By Mohamed Al-Rubeai, M. Al-Rubeai, F. Autuori, E M. Bruckheimer, S.H. Cho, T.G. Cotter, Z. Darzynkiewicz, M.G. Farrace, N.L. Harvey, J. Herrmann, S. Kumar, T.J. McdDonnell, A.J. McGowan, S.L. McKenna, R. O'Connor, S. Oliverio, M. Piacentini, M. Piredda, M.
The purpose of this quantity is to supply an in-depth assessment of the state of the art learn on apoptosis with contributions from key teams operating within the box. this sort of programme cellphone dying has acquired broad and swift awareness and now's regarded as one of many most well-liked components of technological know-how. the amount covers a number of points of the apoptotic dying procedure from the morphological and biochemical positive factors, mechanisms and genetic law to its function in pathological technique and capability implications for biomedical study and biopharmaceutical creation.
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1997 Cell vol. 90:405413). The protein is called Apaf-1 (apoptotic protease activating factor-t), and has regions of homology to both CED-4 and CED-3. Binding of catochrome C to Apaf-1 is required to trigger the activation of caspase-3. 10 References 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. 20. Clarke PGH, Clark S (1996) Anat Embryol 193:81 Lockshin RA, Williams CM (1964) J Insect Physiol 10:643 Saunders JW (1966) Science 154:604 Tata JR (1966) Dev Biol 13:77 Munk A (1971) Perspect Biol Med 14:265 Lockshin RA (1969) J Insect Physiol 15:1505 Kerr JFR, Wyllie AH, Currie AH (1972) Br J Cancer 26:239 Wyllie AH, Kerr JFR, Currie AR (1980) 68:251 Ellis HM, Horvitz HR (1986) Cell 44:817 Ellis RE, Yuan JY, Horvitz HR (1991) Ann Rev Cell Biol 7:663 Williams GT, Smith CA, McCarthy NJ, Grimes EA (1992) Trends Cell Biol 2: 263 Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR (1993) Cell 75:641 Hengartner MO, Horvitz HR (1994) Cell 76: 665 White E (1996) Genes and Dev 10:1 Chinnaiyan A, Dixit V (1996) Curr Biol 6:555 Cohen JJ, Duke RC, Fadok VA, Sellins KS (1992) Ann Rev Immunol 10: 267 Schwarz LM, Smith SW, ]ones MEE, Osborne BA (1993) 90:980 Jacobson MD, Weil M, RaffMC (1997) Cell 88:347 Vaux DL, Weissman IL, Kim SK (1992) Science 258:1955 Cornillon S, Foa C, Davoust J, Buonavista N, Gross JD, Goldstein P (1994) J Cell Sci 107:2691 21.
In addition, anti-apoptotic proteins such as Bcl-2, v-Abl and mutant P53 can inhibit Myc induced cell death, enabling proliferation to be the primary biological consequence of Myc de-regulation [132-134]. In vivo co-operation between m y c and bcl-2 has been demonstrated in experiments with transgenic mice. Mice transgenic for rnyc alone did not show hyperplasia despite an augmentation in proliferation, whereas rnyc/bcl-2 double transgenics rapidly developed malignant lymphomas . Thus the ability of Myc to induce two separate and functionally conflicting pathways necessitates the presence of a survival cytokine or gene, and provides a rationale for oncogene co-operation in cellular transformation .
Some are the products of oncogenes or tumor suppressor genes, e. , such as c-myc or wt p53 [30-32]. Others are viral proteins such as BHRF1, a product of the Epstein Barr virus, which is homologous to Bcl-2, or crmA, a product of cowpox virus, an inhibitor of caspases [33, 34]. These virally encoded proteins promote their intracellular propagation by postponing apoptosis. Given such a wide range of regulatory steps and molecules, there are many possibilities for interaction with the components involved in the regulation of apoptosis and thereby to modulate the cell's propensity to die.