China 
Africa 
Explore chapters and articles related to this topic
Genomic analysis for functional roles of thioredoxin reductases and their expressions in osteoarthritis
Published in Gary Bañuelos, Zhi-Qing Lin, Dongli Liang, Xue-bin Yin, Selenium Research for Environment and Human Health: Perspectives, Technologies and Advancements, 2019
However, a genomic analysis about TXNRD1, TXNRD2, and TXNRD3 is necessary to conduct to help understand the function roles of TrxRs comprehensively. In this study, results from GO enrichment analysis showed that TXNRD1, TXNRD2, and TXNRD3 mainly exert biological functions such as antioxidant activity, cell homeostasis, cell oxidant detoxification, and coenzyme binding, and are mainly involved in selenocompound metabolism, cysteine and methionine metabolism, NOD-like receptor signaling pathways, etc. These results are similar to those from previous studies. In the PPI network of TrxRs, TXNRD1 was the core protein, followed by TXNRD2 and TXN, which showed that TXNRD1 and TXNRD2 were key members in their family. TXN acts as a homodimer and is involved in many redox reactions. The encoded protein is active in the reversible S-nitrosylation of cysteines in certain proteins, which is part of the response to intracellular nitric oxide (Zhang et al. 2019, Kamal et al. 2016).
Nitric Oxide-Induced Tolerance in Plants under Adverse Environmental Conditions
Published in Hasanuzzaman Mirza, Nahar Kamrun, Fujita Masayuki, Oku Hirosuke, Tofazzal M. Islam, Approaches for Enhancing Abiotic Stress Tolerance in Plants, 2019
Neidiquele M. Silveira, Amedea B. Seabra, Eduardo C. Machado, John T. Hancock, Rafael V. Ribeiro
S-nitrosothiols (RSNOs) belong to an important group of NO• donors, and the most frequently used RSNOs in plants are S-nitrosoglutathione (GSNO) and S-nitroso-N-acetylpenicillamine (SNAP). Nonreductive decomposition of RSNOs leads to the formation of disulfides and release of NO•, which are dependent on light, temperature, the presence of metal ions (Cu2+), and pH (Hou et al., 1999). In addition, oxidized forms of endogenous NO• (such as N2O3) may react with the thiol group (SH) of cysteine residues (Cys) present in proteins, forming an S-nitrosothiol (SNO), a reaction called S-nitrosation or S-nitrosylation (Lindermayr et al., 2005; Aracena-Parks et al., 2006). Thus, RSNOs, such as GSNO, are the natural reservoir of NO• in biological systems, releasing free NO• during its degradation. The GSNO is an S-nitrosated derivative of the most abundant cellular thiol, the glutathione (GSH), which intracellular concentrations may be greater than 10 mM (Hancock and Whiteman, 2018). GSNO itself is not directly absorbed into cells; however, GSNO treatment does cause increases in cellular S-nitrosothiol levels under many conditions. It was hypothesized that GSNO decomposes in the extracellular space to release NO•, which is then able to diffuse across the cell membrane to S-nitrosate protein targets (Broniowska et al., 2013).
Clinical Effects of Pollution
Published in William J. Rea, Kalpana D. Patel, Reversibility of Chronic Disease and Hypersensitivity, Volume 5, 2017
William J. Rea, Kalpana D. Patel
Transglutaminase also cross-links proteins in the extracellular matrix, and therefore is important for wound healing, tissue remodeling, and stabilization of the extracellular matrix. Thus, autoimmunity to transglutaminase leads to destabilization of the microvilli lining the small intestines. Transglutaminase has 18 free cysteine residues which are targets for S-nitrosylation. A cysteine residue is also involved in the catalytic active site. A unique Ca2+-dependent mechanism regulates nitrosylation by NO, mediated by CysNO (S-nitrosocysteine). It was shown experimentally that up to 15 cysteines of transglutaminase were nitrosylated by CysNO in the presence of Ca2+, and this inhibited its enzymatic activity.1161
Cadmium stress in plants: A critical review of the effects, mechanisms, and tolerance strategies
Published in Critical Reviews in Environmental Science and Technology, 2022
Taoufik El Rasafi, Abdallah Oukarroum, Abdelmajid Haddioui, Hocheol Song, Eilhann E. Kwon, Nanthi Bolan, Filip M. G. Tack, Abin Sebastian, M. N. V. Prasad, Jörg Rinklebe
The effect of Cd mitigation on plants involves other mechanisms. It has been reported that the synthetized NO may bind with cysteine thiol and lead to its S-nitrosylation (Astier et al., 2012; Chmielowska-Bąk et al., 2014; Yu et al., 2012). Protein S-nitrosylation has a major role in plant immune control, response, and adaptation to various abiotic stresses (Astier et al., 2012; París et al., 2013). It has been documented that S-nitrosylation can regulate different plant proteins (e.g., peroxiredoxin II E [PrxII E], nonexpressor of pathogenesis-related gene 1 [NPR1], salicylic acid-binding protein 3 [SABP3], the transcription factor TGA1, and the NADPH oxidase AtRBOHD) responsible for signaling and regulating Cd stress (Astier et al., 2012; Chmielowska-Bąk et al., 2014; Rodriguez-Serrano et al., 2009; Spoel & Loake, 2011). Moreover, S-nitrosylation has been shown to modulate the antioxidant system (Wei et al., 2020) by activating various enzymes such as SOD, CAT, APX, and DHAR and help plants to program their cell death in presence of Cd (Nabi et al., 2019). Arasimowicz-Jelonek et al. (2012) demonstrated that NO induces cell death in yellow lupine (Lupinus luteus) roots under exposure of Cd.
Physiological and pathophysiological implications of hydrogen sulfide: a persuasion to change the fate of the dangerous molecule
Published in Journal of the Chinese Advanced Materials Society, 2018
Jan Mohammad Mir, Ram Charitra Maurya
The ER is the primary site of protein synthesis and folding. After being properly folded and disulfide bridged, proteins are trafficked to the Golgi apparatus. During disulfide bond formation, ROS are produced as a result of enzymatic electron transport from thiols to reduce oxygen and produce H2O2.[102] If proteins are misfolded, the unfolded protein response (UPR), which prevents the accumulation of misfolded proteins in the ER, triggers proapoptotic cascades. ER stress and oxidative stress are closely linked. ER stress increases the production of H2S, which sulfhydrates and inhibits protein tyrosine phosphatise (PTP). In turn, PTP inactivates protein kinase-like ER kinase (PERK), which inhibits global translation by phosphorylating elF2α. Thus, H2S regulates ER stress by inhibiting global translation. H2S-induced sulfhydration on cysteine residues of PTP protects the phosphatase from oxidative stress, in a similar manner to NO-induced S nitrosylation of PTP. It is possible that H2S may protect proteins from the highly oxidizing environment of the ER, where protein folding is regulated by redox and large amounts of ROS are produced.