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MicroRNAs (miRNAs) are small RNAs that do not encode for proteins and play key roles in the regulation of gene expression. miRNAs are involved in a comprehensive range of biological processes such as cell cycle control, apoptosis, and several developmental and physiological processes. Oxidative stress can affect the expression levels of multiple miRNAs and, conversely, miRNAs may regulate the expression of redox sensors, alter critical components of the cellular antioxidants, interact with the proteasome, and affect DNA repair systems. The number of publications identifying redox-sensitive miRNAs has increased significantly over the last few years, and some miRNA targets such as Nrf2, SIRT1 and NF-κB have been identified. The complex interplay between miRNAs and ROS is discussed together with their role in myocardial ischemia-reperfusion injury and the potential use of circulating miRNAs as biomarkers of myocardial infarction. Detailed knowledge of redox-sensitive miRNAs is needed to be able to effectively use individual compounds or sets of miRNA-modulating compounds to improve the health-related outcomes associated with different diseases.

This research evaluates the effects of adding a tocopherol mix (0 or 200 mg/kg), two nitrite sources (sodium nitrite or a nitrate-rich vegetable concentrate) and the use of Staphylococcus carnosus together with fermentation types that varied in temperature (12 h at 4 ℃ or 16 ℃) on different quality parameters and acceptability of cooked cured sausages after vacuum packing and storage at 4 ℃ for 120 days. In the presence of S. carnosus, residual nitrate and nitrite levels were reduced. Sausages containing vegetable concentrates and without S. carnosus resulted in higher amounts of residual nitrate and lower curing efficiency. The lowest values in redness and acceptability were observed in those sausages without starter cultures. The addition of tocopherols had no effect on oxidative status and susceptibility to oxidation. However, the highest amount of hydroperoxides was related with nitrite decreased formation. Overall, vegetable concentrates can be used as curing agents if fermentation with a nitrate-reducing starter culture is allowed.

Fortification of food products with iron is a common strategy to prevent or overcome iron deficiency. However, any form of iron is a pro-oxidant and its addition will cause off-flavours and reduce a product's shelf life. A highly bioavailable heme iron ingredient was selected to fortify a chocolate cream used to fill sandwich-type cookies. Two different strategies were assessed for avoiding the heme iron catalytic effect on lipid oxidation: ascorbyl palmitate addition and co-spray-drying of heme iron with calcium caseinate. Oxidation development and sensory acceptability were monitored in the cookies over one-year of storage at room temperature in the dark. The addition of ascorbyl palmitate provided protection against oxidation and loss of tocopherols and tocotrienols during the preparation of cookies. In general, ascorbyl palmitate, either alone or in combination with the co-spray-dried heme iron, prevented primary oxidation and hexanal formation during storage. The combination of both strategies resulted in cookies that were acceptable from a sensory point of view after 1year of storage.

The plant pathogenic bacterium Ralstonia solanacearum injects more than 70 effector proteins (virulence factors) into the host plant cells via the needle-like structure of a type III secretion system. The type III secretion system effector proteins manipulate host regulatory networks to suppress defense responses with diverse molecular activities. Uncovering the molecular function of these effectors is essential for a mechanistic understanding of R. solanacearum pathogenicity. However, few of the effectors from R. solanacearum have been functionally characterized, and their plant targets remain largely unknown. Here, we show that the ChaC domain-containing effector RipAY/RSp1022 from R. solanacearum exhibits γ-glutamyl cyclotransferase (GGCT) activity to degrade the major intracellular redox buffer, glutathione. Heterologous expression of RipAY, but not other ChaC family proteins conserved in various organisms, caused growth inhibition of yeast Saccharomyces cerevisiae, and the intracellular glutathione level was decreased to ∼30% of the normal level following expression of RipAY in yeast. Although active site mutants of GGCT activity were non-toxic, the addition of glutathione did not reverse the toxicity, suggesting that the toxicity might be a consequence of activity against other γ-glutamyl compounds. Intriguingly, RipAY protein purified from a bacterial expression system did not exhibit any GGCT activity, whereas it exhibited robust GGCT activity upon its interaction with eukaryotic thioredoxins, which are important for intracellular redox homeostasis during bacterial infection in plants. Our results suggest that RipAY has evolved to sense the host intracellular redox environment, which triggers its enzymatic activity to create a favorable environment for R. solanacearum infection., This work was supported by Japan Society for the Promotion of Science KAKENHI Grants 22580095 and 25450104 and also, in part, by the General Research Grant of the Institute of Fermentation, Osaka.

