Disulfide stress: a novel type of oxidative stress in acute pancreatitis

Sancho, Mari Luz Moreno; Escobar, Javier; Izquierdo-Álvarez, Alicia; Gil, Anabel; Pérez, Salvador; Pereda, Javier; Zapico, Inés; Vento, Máximo; Sabater, Luís; Marina, Anabel; Martínez‐Ruiz, Antonio; Sastre, Juan

doi:10.1016/j.freeradbiomed.2014.01.009

Cited by 64 publications

(64 citation statements)

References 53 publications

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“…The desalted protein digest was dried, resuspended in 10 µL of 0.1% formic acid and analyzed by RP-LC-MS/MS in an Easy-nLC II system coupled to an ion trap LTQ-Orbitrap-Velos-Pro mass spectrometer (Thermo Scientific), as previously described [40] with minor modifications. The peptides were concentrated (on-line) by reverse phase chromatography using a 0.1 mm×20 mm C18 RP precolumn (Proxeon), and then separated using a 0.075 mm×250 mm C18 RP column (Proxeon) operating at 0.3 µL/min.…”

Section: Methodsmentioning

confidence: 99%

Mitochondrial complex I deactivation is related to superoxide production in acute hypoxia

et al. 2017

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Mitochondria use oxygen as the final acceptor of the respiratory chain, but its incomplete reduction can also produce reactive oxygen species (ROS), especially superoxide. Acute hypoxia produces a superoxide burst in different cell types, but the triggering mechanism is still unknown. Herein, we show that complex I is involved in this superoxide burst under acute hypoxia in endothelial cells. We have also studied the possible mechanisms by which complex I could be involved in this burst, discarding reverse electron transport in complex I and the implication of PTEN-induced putative kinase 1 (PINK1). We show that complex I transition from the active to ‘deactive’ form is enhanced by acute hypoxia in endothelial cells and brain tissue, and we suggest that it can trigger ROS production through its Na+/H+ antiporter activity. These results highlight the role of complex I as a key actor in redox signalling in acute hypoxia.

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Section: Methodsmentioning

confidence: 99%

Mitochondrial complex I deactivation is related to superoxide production in acute hypoxia

et al. 2017

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“…Protein quantification of supernatants was determined using the MicroBCA Protein Assay Kit (ThermoFisher, Waltham, MA). Analysis was performed with high‐performance liquid chromatography coupled with tandem mass spectrometry (LC‐MS/MS) (Moreno et al., ; Shevchenko, Wilm, Vorm, & Mann, ). Searches against the decoy database were done using a false discovery rate <0.01 (Alonso et al., ).…”

Section: Methodsmentioning

confidence: 99%

Missense mutations have unexpected consequences: The McArdle disease paradigm

et al. 2018

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McArdle disease is a disorder of muscle glycogen metabolism caused by mutations in the PYGM gene, encoding for the muscle-specific isoform of glycogen phosphorylase (M-GP). The activity of this enzyme is completely lost in patients' muscle biopsies, when measured with a standard biochemical test which, does not allow to determine M-GP protein levels. We aimed to determine M-GP protein levels in the muscle of McArdle patients, by studying biopsies of 40 patients harboring a broad spectrum of PYGM mutations and 22 controls. Lack of M-GP protein was found in muscle in the vast majority (95%) of patients, irrespective of the PYGM genotype, including those carrying missense mutations, with few exceptions. M-GP protein biosynthesis is not being produced by PYGM mutations inducing premature termination codons (PTC), neither by most PYGM missense mutations. These findings explain the lack of PYGM genotype-phenotype correlation and have important implications for the design of molecular-based therapeutic approaches.

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“…Similarly, overproduction of RI can protect cells against the effects of oxidative stress[22]. In vivo , oxidation of RI has been linked to the progression of pancreatitis [23], as well as to the effectiveness of certain cancer treatments [24]. Intriguingly, RI is present in red blood cells, which contain neither a nucleus nor an RNA.…”

Section: Introductionmentioning

confidence: 99%

Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles

Lomax

Bianchetti

Chang

et al. 2014

Journal of Molecular Biology

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Ribonuclease inhibitor (RI) is a conserved protein of the mammalian cytosol. RI binds with high affinity to diverse secretory ribonucleases (RNases) and inhibits their enzymatic activity. Although secretory RNases are found in all vertebrates, the existence of a non-mammalian RI has been uncertain. Here, we report on the identification and characterization of RI homologs from chicken and anole lizard. These proteins bind to RNases from multiple species, but exhibit much greater affinity for their cognate RNases than for mammalian RNases. To reveal the basis for this differential affinity, we determined the crystal structure of mouse, bovine, and chicken RI·RNase complexes to a resolution of 2.20, 2.21, and 1.92 Å, respectively. A combination of structural, computational, and bioinformatic analyses enabled the identification of two residues that appear to contribute to the differential affinity for RNases. We also found marked differences in oxidative instability between mammalian and non-mammalian RIs, indicating evolution toward greater oxygen-sensitivity in RIs from mammalian species. Taken together, our results illuminate the structural and functional evolution of RI, along with its dynamic role in vertebrate biology.

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Disulfide stress: a novel type of oxidative stress in acute pancreatitis

Cited by 64 publications

References 53 publications

Mitochondrial complex I deactivation is related to superoxide production in acute hypoxia

Mitochondrial complex I deactivation is related to superoxide production in acute hypoxia

Missense mutations have unexpected consequences: The McArdle disease paradigm

Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles

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