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N-Acetylcysteine Serves as Substrate of 3-Mercaptopyruvate Sulfurtransferase and Stimulates Sulfide Metabolism in Colon Cancer Cells

1
Department of Biochemical Sciences, Sapienza University of Rome, Piazzale Aldo Moro 5, I-00185 Rome, Italy
2
CNR Institute of Molecular Biology and Pathology, Piazzale Aldo Moro 5, I-00185 Rome, Italy
3
Instituto de Tecnologia Química e Biológica António Xavier (ITQB NOVA), Avenida da República (EAN), 2780-157 Oeiras, Portugal
*
Authors to whom correspondence should be addressed.
Cells 2019, 8(8), 828; https://doi.org/10.3390/cells8080828
Received: 9 July 2019 / Revised: 31 July 2019 / Accepted: 2 August 2019 / Published: 4 August 2019
(This article belongs to the Special Issue Mitochondrial Bioenergetics in Cancer Cell Biology)
Hydrogen sulfide (H2S) is an endogenously produced signaling molecule. The enzymes 3-mercaptopyruvate sulfurtransferase (MST), partly localized in mitochondria, and the inner mitochondrial membrane-associated sulfide:quinone oxidoreductase (SQR), besides being respectively involved in the synthesis and catabolism of H2S, generate sulfane sulfur species such as persulfides and polysulfides, currently recognized as mediating some of the H2S biological effects. Reprogramming of H2S metabolism was reported to support cellular proliferation and energy metabolism in cancer cells. As oxidative stress is a cancer hallmark and N-acetylcysteine (NAC) was recently suggested to act as an antioxidant by increasing intracellular levels of sulfane sulfur species, here we evaluated the effect of prolonged exposure to NAC on the H2S metabolism of SW480 colon cancer cells. Cells exposed to NAC for 24 h displayed increased expression and activity of MST and SQR. Furthermore, NAC was shown to: (i) persist at detectable levels inside the cells exposed to the drug for up to 24 h and (ii) sustain H2S synthesis by human MST more effectively than cysteine, as shown working on the isolated recombinant enzyme. We conclude that prolonged exposure of colon cancer cells to NAC stimulates H2S metabolism and that NAC can serve as a substrate for human MST. View Full-Text
Keywords: hydrogen sulfide; sulfane sulfur species; enzymatic activity assays; protein expression levels; antioxidants; colorectal cancer hydrogen sulfide; sulfane sulfur species; enzymatic activity assays; protein expression levels; antioxidants; colorectal cancer
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Zuhra, K.; Tomé, C.S.; Masi, L.; Giardina, G.; Paulini, G.; Malagrinò, F.; Forte, E.; Vicente, J.B.; Giuffrè, A. N-Acetylcysteine Serves as Substrate of 3-Mercaptopyruvate Sulfurtransferase and Stimulates Sulfide Metabolism in Colon Cancer Cells. Cells 2019, 8, 828.

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