Fortification of food products with non-heme or heme iron is a common strategy to overcome nutritional iron deficiency. Heme iron is highly bioavailable but it promotes oxidation, as do other iron forms. Palm oil is widely used in the formulation of bakery products and chocolate fillings. The work reported here aims to delay the onset of oxidation of a palm oil matrix fortified with heme iron, as a model for bakery products, through the use of ascorbyl palmitate (0 and 400 mg/kg) and the co-spray-drying of the heme iron with calcium caseinate in two ratios (heme iron concentrate:caseinate, 2:1 and 1:1, w/w). Primary (peroxide value and lipid hydroperoxide content) and secondary (p-anisidine value and hexanal content) oxidation were measured over one year of storage at room temperature in the dark. The combination of ascorbyl palmitate at 400 mg/kg and the co-spray-dried heme iron in a 1:1 ratio was the treatment that best protected iron fortified samples from oxidation during the storage time. Practical applications: Food fortification with iron has been suggested as a good strategy for overcoming iron deficiency. In this study, a heme iron ingredient has been selected due to its higher bioavailability than inorganic iron forms. Nevertheless, as other iron forms, heme iron is a potent pro-oxidant, which may affect the nutritional value, the sensory properties and shelf life of the fortified product. Thus, in this study the co-spray-drying of the heme iron with several coatings was assessed in order to reduce its pro-oxidant activity. The different heme irons were mixed with palm oil, which is a fat widely used in bakery. The combination of co-spray-dried heme iron and ascorbyl palmitate delayed the onset of oxidation, which demonstrates its effectiveness in future iron fortified bakery products. Palm oil is widely used in the formulation of bakery products and chocolate fillings. Therefore, this matrix can be a useful model for iron fortification in bakery products. In a preliminary study with heme iron fortified sunflower oil, the co-spray-drying of heme iron with different coating agents delayed the oxidation onset during accelerated storage at 60°C (see the figure).The combination of ascorbyl palmitate and the co-spray-drying of heme iron with calcium caseinate at 1:1 ratio (CAS 1:1) prevented oxidation of a heme iron fortified palm oil during storage at room temperature in the dark for one year.

Carnitine palmitoyltransferase 1 (CPT1) catalyzes the first step in long-chain fatty acid import into mitochondria, and it is believed to be rate limiting for beta-oxidation of fatty acids. However, in muscle, other proteins may collaborate with CPT1. Fatty acid translocase/CD36 (FAT/CD36) may interact with CPT1 and contribute to fatty acid import into mitochondria in muscle. Here, we demonstrate that another membrane-bound fatty acid binding protein, fatty acid transport protein 1 (FATP1), collaborates with CPT1 for fatty acid import into mitochondria. Overexpression of FATP1 using adenovirus in L6E9 myotubes increased both fatty acid oxidation and palmitate esterification into triacylglycerides. Moreover, immunocytochemistry assays in transfected L6E9 myotubes showed that FATP1 was present in mitochondria and coimmunoprecipitated with CPT1 in L6E9 myotubes and rat skeletal muscle in vivo. The cooverexpression of FATP1 and CPT1 also enhanced mitochondrial fatty acid oxidation, similar to the cooverexpression of FAT/CD36 and CPT1. However, etomoxir, an irreversible inhibitor of CPT1, blocked all these effects. These data reveal that FATP1, like FAT/CD36, is associated with mitochondria and has a role in mitochondrial oxidation of fatty acids.

Significance: Current lifestyles with high-energy diets and little exercise are triggering an alarming growth in obesity. Excess of adiposity is leading to severe increases in associated pathologies, such as insulin resistance, type 2 diabetes, atherosclerosis, cancer, arthritis, asthma, and hypertension. This, together with the lack of efficient obesity drugs, is the driving force behind much research. Recent Advances: Traditional anti-obesity strategies focused on reducing food intake and increasing physical activity. However, recent results suggest that enhancing cellular energy expenditure may be an attractive alternative therapy. Critical Issues: This review evaluates recent discoveries regarding mitochondrial fatty acid oxidation (FAO) and its potential as a therapy for obesity. We focus on the still controversial beneficial effects of increased FAO in liver and muscle, recent studies on how to potentiate adipose tissue energy expenditure, and the different hypotheses involving FAO and the reactive oxygen species production in the hypothalamic control of food intake. Future Directions: The present review aims to provide an overview of novel anti-obesity strategies that target mitochondrial FAO and that will definitively be of high interest in the future research to fight against obesity-related disorders. Antioxid. Redox Signal. 00, 000000.

