Peroxidatic cysteine residue of peroxiredoxin 2 separated from human red blood cells treated by tert-butyl hydroperoxide is hyperoxidized into sulfinic and sulfonic acids

Ishida, Yoichi; Aki, Mariko; Fujiwara, Sohta; Nagahama, Masami; Ogasawara, Yuki

doi:10.1007/s13577-017-0171-0

Cited by 8 publications

(7 citation statements)

References 35 publications

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“…At higher levels of ROS, sulfenic acid undergoes further oxidation to sulfinic (-SO 2 H) or sulfonic (-SO 3 H) acid. Unlike sulfenic modification, sulfinic or sulfonic moieties are irreversible modifications, resulting in permanent damage of the protein, and are considered, in addition to protein carbonylation, markers of oxidative stress. , Interestingly, the above-described biochemical mechanisms enacted by ROS, in relation to their concentration, can produce a reversible modification of the function of a protein or induce an irreversible inactivation.…”

Section: Role Of the Intracellular Redox State In The Control Of Phys...mentioning

confidence: 99%

The Double-Edged Sword Profile of Redox Signaling: Oxidative Events As Molecular Switches in the Balance between Cell Physiology and Cancer

Emanuele

D’Anneo

Calvaruso

et al. 2018

Chem. Res. Toxicol.

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The intracellular redox state in the cell depends on the balance between the level of reactive oxygen species (ROS) and the activity of defensive systems including antioxidant enzymes. This balance is a dynamic process that can change in relation to many factors and/or stimuli induced within the cell. ROS production is derived from physiological metabolic events. For instance, mitochondria represent the major ROS sources during oxidative phosphorylation, but other systems, such as NADPH oxidase or specific enzymes in certain metabolisms, may account for ROS production as well. Whereas high levels of ROS perturb the cell environment, causing oxidative damage to biological macromolecules, low levels of ROS can exert a functional role in the cell, influencing the activity of specific enzymes or modulating some intracellular signaling cascades. Of particular interest appears to be the role of ROS in tumor systems not only because ROS are known to be tumorigenic but also because tumor cells are able to modify their redox state, regulating ROS production to sustain tumor growth and proliferation. Overall, the scope of this review was to critically discuss the most recent findings pertaining to ROS physiological roles as well as to highlight the controversial involvement of ROS in tumor systems.

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Section: Role Of the Intracellular Redox State In The Control Of Phys...mentioning

confidence: 99%

The Double-Edged Sword Profile of Redox Signaling: Oxidative Events As Molecular Switches in the Balance between Cell Physiology and Cancer

Emanuele

D’Anneo

Calvaruso

et al. 2018

Chem. Res. Toxicol.

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“…We previously established a method for the separation and detection of Prx2-SO 2/3 and reduced Prx2 [ 18 , 25 ]. Our method revealed that more hyperoxidized Prx2-SO 3 eluted faster than reduced Prx2.…”

Section: Discussionmentioning

confidence: 99%

Hyperoxidized Peroxiredoxin 2 Is a Possible Biomarker for the Diagnosis of Obstructive Sleep Apnea

et al. 2022

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Peroxiredoxin (Prx) 2 in red blood cells (RBCs) reacts with various reactive oxygen species and changes to hyperoxidized Prx2 (Prx2-SO2/3). Therefore, Prx2 may serve as an indicator of oxidative stress in vivo. This study aimed to analyze Prx2-SO2/3 levels in clinical samples to examine whether the oxidation state of Prx2 in human RBCs reflects the pathological condition of oxidative stress diseases. We first focused on obstructive sleep apnea (OSA), a hypoxic stress-induced disease of the respiratory system, and investigated the levels of Prx2-SO2/3 accumulated in the RBCs of OSA patients. In measurements on a small number of OSA patients and healthy subjects, levels of Prx2-SO2/3 accumulation in patients with OSA were clearly increased compared to those in healthy subjects. Hence, we proceeded to validate these findings with more samples collected from patients with OSA. The results revealed significantly higher levels of erythrocytic Prx2-SO2/3 in patients with OSA than in healthy subjects, as well as a positive correlation between the severity of OSA and Prx2-SO2/3 levels in the RBCs. Moreover, we performed a chromatographic study to show the structural changes of Prx2 due to hyperoxidation. Our findings demonstrated that the Prx2-SO2/3 molecules in RBCs from patients with OSA were considerably more hydrophilic than the reduced form of Prx2. These results implicate Prx2-SO2/3 as a promising candidate biomarker for OSA.

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“…The protein bands of interest were excised and subjected to in-gel digestion for mass spectrometric analysis as described previously 18,19) . The gel pieces were then destained, reduced with dithiothreitol, alkylated with iodoacetamide, and incubated in digestion buffer [50 mM NH4HCO3, 2 μM trypsin (Trypsin Gold; Promega, Madison, WI, USA) and 0.…”

Section: Identification Of Heparin-binding Proteinsmentioning

confidence: 99%

Identification of Heparin-binding Proteins on the Cell Surface of <I>Cryptococcus neoformans</I>

Ikeda

Ichikawa

Tsukiji

et al. 2018

Medical Mycology Journal

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Interactions between virulence factors of pathogens and host responses play an important role in the establishment of infection by microbes. We focused on interactions between Cryptococcus neoformans proteins and heparin, which is abundant on host epithelial cells. Surface proteins were extracted and analyzed. Fractions from anion-exchange column chromatography interacted with heparin in surface plasmon resonance analyses. Heparin-binding proteins were purified and then separated by gel electrophoresis; and were identified as transaldolase, glutathione-disulfide reductase, and glyoxal oxidase. These results imply that multifunctional molecules on C. neoformans cells, such as those involved in heparin binding, may play roles in adhesion that trigger responses in the host.

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Peroxidatic cysteine residue of peroxiredoxin 2 separated from human red blood cells treated by tert-butyl hydroperoxide is hyperoxidized into sulfinic and sulfonic acids

Cited by 8 publications

References 35 publications

The Double-Edged Sword Profile of Redox Signaling: Oxidative Events As Molecular Switches in the Balance between Cell Physiology and Cancer

The Double-Edged Sword Profile of Redox Signaling: Oxidative Events As Molecular Switches in the Balance between Cell Physiology and Cancer

Hyperoxidized Peroxiredoxin 2 Is a Possible Biomarker for the Diagnosis of Obstructive Sleep Apnea

Identification of Heparin-binding Proteins on the Cell Surface of <I>Cryptococcus neoformans</I>

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