 82: 5395–5399, 1985.
27. Nairn, M., Gertler, A., and Birk, Y. The effect of dietary raw and autoclaved soya-bean protein fractions on growth, pancreatic enlargement and pancreatic enzymes in rats. Br. J. Nutr., 47: 1–8, 1981.
28. McGuinness, E. E., Morgan, R. G. H., Levison, D. A., Frape, D. L., Hopewood, D., and Wormsley, K. G. The effect of long-term feeding of soya flour on the rat pancreas. Scand. J. Gastroenterol., 15: 497–502, 1980.
29. Crass, R. A., and Morgan, R. G. H. The effect of long-term feeding of soya bean flour diets on pancreatic growth in the rat. Br. J. Nutr., 47: 119–129, 1982.
30. Flavin, D. F. The effect of soybean trypsin inhibitors on the pancreas of animals and man. Vet. Hum. Toxicol., 24: 25–28, 1982.
31. Ausman, L. M., Harwood, J. P., King, N. W., Sehgal, P. K., Nicolosi, R. J., Hegsted, M. D., Liener, I. E., Donatucci, D., and Tarcza, J. The effects of long-term soy protein and milk protein feeding on the pancreas of Cebus albifrons monkeys. J. Nutr., 115: 1691–1701, 1985.
32. Wolf, W. J., and Cowan, J. C. Soybeans as a food source, pp. 51–53. Cleveland, OH: CRC Press, Inc., 1975.
33. Patten, J. R., Richards, E. A., and Wheeler, J. The effect of raw soybean on the pancreas of adult dogs. Proc. Soc. Exp. Biol. Med., 137: 58, 1971.
34. Patten, J. R., Richards, E. A., and Wheeler, J. The effect of dietary soybean trypsin inhibitor on the histology of dog pancreas. Life Sci., 10(2): 145–150, 1971.
35. Gorrill, A. D. L., and Thomas, J. W. Body weight changes, pancreas size and enzyme activity, and proteolytic enzyme activity and protein digestion in intestinal contents from calves fed soybean and milk protein diets. J. Nutr., 92: 215–223, 1967.
36. Hooks, R. D., Hays, V. W., Speer, V. C., and McCall, J. T. Effects of raw soybeans on pancreatic enzyme concentrations and performance of pigs. Fed. Proc. Am. Soc. Exp. Biol., 24: 894, 1965.
37. Mills, P. K., Beeson, W. L., Abbey, D. E., Fraser, G. E., and Phillips, R. L. Dietary habits and past medical history as related to fatal pancreas cancer risk among adventists. Cancer (Phila.), 61: 2578–2585, 1988.
38. Report of the American Institute of Nutrition Ad Hoc committee on standards for nutritional studies. J. Nutr., 107: 1340–1348, 1977.
39. Kassell, B. Trypsin and chymotrypsin inhibitors from soybeans. Methods Enzymol., 79: 853–862, 1970.
40. Butler, P. J. G., Harris, J. I., Hartler, B. S., and Leberma, R. The use of maleic anhydride for the reversible blocking of amino groups in polypeptide chains. Biochem. J., 772: 679–689, 1968.
41. Madar, Z., Birk, Y., and Gertler, A. Native and modified Bowman-Birk trypsin inhibitor-comparative effect on pancreatic enzymes upon ingestion by quails. Comp. Biochem. Physiol., 48B: 251–256, 1974.
42. Druckrey, H. Production of colonic carcinomas by 1, 2-dialkylhydrazines and azoxyalkanes. In: W. J. Brudette (ed.), Carcinoma of the colon and antecedent epithelium, pp. 267–279. Springfield, IL: C. C. Thomas Publisher, 1970.
43. Maronpot, R. R., Haseman, G. A., Boorman, S. E., Eustic, S. E., Rao, G. N., and Huff, J. E. Liver lesions in B6C3F1 mice: The National Toxicology Program, experience and position. Arch. Toxicol. Suppl., 10: 10–26, 1987.
44. Newberne, P. M. Assessment of the hepatocarcinogenic potential of chemicals: response of the liver. In: G. Plaa and W. R. Hewitt (eds.). Toxicology of the liver, pp. 243–290. New York: Raven Press, 1982.
45. Bradford, M. A. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72: 248–254, 1976.
46. Billings, P. C., St. Clair, W., Owen, A. J., and Kennedy, A. R. Potential intracellular target proteins of the anticarcinogenic Bowman-Birk protease inhibitor identified by affinity chromatography. Cancer Res., 48: 1798–1802, 1988.
47. Heussin, C., and Dowdle, E. B. Electrophoretic analysis of plasminogen activators in polyaerylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem., 102: 196–202, 1980.
48. Zar, J. H. Biostatistical Analysis, pp. 151–162. Englewood Cliff, NJ: Prentice-Hall, 1974.
49. Doell, B. H., Ebden, C. J., and Smith, C. A. Trypsin inhibitor activity of conventional foods which are part of the British diet and some soya products. Qual. Plant. Plant Foods Hum. Nutr., 31: 139–150, 1981.
50. Armstrong, B., and Doll, R. Environmental factors and cancer incidence and mortality in different countries, with special reference to dietary factors. Int. J. Cancer., 75: 617–631, 1975.