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Chap. 1 - CELL INJURY AND CELL DEATH

Published online by Cambridge University Press:  07 September 2011

Adone Baroni
Affiliation:
Second University of Naples
Eleonora Ruocco
Affiliation:
Second University of Naples
Maria Antonietta Tufano
Affiliation:
Second University of Naples
Elisabetta Buommino
Affiliation:
Second University of Naples
Ronni Wolf
Affiliation:
Kaplan Medical Center, Rehovot, Israel
Batya B. Davidovici
Affiliation:
Kaplan Medical Center, Rehovot, Israel
Jennifer L. Parish
Affiliation:
Jefferson Medical College of Thomas Jefferson University
Lawrence Charles Parish
Affiliation:
Jefferson Medical College of Thomas Jefferson University
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Summary

WHEN CELLS are damaged, as often occurs during trauma and metabolic stress, the organism has to choose whether to repair the damage by promoting cell survival or remove irreparably injured cells. Cell injury occurs when an adverse stimulus reversibly disrupts the normal, complex homeostatic balance of the cellular metabolism. In this case, after injury the cells attempt to seal breaks in their membranes, chaperone the removal or refolding of altered proteins, and repair damaged DNA. On the contrary, when cell injury is too extensive to permit reparative responses, the cell reaches a “point of no return” and the irreversible injury culminates in programmed cell death (PCD). Specific properties or features of cells make them more or less vulnerable to external stimuli, thus determining the kind of cellular response. In addition, the characteristic of the injury (type of injury, exposure time, or severity) will also affect the extent of the damage.

We present a short overview of the best-known PCD pathways. We emphasize the apoptotic pathway, considered for years the hallmark of PCD, and the different stimuli that produce cell injury.

CELL INJURY

The survival of multicellular organisms depends on the function of a diverse set of differentiated cell types. After development is complete, the viability of the organism depends on the maintenance and renewal of these diverse lineages. Within each lineage homeostasis is maintained through a delicate balance between cell proliferation and cell death.

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Publisher: Cambridge University Press
Print publication year: 2011

