Abstract
Cellular death can be classified into two broad morphologic groups, necrosis (zonal cellular necrosis) and apoptosis (selective cell death)3,9–11,13. The former process often affects simultaneously a large number of contiguous cells, such as in case of vascular and oxygen deficiency. Apoptosis, on the other hand, often involves isolated cells, usually as part of cell turnover in the tissue. In apoptosing cells, changes have been described in both the nucleus and cytoplasm11,21 (a) nuclear swelling with fragmentation and clumping of the chromatin and (b) cytoplasmic condensation. In contrast to the scattering of cellular debris found in necrosis, cellular material in apoptosis is released as “packaged” apoptotic bodies, which appear to be phagocytized by adjacent viable cells. Again in contrast to necrosis, the functional integrity of the plasma membrane is retained in apoptosis, maintaining the cellular constituents in a confined space while as yet largely undefined biochemical processes alter the nuclear and cytoplasmic constituents.
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References
J. S. Amenta and M. J. Sargus, Mechanisms of protein degradation in growing and non-growing L-cell cultures, Biochem. J. 182:847 (1979).
J. S. Amenta and S. C. Brocher, Evidence for heterogeneity of protein-turnover states in cultured cells, Biochem. J. 190:673 (1980).
J. S. Amenta, S. C. Brocher, J. Mehta, D. Manjunath and F. M. Baccino, Evidence for special relationship between proteolysis and single cell necrosis, Tox. Path. 14:335 (1986).
J. S. Amenta, J. Mehta and F. M. Baccino, Proteolysis associated with thymidine-induced selective cell death in L-cell cultures, in: “Chemical Carcinogenesis: Models and Mechanisms,” F. Feo, P. Pani, A. Columbano, R. Garcea, eds., Plenum Press, New York (1988).
J. S. Amenta and F. M. Baccino, Proteolysis and cell death, in: “current Trends in Intracellular Protein Degradation,” E. Knecht and S. Grisolia, eds., Springer Verlag, (1989).
F. M. Baccino, L. Tessitore and G. Bonelli, Control of protein degradation and growth phase in normal and neoplastic cells, Tox. Path. 12:281 (1984).
Z. Ben-Ishay and E. Farber, Protective effects of an inhibitor of protein synthesis, cycloheximide, on bone marrow damage induced by cytosine arabinoside or nitrogen mustard, Lab. Invest. 33:478 (1975).
G. J. Boer, A simplified microassay of DNA and RNA using ethidium bromide, Anal. Biochem. 65:225 (1975).
I. D. Bowen, Techniques for demonstrating cell death, in: “Cell Death in Biology and Pathology,” I. D. Bowen and R. A. Lochshin, eds., Chapman and Hall, New York, (1981).
K. Ijiri and C. S. Potten, Cell death in cell hierarchies in adult mammalian tissues, in: “Perspectives on Mammalian Cell Death,” C. S. Potten, ed., Oxford Publications, Oxford, (1987).
J. F. R. Kerr, Shrinkage necrosis: A distinct mode of cellular death, J. Path. 105:13 (1971).
J. F. R. Kerr, A. H. Wyllie and A. R. Currie, Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics, Br. J. Cancer 26:239 (1972).
J. F. R. Kerr, J. Searle, B. V. Harmon and C. J. Bishop, Apoptosis, in: “Perspectives on Mammalian Cell Death,” C. S. Potten, ed., Oxford Publications, Oxford, (1987).
M. W. Lieberman, R. S. Verbin, M. Landay, H. Liang, E. Farber, T. N. Lee and R. Starr, A probable role for protein synthesis in intestinal epithelial cell damage induced in vivo by cytosine arabinoside, nitrogen mustard, or X-irradiation, Cancer Res. 30:942 (1970).
O. H. Lowry, N. J. Rosebrough, A. L. Farr and R. J. Randall, Protein measurement with the Folin phenol reagent, J. Biol. Chem. 193:265 (1951).
J. Searle, T. A. Lawson, P. J. Abbott, B. Harmon and J. F. R. Kerr, Electron-microscope study of the mode of cell death induced by cancer chemotherapeutic agents in populations of proliferating normal and neoplastic cells, J. Path. 116:129 (1975).
J. A. Silverman, J. Mehta, S. C. Brocher and J. S. Amenta, Analytical errors in measuring radioactivity in cell proteins and their effect on estimates of protein turnover in L cells, Biochem. J. 226:361 (1985).
J. R. Tata, Requirement for RNA and protein synthesis for induced regression of tadpole tail in organ culture, Devel. Biol. 13:77 (1966).
L. Tessitore, G. Bonelli, G. Cecchini, J. S. Amenta and F. M. Baccino, Regulation of protein turnover versus growth state: Ascites hepatoma as a model for studies both in the animal and in vitro, Arch. Biochem. Biophys. 255:372 (1987).
R. S. Verbin, G. Diluiso and E. Farber, Protective effects of cycloheximide against 1-beta-D-arabinosyl-cytosine-induced intestinal lesions, Cancer Res. 33:2086 (1973).
A. H. Wyllie, J. F. R. Kerr and A. R. Currie, The significance of apoptosis, Int. Rev. Cytol. 68:251 (1980).
A. H. Wyllie, Cell death: a new classification separating apoptosis from necrosis, in: “Cell Death in Biology and Pathology,” I. D. Bowen, R. A. Lockshin, Chapman and Hall, New York, (1981).
A. H. Wyllie, Apoptosis: Cell death in tissue regulation, J. Pathol. 153:313 (1987).
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Amenta, J.S., Sargus, M.J., Bonelli, G., Baccino, F.M. (1991). An in Vitro Model for Apoptosis: Uptake and Degradation of Apoptotic Bodies. In: Columbano, A., Feo, F., Pascale, R., Pani, P. (eds) Chemical Carcinogenesis 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3694-9_43
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DOI: https://doi.org/10.1007/978-1-4615-3694-9_43
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