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      Modulation of Nitrosative Stress via Glutathione-Dependent Formaldehyde Dehydrogenase and S-Nitrosoglutathione Reductase

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          Abstract

          Glutathione-dependent formaldehyde dehydrogenase (GFD) from Taiwanofungus camphorata plays important roles in formaldehyde detoxification and antioxidation. The enzyme is bifunctional. In addition to the GFD activity, it also functions as an effective S-nitrosoglutathione reductase (GSNOR) against nitrosative stress. We investigated the modulation of HEK (human embryonic kidney) 293T cells under nitrosative stress by transfecting a codon optimized GFD cDNA from Taiwanofungus camphorata (Tc-GFD- O) to these cells. The parental and transfected HEK 293T cells were then subjected to S-nitrosoglutathione treatment to induce nitrosative stress. The results showed that in Tc-GFD- O-transfected 293T cells, the expression and activity of GFD increased. Additionally, these cells under the nitrosative stress induced by S-nitrosoglutathione showed both higher viability and less apoptosis than the parental 293T cells. This finding suggests that the Tc-GFD- O in HEK 293T cells may provide a protective function under nitrosative stress.

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          Annexin V-affinity assay: a review on an apoptosis detection system based on phosphatidylserine exposure.

          Frans Ramaekers, Luc J.W. Nieland, Manon van Engeland … (1998)
          Apoptosis is a programmed, physiological mode of cell death that plays an important role in tissue homeostasis. Understanding of the basic mechanisms that underlie apoptosis will point to potentially new targets of therapeutic treatment of diseases that show an imbalance between cell proliferation and cell loss. In order to conduct such research, techniques and tools to reliably identify and enumerate death by apoptosis are essential. This review focuses on a novel technique to detect apoptosis by targeting for the loss of phospholipid asymmetry of the plasma membrane. It was recently shown that loss of plasma membrane asymmetry is an early event in apoptosis, independent of the cell type, resulting in the exposure of phosphatidylserine (PS) residues at the outer plasma membrane leaflet. Annexin V was shown to interact strongly and specifically with PS and can be used to detect apoptosis by targeting for the loss of plasma membrane asymmetry. Labeled annexin V can be applied both in flow cytometry and in light microscopy in both vital and fixed material by using appropriate protocols. The annexin V method is an extension to the current available methods. This review describes the basic mechanisms underlying the loss of membrane asymmetry during apoptosis and discusses the novel annexin V-binding assay.
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            Function of S-nitrosoglutathione reductase (GSNOR) in plant development and under biotic/abiotic stress.

            Marina Leterrier, Marina Leterrier, Mounira Chaki … (2011)
            During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC 1.2.1.1), catalyzes the NADH-dependent reduction of S-nitrosoglutathione (GSNO) and therefore was also designated as GSNO reductase. This finding has opened new aspects in the metabolism of nitric oxide (NO) and NO-derived molecules where GSNO is a key component. In this article, current knowledge of the involvement and potential function of this enzyme during plant development and under biotic/abiotic stress is briefly reviewed.
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              A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy.

              C Hagemeier, Stefan Bartoschek, Meike Goenrich … (2002)
              The formation of S-hydroxymethylglutathione from formaldehyde and glutathione is a central reaction in the consumption of the cytotoxin formaldehyde in some methylotrophic bacteria as well as in many other organisms. We describe here the discovery of an enzyme from Paracoccus denitrificans that accelerates this spontaneous condensation reaction. The rates of S-hydroxymethylglutathione formation and cleavage were determined under equilibrium conditions via two-dimensional proton exchange NMR spectroscopy. The pseudo first order rate constants k(1)* were estimated from the temperature dependence of the reaction and the signal to noise ratio of the uncatalyzed reaction. At 303 K and pH 6.0 k(1)* was found to be 0.02 s(-1) for the spontaneous reaction. A 10-fold increase of the rate constant was observed upon addition of cell extract from P. denitrificans grown in the presence of methanol corresponding to a specific activity of 35 units mg(-1). Extracts of cells grown in the presence of succinate revealed a lower specific activity of 11 units mg(-1). The enzyme catalyzing the conversion of formaldehyde and glutathione was purified and named glutathione-dependent formaldehyde-activating enzyme (Gfa). The gene gfa is located directly upstream of the gene for glutathione-dependent formaldehyde dehydrogenase, which catalyzes the subsequent oxidation of S-hydroxymethylglutathione. Putative proteins with sequence identity to Gfa from P. denitrificans are present also in Rhodobacter sphaeroides, Sinorhizobium meliloti, and Mesorhizobium loti.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 14 August 2014
                Publication date Collection: August 2014
                Volume: 15
                Issue: 8
                Pages: 14166-14179
                Affiliations
                [1 ]Department of Bioscience and Biotechnology and Center of Excellence for the Oceans, National Taiwan Ocean University, Keelung 202, Taiwan; E-Mail: huang_sara1208@ 123456yahoo.com.tw
                [2 ]Institute of Biotechnology, National Changhua University of Education, Changhua 500, Taiwan; E-Mail: kencf@ 123456cc.ncue.edu.tw
                [3 ]Department of Chemistry, Western Illinois University, Macomb, IL 61455, USA; E-Mails: L-Wen@ 123456wiu.edu (L.W.); J-Huang3@ 123456wiu.edu (J.-K.H.)
                Author notes
                [†]

                These authors contributed equally to this work.

                [* ]Author to whom correspondence should be addressed; E-Mail: B0220@ 123456mail.ntou.edu.tw ; Tel.: +886-2-2462-2192 (ext. 5513); Fax: +886-2-2462-2320.
                Article
                Publisher ID: ijms-15-14166
                DOI: 10.3390/ijms150814166
                PMC ID: 4159844
                PubMed ID: 25196517
                SO-VID: dca7c6a7-96d0-4b15-8e24-de7947c06b7f
                Copyright © © 2014 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 17 June 2014
                Date revision received : 28 July 2014
                Date accepted : 08 August 2014
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: taiwanofungus camphorata (formerly named antrodia camphorata),glutathione-dependent formaldehyde dehydrogenase (gfd),s-nitrosoglutathione (gsno),s-nitrosoglutathione reductase (gsnor)
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: taiwanofungus camphorata (formerly named antrodia camphorata), glutathione-dependent formaldehyde dehydrogenase (gfd), s-nitrosoglutathione (gsno), s-nitrosoglutathione reductase (gsnor)

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