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References

Broker, , Kruyt, FAE, Giaccone, G.Cell death independent of caspases: a review. Clin Cancer Res. 2005;11:3155–62.CrossRefGoogle ScholarPubMed
Barr, PJ, Tomei, LD. Apoptosis and its role in human disease. Biotechnology. 1994;12:487–93.CrossRefGoogle ScholarPubMed
Skulachev, VP. The programmed death phenomena, aging, and the Samurai law of biology. Exp Gerontol. 2001;36:996–1024.CrossRefGoogle ScholarPubMed
Skulachev, VP. Programmed death phenomena: from organelle to organism. Ann NY Acad Sci. 2002;959:214–37.CrossRefGoogle ScholarPubMed
Cobb, JP, Hotchkiss, RS, Karl, IE, Buchman, TG. Mechanism of cell injury and death. Br J Anaesth. 1996;77:3–10.CrossRefGoogle Scholar
Majno, G, Joris, I.Apoptosis, oncosis, and necrosis. An overview of cell death. Am J Pathol. 1995;146:3–15.Google ScholarPubMed
Proskuryakov, SY, Konoplyannikov, AG, Gabai, VL. Necrosis: a specific form of programmed cell death?Exp Cell Res. 2003;283:1–16.CrossRefGoogle ScholarPubMed
Fietta, P. Many ways to die: passive and active cell death styles. Riv Biol. 2006;99:69–83.Google ScholarPubMed
Blagosklonny, MV. Cell death beyond apoptosis. Leukemia. 2000;14:1502–8.CrossRefGoogle ScholarPubMed
Sperandio, S, Belle, I, Bredesen, . An alternative, non apoptotic form of programmed cell death. Proc Natl Acad Sci USA. 2000;97:14376–81.CrossRefGoogle Scholar
King, KL, Cidlowski, JA. Cell cycle and apoptosis: common pathways to life and death. J Cell Biochem. 1995;58:175–80.CrossRefGoogle ScholarPubMed
Raff, MC. Social controls on cell survival and cell death. Nature. 1993;356:397–400.CrossRefGoogle Scholar
Sen, S.Programmed cell death: concept, mechanism and control. Biol Rev. 1992;67:287–319.CrossRefGoogle ScholarPubMed
Lennon, SV, Martin, SJ, Cotter, TG. Dose-dependent induction of apoptosis in human tumor cell lines by widely diverging stimuli. Cell Prolif. 1991;24:203–14.CrossRefGoogle ScholarPubMed
Kerr, JFR. Shrinkage necrosis: a distinct mode of cellular death. J Pathol. 1971;105:13–20.CrossRefGoogle ScholarPubMed
Shrek, R, Chandra, S, Molnar, Z, Stefani, SS. Two types of interphase death of lymphocytes exposed to temperatures of 37–45°C. Radiat Res. 1980;82:162–70.CrossRefGoogle Scholar
Kerr, JFR, Willie, AH, Currie, AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer. 1972;26:239–57.CrossRefGoogle ScholarPubMed
Chang, HY, Yang, X. Proteases for cell suicide: functions and regulation of caspases. Microbiol Mol Biol Rev. 2000;64:821–46.CrossRefGoogle ScholarPubMed
Barrett, JC, Annab, , Alcorta, D, et al. Cellular senescence and cancer. Cold Spring Harbor Symposia on Quantitative Biology Vol LIX. 1994.Google Scholar
Guenal, I, Risler, Y, Mignotte, B. Down-regulation of actin genes precedes microfilament network disruption and actin cleavage during p53-mediated apoptosis. Br J Cell Sci. 1997;110:489–95.Google ScholarPubMed
Nagata, S. Apoptotic DNA fragmentation. Exp Cell Res. 2000;256:12–8.CrossRefGoogle ScholarPubMed
Cruchten, S, Broeck, W.Morphological and biochemical aspects of apoptosis, oncosis, and necrosis. Anat Histol Embryol. 2002;31:214–23.CrossRefGoogle ScholarPubMed
Platt, N, da Silva, RP, Gordon, S.Recognizing death: the phagocytosis of apoptotic cells. Trends Cell Biol. 1998;8:365–72.CrossRefGoogle ScholarPubMed
Savill, J, Fadok, V.Corpse clearance defines the meaning of cell death. Nature. 2000;407:784–8.CrossRefGoogle ScholarPubMed
West, JD, Ji, C, Marnett, LJ. Modulation of DNA fragmentation factor 40 nuclease activity by poly(ADP-ribose) polymerase-1. J Biol Chem. 2005;280:15141–7.CrossRefGoogle ScholarPubMed
Contassot, E, Gaide, O, French, . Death receptors and apoptosis. Dermatol Clin. 2007;25:487–501.CrossRefGoogle ScholarPubMed
Susin, SA, Zamzami, N, Castedo, M, et al. The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas(Apo-1(CD95- and ceramide-induced apoptosis. J Exp Med. 1997;186:25–37.CrossRefGoogle ScholarPubMed
Temme, A, Rieger, M, Reber, F, et al. Localization, dynamics and function of survivin revealed by expression of functional survivinDsRed fusion proteins in the living cell. Mol Biol Cell. 2003;14:78–92.CrossRefGoogle ScholarPubMed
Nouraini, S, Six, E, Matsuyama, S, et al. The putative pore-forming domain of Bax regulates mitochondrial localization and interaction with Bcl-XL. Mol Cell Biol. 2000;20:1604–15.
Leist, M, Jäättelä, M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol. 2001;2:589–98.CrossRefGoogle Scholar
Sabbatini, P, Chiou, SK, Rao, L, White, E. Modulation of p53-mediated transcriptional repression and apoptosis by the adenovirus E1B 19k protein. Mol Cell Biol. 1995;15:1060–70.CrossRefGoogle ScholarPubMed
Oren, M. Decision making by p53: life, death and cancer. Cell Death Differ. 2003;10:431–42.CrossRefGoogle ScholarPubMed
Breckenridge, DG, Germain, M, Mathai, JP, et al. Regulation of apoptosis by endoplasmic reticulum pathways. Oncogene. 2003;22:8608–18.CrossRefGoogle ScholarPubMed
