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  • Preliminary analyses of these identified two bands for MALDI

    2022-08-04

    Preliminary analyses of these identified two bands for MALDI-TOF/TOF have shown the presence of approximately 20 proteins, most of which have not yet been characterized. However, several proteins, such as cytochrome c oxidase [53], peroxiredoin II E [54] and alcohol dehydrogenase [55], have been identified which were previously found to be S-nitrosylated. However, more in-depth analyses will be necessary to corroborate the identification of these proteins in pepper fruits.
    Conclusion Pepper Heparin ripening is characterized by drastic changes at the phenotypic and biochemical level. Nitric oxide and related molecules (reactive nitrogen species, RNS) are involved in many physiological processes. Previously, it has been shown that NO content decreases during pepper fruit ripening, accompanied by an increase in nitrated proteins, with catalase being a prominent target with lower activity in red pepper [3]. These data suggested the presence of nitro-oxidative stress similar to that observed in other organs such as leaves and roots during senescence [31], [56] The decrease in GSNOR activity observed during ripening is very much in line with the increase observed in protein S-nitrosylated proteins, which can be an excellent reservoir of NO acting as a mechanism to regulate the function of target proteins. Fig. 3 depicts a proposed model for the involvement of RNS in the ripening of pepper fruits, in which the important role played by NO metabolism in this process is summarized. This process is characterized by a general increase in protein nitration [3] and S-nitrosylation, with a decline being observed in GSNO reductase activity during the transition from the green to the red pepper stage. This is a new clue to understanding the involvement of NO in the fruit ripening mechanism, which could have biotechnological applications in the field of post-harvest technologies as the application of exogenous NO in low doses can delay fruit ripening [57], [58]. Nevertheless, a more in-depth study of the endogenous NO metabolism is required to advance our knowledge of these processes.
    Acknowledgment This work was supported by the ERDF-cofinanced grant from the Ministry of Economy and Competitiveness (AGL2015-65104-P) and Junta de Andalucía (group BIO192), Spain. M.R.R acknowledges an FPI fellowship from the Ministry of Science and Innovation, Spain (AGL2011-26044). Proteomic analyses were performed at the “Servicio Central de Apoyo a la Investigación” (SCAI, University of Córdoba, Spain). The technical assistance of Carmelo Ruiz-Torres and María J. Campos is also acknowledged.
    Introduction Nitric oxide (NO) affects the functions of a wide range of proteins through S-nitrosylation, the covalent modification of cysteine thiols [1]. Protein S-nitrosylation is increased by NO synthases (NOSs) but down-regulated by S-nitrosoglutathione reductase (GSNOR), a ubiquitous and highly conserved denitrosylase [2], [3], [4]. By preventing excessive protein S-nitrosylation, GSNOR plays an evolutionarily conserved, critical role in protecting against nitrosative stress [2], [3]. Studies of GSNOR-deficient (GSNOR−/−) mice have shown that GSNOR deficiency results in protection from asthma and myocardial infarction but also leads to increased susceptibility to septic shock, liver cancer, and lymphopenia [3], [4], [5], [6], [7], [8]. Accumulating evidence in humans and animals suggest important roles of S-nitrosothiols (SNOs) in lung. S-nitrosoglutathione (GSNO) may represent a major source of bronchodilatory NO bioactivity [9] and it is reportedly depleted from airway lining fluid in human asthmatics [10], [11]. Reduction in airway GSNO has been reported to be associated with increased GSNOR activity [12]. Single nucleotide polymorphisms in the human GSNOR gene have been linked to increased risk of asthma and decreased responsiveness to β-agonist therapy in asthmatics [13], [14], [15]. GSNOR deficiency protects mice from airway hyper responsiveness Heparin in experimental asthma [5]. In addition, GSNO may increase expression and maturation of wild-type and ΔF508 mutant cystic fibrosis transmembrane conductance regulatory protein [16], [17].