APOPTOSIS: REGULATION AND MECHANISMS OF THE PROGRAMMED CELL SUICIDE-REVIEW
Keywords:
Keywords: apoptosis, programmed cell death, caspases, Bcl-2 family, mitochondrial pathway, extrinsic pathway, intrinsic pathway, cell signaling, apoptotic regulators, p53, death receptors, cytochrome c, DNA fragmentation, cell cycle, cancer therapy, immune response, cellular homeostasis.Abstract
bstract: Apoptosis, or programmed cell death, is a hallmark process of cellular
homeostasis, embryonic development, and immune responses. It therefore plays an
important role in the elimination of damaged or unnecessary cells through the
protection of an organism against harmful effects, such as tumorigenesis and
autoimmune diseases.
It reviews the current understanding of the mechanisms that regulate apoptosis,
focusing on intrinsic and extrinsic pathways, regulatory molecules, and the biological
significance of apoptosis both in health and disease. Beyond these issues, the review
will discuss possible therapeutic interventions directed to apoptotic pathways for the
treatment of cancer, neurodegenerative disorders, and other diseases involving
dysregulation of apoptosis.
References
References:
1. Abate M. et al. Mitochondria as playmakers of apoptosis, autophagy and senescence
//Seminars in cell & developmental biology. – Academic Press, 2020. – Т. 98. – С.
139-153.
2. Alqathama A. CASPASE-3 FUNCTION //CASPASE-3. – С. 21.
3. Asadi M. et al. Caspase‐3: structure, function, and biotechnological aspects
//Biotechnology and Applied Biochemistry. – 2022. – Т. 69. – №. 4. – С. 1633-
1645.
4. Ashkenazi A. Targeting the extrinsic apoptosis pathway in cancer //Cytokine &
growth factor reviews. – 2008. – Т. 19. – №. 3-4. – С. 325-331.
5. Berthelet J., Dubrez L. Regulation of apoptosis by inhibitors of apoptosis (IAPs)
//Cells. – 2013. – Т. 2. – №. 1. – С. 163-187.
6. Breckenridge D. G. et al. Regulation of apoptosis by endoplasmic reticulum
pathways //Oncogene. – 2003. – Т. 22. – №. 53. – С. 8608-8618.
7. Carson D. A., Ribeiro J. M. Apoptosis and disease //The Lancet. – 1993. – Т. 341.
– №. 8855. – С. 1251-1254.
8. Chao D. T. et al. Bcl-XL and Bcl-2 repress a common pathway of cell death //The
Journal of experimental medicine. – 1995. – Т. 182. – №. 3. – С. 821-828.
9. Chota A., George B. P., Abrahamse H. Interactions of multidomain pro-apoptotic
and anti-apoptotic proteins in cancer cell death //Oncotarget. – 2021. – Т. 12. – №.
16. – С. 1615.
10. Clement M. V., Stamenkovic I. Fas and tumor necrosis factor receptor-mediated
cell death: similarities and distinctions //The Journal of experimental medicine. –
1994. – Т. 180. – №. 2. – С. 557-567.
11. DeLong M. J. Apoptosis: a modulator of cellular homeostasis and disease states
//Annals of the New York Academy of Sciences. – 1998. – Т. 842. – №. 1. – С. 82-
90.
12. Erekat N. S. Apoptosis and its therapeutic implications in neurodegenerative
diseases //Clinical Anatomy. – 2022. – Т. 35. – №. 1. – С. 65-78.
13. Falschlehner C. et al. TRAIL and other TRAIL receptor agonists as novel cancer
therapeutics //Therapeutic Targets of the TNF Superfamily. – 2009. – С. 195-206.
14. Favaloro B. et al. Role of apoptosis in disease //Aging (Albany NY). – 2012. – Т.
4. – №. 5. – С. 330.
15. Fernald K., Kurokawa M. Evading apoptosis in cancer //Trends in cell biology. –
2013. – Т. 23. – №. 12. – С. 620-633.
16. Fesik S. W., Shi Y. Controlling the caspases //Science. – 2001. – Т. 294. – №. 5546.
– С. 1477-1478.
17. Fulda S. Tumor resistance to apoptosis //International journal of cancer. – 2009. –
Т. 124. – №. 3. – С. 511-515.
18. Green D. R. The mitochondrial pathway of apoptosis part II: the BCL-2 protein
family //Cold Spring Harbor perspectives in biology. – 2022. – Т. 14. – №. 6. – С.
a041046.
19. Guerrache A., Micheau O. TNF-Related Apoptosis-Inducing Ligand: Non-
Apoptotic Signalling //Cells. – 2024. – Т. 13. – №. 6. – С. 521.
