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  • Although NO may act as the substrate

    2022-10-01

    Although, NO2− may act as the substrate for NO biosynthesis no strict correlation between NO2− fluctuation in roots and NO content was observed in tomato roots. As the culture period was prolonged NO2− concentration declined in control and m-Tyr exposed seedlings, and finally its concentration was slightly lower in treated roots. In GSNOR null mutants of Arabidopsis the increase in NO2− content appeared to be correlated with the raise in total nitroso species (SNO and N-nitroso products) concentration, suggesting a link between protein nitrosation and the nitrate assimilation pathway [53]. Tested NPAA stimulated O2- formation in tomato roots, similarly as previously was described after application of canavanine [30]. Increased level of O2- may be due to insufficient activity of SOD in m-Tyr exposed plants (unpublished data) or incorporation of m-Tyr into proteins may lead to misfolding of CVT 10216 receptor transport chain proteins as suggested for E. coli[54]. The enhancement in O2- generation correlated well to APF fluorescence; in root extracts of m-Tyr stressed plants ONOO− level was significantly higher than in the control. Considering ONOO− as the main oxidative agent responsible for protein nitration we are not surprised by increased content of 3-NT in roots of tomato exposed to m-Tyr. Enlargement of 3-NT formation was rapid and remained stable during m-Tyr application period and confirms other reports suggesting that accumulation of 3-NT is a common plant response to stress conditions [55]. In citrus plants Tyr nitration in leaves and roots after salt stress, treatment with NO or H2O2 were demonstrated [56], [57]. Our earlier observations indicated that supplementation of tomato roots with canavanine enriched 3-NT content just at the beginning of the culture period, after stress prolongation its level, although was increasing constantly, was significantly lower than in control plants. Proteomics research done on Arabidopsis infected with pathogen suggests that the peak of nitrated proteins is transient, and some mechanisms of its reversibility should exist [58]. Although, there is no doubt that, the primary mode of action of m-Tyr is linked to incorporation into proteins instead of Phe, based on our data, its phytotoxicity may be explained also by effect on ROS/RNS level and metabolism. In perspectives, research of phytohormonal regulation of root growth in m-Tyr treated plants would be of great interest, as a close relationship of NO and hormones was confirmed in physiological or stress conditions (see Refs. [51], [66] for review). Disturbances of RNS-phytohormonal (auxin/ethylene) homeostasis by application of allelopathic compounds was investigated only in our just recently published papers focused on mode of action of canavanine or farnesene [31], [50].
    Acknowledgments The work was performed during realization of the project financed by National Science Centre, Poland2014/13/B/NZ9/02074 given to AG and financial support for young scientist funded by WULS-SGGW no. 505-10-010200-L00329-99 given to OA. Authors are greatly thankful to L. Kubienová (Palacký University) for providing GSNOR antibodies, R. Bogatek for fruitful discussion during manuscript preparation and B. Godley for English correction.
    Introduction Nitric oxide (NO) is a small molecule that plays a vital role in a multitude of biological processes [1], [2]. As a neurotransmitter, NO participates versatilely in learning and memory in the nervous system [3]. For example, NO acts as retrograde messenger to induce long-term potentiation (LTP), a prominent form of synaptic plasticity, which is associated with memory formation in the hippocampus [4], [5]. The majority of NO bioactivity studies have focused on upstream regulation and NO synthesis controlled by nitric oxide synthases (NOSs) [6], [7], [8], [9]. However, little is known regarding downstream regulation and the effect of NO metabolism on learning and memory. In 1998, Jensen et al. reported that alcohol dehydrogenase class III (ADH III) blocks NO function by reducing S-nitrosoglutathione (GSNO) to NH3[10], and for this reason, ADH III is also named S-nitrosoglutathione reductase (GSNOR). GSNOR is highly conserved from bacteria to humans and is extensively expressed in organisms [11]. GSNO is the main reservoir for non-protein S-nitrosothiols (SNOs) [12] and temporally and spatially extends functions of the fragile NO. GSNO also induces S-nitrosation of protein cysteine thiols, a post-translational modification (PTM) [13], [14], to regulate protein functions such as enzyme activity, protein stability, and protein localization. GSNOR turnover significantly influences the level of whole-cell S-nitrosation [11], [15], [16], [17], [18]. Therefore, high specificity of GSNOR toward GSNO and regulation of S-nitrosation [11], [16] have established a direct relationship between GSNOR and NO metabolism. In addition to the general functions of NO in an organism [1], GSNOR is involved in the cardiovascular system [16], immune system [16], [19], and respiratory system [17], [20] by regulating NO metabolism. However, the role of GSNOR and NO metabolism in the nervous system remains poorly understood. Results have been shown that nitric oxide synthase (NOS) inhibition results in learning and memory defects [21]. Therefore, the present study was designed to determine the effect of GSNOR on learning and memory. GSNOR is the sole alcohol dehydrogenase isozyme in vertebrate brains, while the failure to detect any ethanol dehydrogenase activity makes its function in brains an interesting question [22].