Abstract
Apoptosis is a form of cell death characterized by chromatin condensation, cytoplasmic blebbing and DNA fragmentation. The earliest changes of apoptosis include the loss of cell junctions and other plasma membrane structures such as microvilli. The most significant morphological and biochemical changes in apoptotic cells occur in the nucleus. The chromatin rapidly forms dense aggregates and activation of endogenous endonuclease results in the cleavage of the chromatin into oligonucleosome-length DNA fragments (200 base pairs), which are considered to be characteristic biochemical markers for apoptosis (1,2). Apoptosis was observed in many tissues, both healthy and neoplastic, adult and embryonic (3). It is known to occur in neoplastic tissue in response to treatment. Several anticancer drugs have been shown to induce apoptosis in different cells (4–6).
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References
Schwartzman, R.A. and Cidlowski, J.A. Apoptosis: The biochemistry and molecular biology of programmed cell death. Endocrine rev., 14:133–151, 1993.
Laiho, K.U., Berezesky, I.K. and Trump, B.F. The role of calcium in cell injury: Studies in Erlich ascites tumor cells following injury with anoxia and organic mercurials. Surv. Synth. Path. Res. 2:170–183, 1983.
Duke CR, Ojcius DM and Young JDE. Cell suicide in health and disease. Scientific American, pp.80–87, December 1996.
Buttyan, R., Olsson, CA., Pintar, J., Chang, C, Bandyk, M., Ng,P-Y. and Sawczuk, I.S. Induction of the TRPM-2 gene in cells undergoing programmed cell death. Mol. Cell Biol. 9:3473–3481, 1989.
Kaufmann, S.H. Induction of endonucleolytic DNA cleavage in human melogenous leukemia cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: a cautionary note. Cancer Res. 49:5870–5878, 1989.
Barry M.A., Behnke, C,A., Eastman, A. Activation of programmed cell death (apoptosis) by cisplatin, other anticancer drugs, toxins and hyperthemia. Biochem.Pharmacol. 40:2353–2362, 1990.
McConkey, D.J., Hartzell, P., Nicotera, P. and Orrenius, S. Calcium-activated DNA fragmentation kills immature thymocytes. FASEB J, 3:1843–1849, 1989.
Cohen, J.J. and Duke, R.C. Glucocorticoid activation of calcium-dependent endonuclease in thymocyte nuclei leads to cell death. J Immunol, 132:38–42, 1984.
Whyte, M.K.B., Meagher, L.C., MacDermot, J. and Haslett, C. Impairment of function in aging neutrophils is associated with apoptosis. J Immuonol, 150:5124–5134, 1993.
Shaw P, Bovey R, Tardy S, Sahli R, Sordat B and Costa J, Induction of apoptosis by wild-type p53 in human colon tumor derived cell line. Proc. Natl. Acad. Sci. USA 89:4495–4499, 1992
Yonish-Rouach, E., Resnitzky, D., Lotem, J., Sachs, L., Kimchi, A. and Oren, M. Wild-type p53 induced apoptosis of myeloid leukemic cells that is inhibited by interleukin-6. Nature(Lond.), 352:345–347, 1991.
Evan, G.I., Wyllie, A.H., Gilbert, C.S., et al. Induction of apoptosis in fibroblasts by c-myc protein. Cell, 69:119–128, 1992.
Vaux, D.L. and Weissman, I.L. Neither macromolecular synthesis nor myc is required for cell death via the mechanism that can be controlled by bcl-2. Mol Cell Biol, 13:7000–7005, 1993.
Oltvai, ZN., Milliman, CL. and Korsmeyer, SJ. Bcl-2 heterodimerized in vivo with a conserved homology Box that accelerates programed cell death. Cell, 74:609–619, 1993.
Benito E, Obrador A, Stiggelbout A,Bosch FX, Mulet M, Munoz N and Kaldor JA. Population-based case-control study of colorictal cancer in Majorka. Int J Cancer, 45:69–76, 1990.
Graham S. Diet in the epidemiology of breast cancer. Am J Epidemiol 116:68–75, 1982.
Graham S. Results of case control studies of diet and cancer in Baffalo. Cancer Res 43:2409–2413.
Scholar EM, Wolterman K, Birt DF and Bresnick E. Effect of dietary fat on metastasis of Lewis Lung Carcinoma and the BALB/c Mammary Carcinoma. Nutr Cancer 12:109–115, 1989.
McDanell R, McLean AE, Hanley AB, Heany RK and Fenwick GR. Cemical and biological properties of indole glucosinolates (glucobrassicins): a review. Food Chem Toxicol 26:59–70, 1988.
Bradfield CA and Bjeldanes LF. Structure activity relationships of dietary indoles: a proposed mechanism of action as modifiers of xenobiotic metabolism. J Toxic Environ Health, 21:311–323, 1987.
Dashwood RH, Uyetake L, Fong AT, Hendrich JD and Bailey GS. In vivo disposition of the natural anticarcinogen indole-3-carbinol after PO administration to rainbow trout. Fd Chem Toxicol 27:385–392, 1989.
Xiaokang G, Yannai S, Rennert G, Gruener N and Fares FA. 3,3′-diindolylmethane induced apoptosis in human cancer cells. Biochem Bioph Res Comm 228:153–158, 1996.
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Fares, F.A., Ge, X., Yannai, S., Rennert, G. (1998). Dietary Indole Derivatives Induce Apoptosis in Human Breast Cancer Cells. In: Walden, P., Trefzer, U., Sterry, W., Farzaneh, F., Zambon, P. (eds) Gene Therapy of Cancer. Advances in Experimental Medicine and Biology, vol 451. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5357-1_25
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DOI: https://doi.org/10.1007/978-1-4615-5357-1_25
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