Email this article 
INTRACELLULAR TARGETS OF PROAPOPTOTIC INFLUENCE OF GASEOUS TRANSMITTERS
- Authors: Tashireva L.A.1, Starikova E.G.1, Novitskii V.V.1, Ryazantseva N.V.1
-
Affiliations:
- Siberian State Medical University, Tomsk
- Issue: Vol 67, No 10 (2012)
- Pages: 77-81
- Section: SHORT MESSAGES
- Published: 10.10.2012
- URL: https://vestnikramn.spr-journal.ru/jour/article/view/260
- DOI: https://doi.org/10.15690/vramn.v67i10.420
- ID: 260
Cite item
Full Text
Abstract
Main molecular targets of nitric oxide, hydrogen sulfide and carbon monoxide proapoptotic action in Jurkat cells were determined in this study. Decrease of mitochondrial transmembrane potential was shown during all three gases action. Reason of this event is the Bcl-2 family members disbalance. Proapoptotic proteins release after mitochondrion membranes permeabilisation could be abolished by protein xIAP inhibition of caspase -9 and-3 activity during NO and CO application.
Keywords
About the authors
L. A. Tashireva
Siberian State Medical University, Tomsk
Author for correspondence.
Email: lkleptsova@mail.ru
аспирант кафедры патофизиологии ГБОУ ВПО СибГМУ МЗ РФ Адрес: 634050, Томск, Московский тракт, д. 2 Тел.: (3822) 66-30-50 Россия
E. G. Starikova
Siberian State Medical University, Tomsk
Email: to-elen@yandex.ru
кандидат медицинских наук, докторант кафедры патофизиологии ГБОУ ВПО СибГМУ МЗ РФ Адрес: 634050, Томск, Московский тракт, д. 2 Тел.: (3822) 24-37-81 Россия
V. V. Novitskii
Siberian State Medical University, Tomsk
Email: office@ssmu.ru
академик РАМН, профессор, заведующий кафедрой патофизиологии ГБОУ ВПО СибГМУ МЗ РФ Адрес: 634050, Томск, Московский тракт, д. 2 Тел.: (3822) 53-04-23 Россия
N. V. Ryazantseva
Siberian State Medical University, Tomsk
Email: strateg@ssmu.ru
доктор медицинских наук, профессор, заведующая кафедрой фундаментальных основ клинической медицины ГБОУ ВПО СибГМУ МЗ РФ Адрес: 634050, Томск, Московский тракт, д. 2 Тел.: (3822) 52-77-47 Россия
References
- Martinou J.C., Youle R.J. Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Dev. Cell. 2011; 21 (1): 92–101.
- Chau B.N., Cheng E.H., Kerr D.A., Hardwick J.M. Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1. Mol. Cell. 2000; 6 (1): 31–40.
- Smolewski P., Robak T. Inhibitors of apoptosis proteins (IAPs) as potential molecular targets for therapy of hematological malignancies. Curr. Mol. Med. 2011; 11 (8): 633–649.
- Olsson M., Zhivotovsky B. Caspases and cancer. Cell Death Differ. 2011; 18 (9): 41–49.
- Starikova E.G., Ryazantseva N.V., Novitskii V.V., Tashireva L.A., Starikov Yu.V., Stepovaya E.A., Osikhov I.A., Vasil'eva O.A., Yakushina V.D. The role of intracellular gaseous transmitters hydrogen sulfide and nitric oxide in apoptosis regulation of normal and blast cells. Byulleten' sibirskoi meditsiny = Bulletin of siberian medicine. 2011; 6: 40–44.
- Skovgaard N., Gouliaev A., Aalling M., Simonsen U. The role of endogenous H2S in cardiovascular physiology. Curr. Pharm. Biotechnol. 2011; 12 (9): 1385–1393.
- García-Sáez A.J., Fuertes G., Suckale J., Salgado J. Permeabilization of the outer mitochondrial membrane by Bcl-2 proteins. Adv. Exp. Med. Biol. 2010; 677: 91–105.
- Azad N., Vallyathan V., Wang L., Tantishaiyakul V., Stehlik C., Leonard S.S., Rojanasakul Y. S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. J. Biol. Chem. 2006; 281 (45): 34124–34134.
- Yang G.D., Wang R. H2S and cellular proliferation and apoptosis. Sheng Li Xue Bao. 2007; 59 (2): 133–140.
- Mustafa A.K., Gadalla M.M., Sen N., Kim S., Mu W., Gazi S.K., Barrow R.K., Yang G., Wang R., Snyder S.H. H2S signals through protein S-sulfhydration. Sci. Signal. 2009; 2 (96): 72.
- Bertini I., Chevance S., Del Conte R., Lalli D., Turano P. The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. PLoS One. 2011; 6 (4): 18329–18336.
- Elkholi R., Floros K.V., Chipuk J.E. The role of BH3-only proteins in tumor cell development, signaling, and treatment. Genes Cancer. 2011; 2 (5): 523–537.
Supplementary files
