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Montesanti G, Parisella ML, Garofalo G, et al. Nitrite as Direct S-Nitrosylating Agent of Kir2.1 Channels. Int Sch Res Notices. 2014;2014:517126doi: 10.1155/2014/517126.
Montesanti, G., Parisella, M. L., Garofalo, G., & Pellegrino, D. (2014). Nitrite as Direct S-Nitrosylating Agent of Kir2.1 Channels. International scholarly research notices, 2014517126. https://doi.org/10.1155/2014/517126
Montesanti, Gabriella, et al. "Nitrite as Direct S-Nitrosylating Agent of Kir2.1 Channels." International scholarly research notices vol. 2014 (2014): 517126. doi: https://doi.org/10.1155/2014/517126
Montesanti G, Parisella ML, Garofalo G, Pellegrino D. Nitrite as Direct S-Nitrosylating Agent of Kir2.1 Channels. Int Sch Res Notices. 2014 Jul 16;2014:517126. doi: 10.1155/2014/517126. eCollection 2014. PMID: 27379296; PMCID: PMC4897243.
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Int Sch Res Notices. 2014 Jul 16;2014:517126. doi: 10.1155/2014/517126. eCollection 2014.

Nitrite as Direct S-Nitrosylating Agent of Kir2.1 Channels.

International scholarly research notices

Gabriella Montesanti, Maria Laura Parisella, Giusi Garofalo, Daniela Pellegrino

Affiliations

  1. Department of Biology, Ecology and Earth Sciences (DiBEST), University of Calabria, Arcavacata di Rende, 87036 Cosenza, Italy.

PMID: 27379296 PMCID: PMC4897243 DOI: 10.1155/2014/517126

Abstract

Nitrite, a physiological nitric oxide (NO) storage form and an alternative way for NO generation, affects numerous biological processes through NO-dependent and independent pathways, including the S-nitrosylation of thiol-containing proteins. Mechanisms underlying these phenomena are not fully understood. The purpose of this study was to analyse in the rat heart (as prototype of mammalian heart) whether nitrite affects S-nitrosylation of cardiac proteins and the potential targets for S-nitrosylation. Rat hearts, perfused according to Langendorff, were exposed to nitrite. By Biotin Switch Method, we showed that nitrite treatment increased the degree of S-nitrosylation of a broad range of membrane proteins. Further analysis, conducted on subfractioned proteins, allowed us to identify a high level of nitrosylation in a small range of plasmalemmal proteins characterized by using an anti-Kir2.1 rabbit polyclonal antibody. We also verified that this effect of nitrite is preserved in the presence of the NO scavenger PTIO (2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl 3-oxide). Our results suggest, for the first time, that nitrite represents a direct S-nitrosylating agent in cardiac tissues and that inward-rectifier potassium ion channels (Kir2.1) are one of the targets. These observations are of relevance since they support the growing evidence that nitrite is not only a NO reserve but also a direct modulator of important functional cardiac proteins.

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