20. Han Y. H. et al. Regulation of anoikis by extrinsic death receptor pathways //Cell
Communication and Signaling. – 2023. – Т. 21. – №. 1. – С. 227.
21. Hao Z. et al. Specific ablation of the apoptotic functions of cytochrome C reveals a
differential requirement for cytochrome C and Apaf-1 in apoptosis //Cell. – 2005. –
Т. 121. – №. 4. – С. 579-591.
22. Hensley P., Mishra M., Kyprianou N. Targeting caspases in cancer therapeutics
//Biological chemistry. – 2013. – Т. 394. – №. 7. – С. 831-843.
23. Inoue N. et al. Molecular characteristics of porcine Fas-associated death domain
(FADD) and procaspase-8 //Journal of Reproduction and Development. – 2007. –
Т. 53. – №. 2. – С. 427-436.
24. Kumar V., Maity S. ER stress-sensor proteins and ER-mitochondrial crosstalk—
signaling beyond (ER) stress response //Biomolecules. – 2021. – Т. 11. – №. 2. –
С. 173.
25. Lei C. et al. Copper induces mitochondria-mediated apoptosis via AMPK-mTOR
pathway in hypothalamus of Pigs //Ecotoxicology and environmental safety. –
2021. – Т. 220. – С. 112395.
26. Letai A. Apoptosis and cancer //Annual Review of Cancer Biology. – 2017. – Т. 1.
– №. 1. – С. 275-294.
27. Maximov G. K., Maximov K. G. The role of p53 tumor-suppressor protein in
apoptosis and cancerogenesis //Biotechnology & Biotechnological Equipment. –
2008. – Т. 22. – №. 2. – С. 664-668.
28. McIlwain D. R., Berger T., Mak T. W. Caspase functions in cell death and disease
//Cold Spring Harbor perspectives in biology. – 2013. – Т. 5. – №. 4. – С. a008656.
29. Mollazadeh H. et al. Effects of statins on mitochondrial pathways //Journal of
Cachexia, Sarcopenia and Muscle. – 2021. – Т. 12. – №. 2. – С. 237-251.
30. Nair P. et al. Apoptosis initiation through the cell-extrinsic pathway //Methods in
enzymology. – Academic Press, 2014. – Т. 544. – С. 99-128.
31. Obeng E. Apoptosis (programmed cell death) and its signals-A review //Brazilian
Journal of Biology. – 2020. – Т. 81. – №. 4. – С. 1133-1143.
32. Pantiya P. et al. Mitochondrial abnormalities in neurodegenerative models and
possible interventions: Focus on Alzheimer’s disease, Parkinson’s disease,
Huntington’s disease //Mitochondrion. – 2020. – Т. 55. – С. 14-47.
33. Pop C., Salvesen G. S. Human caspases: activation, specificity, and regulation
//Journal of biological Chemistry. – 2009. – Т. 284. – №. 33. – С. 21777-21781.
34. Salvesen G. S. Caspases and apoptosis //Essays in biochemistry. – 2002. – Т. 38. –
С. 9-19.
35. Selivanova G., Wiman K. G. Reactivation of mutant p53: molecular mechanisms
and therapeutic potential //Oncogene. – 2007. – Т. 26. – №. 15. – С. 2243-2254.
36. Sgorbissa A. et al. Caspase-3 and caspase-7 but not caspase-6 cleave Gas2 in vitro:
implications for microfilament reorganization during apoptosis //Journal of cell
science. – 1999. – Т. 112. – №. 23. – С. 4475-4482.
37. Sharma V. K. et al. Apoptotic pathways and Alzheimer’s disease: probing
therapeutic potential //Neurochemical research. – 2021. – Т. 46. – №. 12. – С. 3103-
3122.
38. Shelton S. N., Dillard C. D., Robertson J. D. Activation of caspase-9, but not
caspase-2 or caspase-8, is essential for heat-induced apoptosis in Jurkat cells
//Journal of Biological Chemistry. – 2010. – Т. 285. – №. 52. – С. 40525-40533.
39. Van Opdenbosch N., Lamkanfi M. Caspases in cell death, inflammation, and
disease //Immunity. – 2019. – Т. 50. – №. 6. – С. 1352-1364.
40. Vogler M. et al. Bcl-2 inhibitors: small molecules with a big impact on cancer
therapy //Cell Death & Differentiation. – 2009. – Т. 16. – №. 3. – С. 360-367.
41. Wu C. C., Bratton S. B. Regulation of the intrinsic apoptosis pathway by reactive
oxygen species //Antioxidants & redox signaling. – 2013. – Т. 19. – №. 6. – С. 546-
558.
42. Zimmermann K. C., Green D. R. How cells die: apoptosis pathways //Journal of
Allergy and Clinical Immunology. – 2001. – Т. 108. – №. 4. – С. S99-S103.