This is a copy of an article published in the Antioxidants & Redox Signaling © Mary Ann Liebert, Inc. Antioxidants & Redox Signaling is available online at http://online.liebertpub.com, Cysteine oxidation mediates oxidative stress toxicity and signaling. It has been long proposed that the thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (Trr), is not only involved in recycling classical Trx substrates, such as ribonucleotide reductase, but it also regulates general cytoplasmic thiol homeostasis. To investigate such a role, we have performed a proteome-wide analysis of cells expressing or not the two components of the Trx system. We have compared the reversibly oxidized thiol proteomes of wild-type Schizosaccharomyces pombe cells with mutants lacking Trx or Trr. Specific Trx substrates are reversibly-oxidized in both strain backgrounds; however, in the absence of Trr, Trx can weakly recycle its substrates at the expense of an alternative electron donor. A massive thiol oxidation occurs only in cells lacking Trr, with 30% of all cysteinecontaining peptides being reversibly oxidized; this oxidized cysteine proteome depends on the presence of Trxs. Our observations lead to the hypothesis that, in the absence of its reductase, the natural electron donor Trx becomes a powerful oxidant and triggers general thiol oxidation., This work was supported by the Spanish Ministry of Science and Innovation (BFU2009-06933 and BFU2012-32045), PLAN E and FEDER, by the Spanish program Consolider- Ingenio 2010 Grant CSD 2007-0020, and by SGR2009-196 from Generalitat de Catalunya (Spain) to E.H. E. H. and J.A. are recipients of ICREA Academia Awards (Generalitat de Catalunya).

12 páginas, 6 figuras, 6 tablas., Submersed vegetation is a common feature in about 70% Pyrenean high mountain (>1500 m a.s.l.) lakes. Isoetids and soft-water elodeids are common elements of this underwater flora and can form distinct vegetation units (i.e. patches of vegetation dominated by different species) within complex mosaics of vegetation in shallow waters (, This study was funded by the Red de Parques Nacionales of the Spanish Ministry of the Environment (ref. 118/2003).

30 p.-9 fig.-2 tab.-10 fig. supl.-3 tab. supl., A dye-decolorizing peroxidase (DyP) from Pleurotus ostreatus (PosDyP4) catalyzes the oxidation of Mn2+ to Mn3+, in the presence of H2O2, with an efficiency similar to the well-known manganese peroxidases and versatile peroxidases from this and other white-rot fungi. PosDyP4 has been overexpressed in Escherichia coli as an active enzyme, and its crystal structure has been solved at 1.56 Å resolution. A combination of substrate diffusion simulations on the solved structure using the PELE software, electron paramagnetic resonance, and site-directed mutagenesis led to identification of the residues involved in Mn2+ oxidation. The oxidation site in PosDyP4 is different than the conserved site in the other Mn-oxidizing peroxidases mentioned above, and it includes four acidic residues (three aspartates and one glutamate) located at the surface of the protein. Moreover, since the Mn2+ ion is not in direct contact with the heme propionates, a tyrosine residue participates in the electron transfer to the cofactor, being the only essential individual residue for PosDyP4 oxidation of the metal ion. The four acidic residues contribute to Mn2+ binding in different extents, with the glutamate also involved in the initial electron transfer to the key tyrosine, as confirmed by the >50-fold decreased kcat after removing its side-chain carboxylic group. A second electron transfer pathway operates in PosDyP4 for the oxidation of aromatics and dyes starting at a surface tryptophan, as reported in other fungal and prokaryotic DyPs, and connecting with the final part of the Mn2+ oxidation route. Both tryptophanyl and tyrosyl radicals, potentially involved in catalysis, were detected by electron paramagnetic resonance of the native enzyme and its tryptophan-less variant, respectively., This work has been funded by the H2020 BBIJU (www.bbi-europe.eu) project EnzOx2 (BBIPPP-2015-2-720297; www.enzox2.eu) and the FP7 project INDOX (KBBE 2013-7-613549; www.indoxproject.eu), together with the BIO2014-56388-R (NOESIS), BFU2016-77835-R, CTQ2016-79138-R and (BIO2017-86559-R (GENOBIOREF) projects of the Spanish Ministry of Economy, Industry and Competitiveness, cofinanced by FEDER funds.The sequencing of P. ostreatus genome at JGI was supported by the DOE Office of Science, under Contract No. DE-AC02-05CH11231. We thank the staff of the ID30B beamline at ESRF(Grenoble, France) for assistance. CSGI (Florence, Italy) FFABR 2017 (Legge 232/2016 Comma 295, and Legge di Bilancio 2017) and MIUR (Dipartimento di Eccellenza, 2018-2022) grants are acknowledged for financial support.