Rao, RV, Poksay, KS, Castro-Obregon, S, et al. Molecular components of a cell death pathway activated by endoplasmic reticulum stress. J Biol Chem. 2004;279:177–87.CrossRefGoogle ScholarPubMed
Guroff, G. A neutral, calcium-activated proteinase from the soluble fraction of the brain. J Biol Chem. 1964;239:149–55.Google Scholar
Wang, KK. Calpain and caspase: can you tell the difference?Trends Neurosci. 2000;23:20–6.CrossRefGoogle ScholarPubMed
Mathiasen, IS, Lademann, U, Jäättelä, M. Apoptosis induced by vitamin D compounds in breast cells is inhibited by bcl-2 but does not involve known caspases or p53. Cancer Res. 1999;59:4848–56.Google ScholarPubMed
Taylor, JP, Hardy, J, Fischbeck, KH. Toxic proteins in neurodegenerative disease. Science. 2002;296:1991–5.CrossRefGoogle ScholarPubMed
Gozuacik, D, Kimchi, A.Autophagy as a cell death and tumor suppressor mechanism. Oncogene. 2004;23:2891–906.CrossRefGoogle ScholarPubMed
Danial, NN, Korsmeyer, SJ. Cell death: critical control points. Cell. 2004;116:205–19.CrossRefGoogle ScholarPubMed
Shintani, T, Klionsky, DJ. Autophagy in health disease: a double-edged sword. Science. 2004;306:990–6.CrossRefGoogle ScholarPubMed
Yue, Z, Jin, S, Yang, C, et al. Beclin 1, an autophagy gene essential for early embryonic development, is a haplo-insufficient tumor suppressor. Proc Natl Acad Sci USA. 2003;100:15077–82.CrossRefGoogle Scholar
Pattingre, S, Tassa, A, Qu, X, et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell. 2005;122:927–39.CrossRefGoogle ScholarPubMed
Castro-Obregon, S, Del Rio, G, Chen, SF, et al. A ligand-receptor pair that triggers a non-apoptotic form of programmed cell death. Cell Death Differ. 2002;9:807–17.CrossRefGoogle ScholarPubMed
Tanabe, K, Nakanishi, H, Maeda, H, et al. A predominant apoptotic death pathway of neuronal PC12 cells induced by activated microglia is displaced by a non-apoptotic death pathway following blockage of caspase-3-dependent cascade. J Biol Chem. 1999;274:15725–31.CrossRefGoogle ScholarPubMed
Mochizuki, T, Asai, A, Saito, N, et al. Akt protein kinase inhibits non-apoptotic programmed cell death induced by ceramide. J Biol Chem. 2002;277:2790–7.CrossRefGoogle ScholarPubMed
Eby, MT, Jasmin, A, Kumar, A, et al. A novel member of the tumor necrosis factor receptor family, activates the c-Jun N-terminal kinase pathway and mediates caspase-independent cell death. J Biol Chem. 2000;275:15336–42.CrossRefGoogle ScholarPubMed
Koh, JY, Gwang, BJ, Lobner, D, Choi, DW. Potential necrosis of cultured cortical neurons by neurotrophins. Science. 1995;268:573–5.CrossRefGoogle Scholar
Edinger, AL, Thompson, CB. Death by design: apoptosis, necrosis and autophagy. Curr Opin Cell Biol. 2004;16:663–9.CrossRefGoogle ScholarPubMed
Zong, WX, Thompson, CB. Necrotic death as a cell fate. Genes Dev. 2006;20:1–15.CrossRefGoogle ScholarPubMed
Sauter, B, Albert, ML, Francisco, L, et al. Consequences of cell death: exposure to necrotic tumor cells, but not primary tissue cells or apoptotic cells, induces the maturation of immunostimulatory dendritic cells. J Exp Med. 2000;191:423–34.CrossRefGoogle ScholarPubMed
Bowen, AR, Hanks, AN, Allen, SM, et al. Apoptosis regulators and responses in human melanocytic and keratinocytic cells. J Invest Dermatol. 2003;120:48–55.CrossRefGoogle ScholarPubMed
Soengas, MS, Lowe, SW. Apoptosis and melanoma chemoresistance. Oncogene. 2003;22:3138–51.CrossRefGoogle ScholarPubMed
Johnstone, RW, Ruefli, AA, Lowe, SW. Apoptosis: a link between cancer genetics and chemotherapy. Cell. 2002;108:153–64.CrossRefGoogle ScholarPubMed
Thompson, CB. Apoptosis in the pathogenesis and treatment of disease. Science. 1995;267:1456–62.CrossRefGoogle Scholar
Puviani, M, Marconi, A, Cozzani, E, Pincelli, C. Fas ligand in pemphigus sera induces keratinocyte apoptosis through the activation of caspase-8. J Invest Dermatol. 2003;120:164–7.CrossRefGoogle ScholarPubMed
Korman, N. Pemphigus. J Am Acad Dermatol. 1988;18:1219–38.CrossRefGoogle ScholarPubMed
Weiske, J, Schoneberg, T, Shroder, W, et al. The fate of desmosomal proteins in apoptotic cells. J Biol Chem. 2001;276:41175–81.CrossRefGoogle ScholarPubMed
Baroni, A, Buommino, E, Paoletti, I, et al. Pemphigus serum and captopril induce hsp 70 and inducible nitric oxide synthase overexpression, triggering apoptosis in human keratinocytes. Br J Dermatol. 2004;150:1070–80.CrossRefGoogle ScholarPubMed
Arredondo, J, Cheryavsky, AI, Karaouni, A, Grando, SA. Novel mechanism of target cell death and survival and of therapeutic action of IVIg in pemphigus. Am J Pathol. 2005;167:1531–44.CrossRefGoogle ScholarPubMed
Kitanaka, C, Kuchino, Y. Caspase-independent programmed cell death with necrotic morphology. Cell Death Differ. 1999;6:508–15.CrossRefGoogle ScholarPubMed
Bursch, W.The autophagosomal-lysosomal compartment in cell death. Cell Death Differ. 2001;8:569–81.CrossRefGoogle ScholarPubMed

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