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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 383, Issue 3-4

Issues

Nitric Oxide and Cell Signaling Pathways in Mitochondrial-Dependent Apoptosis

C.S. Boyd / E. Cadenas
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.045

Abstract

Nitric oxide, generated by endogenous nitric oxide synthases or nitric oxide donors, can promote or prevent apoptosis induced by diverse proapoptotic stimuli in cell culture models. Both mitochondrialdependent and independent apoptotic signaling pathways mediate this dichotomous cellular response to nitric oxide. The molecular mechanisms behind these effects are complex and involve a number of nitrogen oxiderelated species that are more reactive than nitric oxide itself. The local cellular environment plays a dynamic role in determining the nature and concentration of these species. Important components of the microenvironment include: the cellular redox state, glutathione, transition metals and the presence of other oxygen and nitrogencentered radicals. In particular, redoxsensitive nitrosating species are favorably generated under physiological conditions and capable of modifying multiple cell signaling pathways through reversible Snitrosation reactions. Cytochrome c release from mitochondria is an important mechanism for the activation of caspase-3 and the initiation of cell death in response to intrinsic proapoptotic stimuli, including oxidative and nitrosative stress. In turn, caspases and mitogen associated protein kinases may modulate cytochrome c release through their effects on the Bcl-2 family of proteins. This review will focus on (i) the importance of the cellular environment in determining the fate of nitric oxide and (ii) the ability of Snitrosation to regulate mitochondrialdependent apoptosis at the level of mitochondrial bioenergetics, cytochrome c release, caspases, mitogen associated protein kinases, and the Bcl-2 family of proteins.

About the article

Published Online: 2005-06-01

Published in Print: 2002-04-12


Citation Information: Biological Chemistry, Volume 383, Issue 3-4, Pages 411–423, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.045.

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