RESEARCH ON THE INFLUENCE OF VARIOUS SUBSTANCES ON CASPASE ACTIVITY (REVIEW)
Abstract
About the Authors
E. S. KokarevaRussian Federation
V. V. Morozov
Russian Federation
Ya. M. Stanishevskiy
Russian Federation
M. A. Zhuravleva
Russian Federation
A. V. Zubkov
Russian Federation
References
1. Vladimirskaja E. B. Mechanisms of apoptotic cell death. Hematology and transfusiology. 2002. T. 47. № 2. P. 35-40.
2. Grigor’ev M. Ju., Imjanitov E. N., Hanson K. P. Apoptosis is normal and pathological. Medical Academic Journal. T. 3. № 3. P. 3-11.
3. Nagornev V. A., Voskan’janc A. N. Apoptosis and its role in atherogenesis. Medical Academic Journal. 2003. T. 3. № 4. P. 3-18.
4. Robinson M. V., Trufakin V. A. Apoptosis of cells of the immune system. Successes of modern biology. 1991. T. 3. Vyp. 2. P. 246-259.
5. Rodriguez J., Lazebnik Y. Caspase-9 and Apaf-1 form an active holoenzyme. Genes Dev. 1999. № 13. Р. 3179-3184.
6. Saleh A., Srinivasula S. M., Acharya S., Fishel R., Alnemri E. S. Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J. Biol. Chem. 1999. V. 274. P. 17941-17945.
7. Yang X., Chang H. Y., Baltimore D. Essential role of CED-4 oligomerization in CED-3 activation and apoptosis. Science. 1998. V. 281. P. 1355-1357.
8. Kumar S., Doumanis J. The fly caspases. Cell Death Differ. 2000. № 7. Р. 1039-1044.
9. Shi Y. Apoptosome: the cellular engine for the activation of caspase-9. Structure. 2002. № 10. Р. 285-288.
10. Wei Y. The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity. Chem. Biol. 2000. № 7. Р. 423-432.
11. Salvesen G. S., Duckett C. S. IAP proteins: blocking the road to death’s door. Nature Rev. Mol. Cell Biol. 2002. № 3. Р. 401-410.
12. Sun C. NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP. Nature. 1999. V. 401. P. 818-822.
13. Ashhab Y., Alian A., Polliack A. Two splicing variants of a new inhibitor of apoptosis gene with different biological properties and tissue distribution pattern. FEBS Lett. 2001. V. 495. P. 56-60.
14. Zoog S. J., Schiller J. J., Wetter J. A. Baculovirus apoptotic suppressor P49 is a substrate inhibitor of initiator caspases resistant to P35 in vivo. EMBO J. 2002. V. 21. P. 5130-5140.
15. Srinivasula S. M. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO mediates opposing effects on caspase activity and apoptosis. Nature. 2001. V. 409. P. 112-116.
16. Shi Y. A conserved tetrapeptide motif: potentiating apoptosis through IAP-binding. Cell Death Differ. 2002. № 9. P. 93-95.
17. Wu G. Structural basis of IAP recognition by Smac/DIABLO. Nature. 2000. V. 408. P. 1008-1012.
18. Yang X., Chang H. Y., Baltimore D. Autoproteolytic activation of procaspases by oligomerization. Mol. Cell. 1998. № 1. Р. 319-325.
19. Boatright K. M., Salvesen G. S. Mechanisms of caspase activation. Boatright, Curr. Opin. Cell Biol. 2003. № 15. Р. 725-731.
20. Olivera S.-C. M., Caballero B. M., Argent R., Alonso J. C., Centeno F., Lorenzo M. J. JNK signaling pathway regulates sorbitol-induced Tau proteolysis and apoptosis in SH-SY5Y cells by targeting caspase-3. Arch Biochem Biophys. 2017. № 15. V. 636. P. 42-49.
21. Lou M., Zhang L. N., Ji P. G., Feng F. Q., Liu J. H., Yang C., Li B. F., Wang L. Quercetin nanoparticles induced autophagy and apoptosis through AKT/ERK/Caspase-3signaling pathway in human neuroglioma cells: In vitro and in vivo, Biomed Pharmacother. 2016. V. 84. P. 1-9.
22. Liu R., Shih T.-C., Deng X., Anwar L., Ahadi S., Kumaresan P., Lam K. S. Design, Synthesis, and Application of OB2C Combinatorial Peptide and Peptidomimetic Libraries, Methods Mol. Biol. 2015. V. 1248. P. 3-22.
23. Allaman-Pillet N., Oberson A., Schorderet D. F., BIRO1, a Cell-Permeable BH3 Peptide, Promotes Mitochondrial Fragmentation and Death of Retinoblastoma Cells, Mol. Cancer Res. 2015. V. 13. №1. P. 86-97.
24. Russo P., Arzani D., Trombino S., Falugi C. С-myc Down-Regulation Induces Apoptosis in Human Cancer Cell Lines Exposed to RPR-115135 (C31H29NO4), a Non-Peptidomimetic Farnesyltransferase Inhibitor, The journal of pharmacology and experimental therapeutics. 2003. V. 304. P. 37-47.
Review
For citations:
Kokareva E.S., Morozov V.V., Stanishevskiy Ya.M., Zhuravleva M.A., Zubkov A.V. RESEARCH ON THE INFLUENCE OF VARIOUS SUBSTANCES ON CASPASE ACTIVITY (REVIEW). Drug development & registration. 2018;(4):29-36. (In Russ.)