scholarly journals Relation of Redox and Structural Alterations of Rat Skin in the Function of Chronological Aging

2019 ◽  
Vol 2019 ◽  
pp. 1-12 ◽  
Author(s):  
Aleksandra Jankovic ◽  
Luciano Saso ◽  
Aleksandra Korac ◽  
Bato Korac
Keyword(s):  
Oxidative Damage ◽  
Thioredoxin Reductase ◽  
Methionine Sulfoxide ◽  
Skin Aging ◽  
Methionine Sulfoxide Reductase ◽  
Ultrastructural Changes ◽  
Rat Skin ◽  
Compensatory Response ◽  
Chronological Aging ◽  
Skin Development

Accumulation of oxidative insults on molecular and supramolecular levels could compromise renewal potency and architecture in the aging skin. To examine and compare morphological and ultrastructural changes with redox alterations during chronological skin aging, activities of antioxidant defense (AD) enzymes, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GR), thioredoxin reductase (TR), and methionine sulfoxide reductase A (MsrA), and the markers of oxidative damage of biomolecules—4-hydroxynonenal (HNE) and 8-oxoguanine (8-oxoG)—were examined in the rat skin during life (from 3 days to 21 months). As compared to adult 3-month-old skin, higher activities of CAT, GSH-Px, and GR and a decline in expression of MsrA are found in 21-month-old skin. These changes correspond to degenerative changes at structural and ultrastructural levels in epidermal and dermal compartments, low proliferation capacity, and higher levels of HNE-modified protein aldehydes (particularly in basal lamina) and 8-oxoG positivity in nuclei and mitochondria in the sebaceous glands and root sheath. In 3-day-old skin, higher activities of AD enzymes (SOD, CAT, GR, and TR) and MsrA expression correspond to intensive postnatal development and proliferation. In contrast to 21-month-old skin, a high level of HNE in young skin is not accompanied by 8-oxoG positivity or any morphological disturbances. Observed results indicate that increased activity of AD enzymes in elderly rat skin represents the compensatory response to accumulated oxidative damage of DNA and proteins, accompanied by attenuated repair and proliferative capacity, but in young rats the redox changes are necessary and inherent with processes which occur during postnatal skin development. Мorphological and ultrastructurаl changes are in line with the redox profile in the skin of young and old rats.

scholarly journals Redox-mediated regulation of a labile, evolutionarily conserved cross-β structure formed by the TDP43 low complexity domain

2019 ◽  
Author(s):  
Yi Lin ◽  
Xiaoming Zhou ◽  
Masato Kato ◽  
Daifei Liu ◽  
Sina Ghaemmaghami ◽  
...  
Keyword(s):  
Rna Binding ◽  
Thioredoxin Reductase ◽  
Methionine Sulfoxide ◽  
Low Complexity ◽  
Methionine Sulfoxide Reductase ◽  
Methionine Residue ◽  
Low Concentrations ◽  
Evolutionarily Conserved ◽  
Methionine Residues ◽  
Self Association

SummaryAn evolutionarily conserved low complexity (LC) domain is found within a 152 residue segment localized to the carboxyl-terminal region of the TDP43 RNA-binding protein. This TDP43 LC domain contains ten conserved methionine residues. Self-association of this domain leads to the formation of liquid-like droplets composed of labile, cross-β polymers. Exposure of polymers to low concentrations of H2O2 leads to a phenomenon of droplet melting that can be reversed upon exposure of the oxidized protein to the MsrA and MsrB methionine sulfoxide reductase enzymes, thioredoxin, thioredoxin reductase and NADPH. Morphological features of the cross-β polymers were revealed by a method of H2O2-mediated footprinting. Similar TDP43 LC domain footprints were observed in highly polymerized, hydrogel samples, liquid-like droplet samples, and living cells. The ability of H2O2 to impede cross-β polymerization was abrogated by a prominent ALS-causing mutation that changes methionine residue 337 to valine. These observations offer potentially useful insight into the biological role of TDP43 in facilitating synapse-localized translation, as well as aberrant aggregation of the protein in neurodegenerative disease.

scholarly journals Selenoproteins and their emerging roles in signaling pathways

2020 ◽  
Vol 11 (2) ◽  
pp. 186-199
Author(s):  
N. V. Stanishevska
Keyword(s):  
Endoplasmic Reticulum ◽  
Signaling Pathways ◽  
Signaling Pathway ◽  
Thioredoxin Reductase ◽  
Methionine Sulfoxide ◽  
Mapk Signaling ◽  
Methionine Sulfoxide Reductase ◽  
Selenoprotein S ◽  
Selenoprotein K ◽  
Er Membrane

The functional activity of selenoproteins has a wide range of effects on complex pathogenetic processes, including teratogenesis, immuno-inflammatory, neurodegenerative. Being active participants and promoters of many signaling pathways, selenoproteins support the lively interest of a wide scientific community. This review is devoted to the analysis of recent data describing the participation of selenoproteins in various molecular interactions mediating important signaling pathways. Data processing was carried out by the method of complex analysis. For convenience, all selenoproteins were divided into groups depending on their location and function. Among the group of selenoproteins of the ER membrane, selenoprotein N affects the absorption of Ca2+ by the endoplasmic reticulum mediated by oxidoreductin (ERO1), a key player in the CHOP/ERO1 branch, a pathogenic mechanism that causes myopathy. Another selenoprotein of the ER membrane selenoprotein K binding to the DHHC6 protein affects the IP3R receptor that regulates Ca2+ flux. Selenoprotein K is able to affect another protein of the endoplasmic reticulum CHERP, also appearing in Ca2+ transport. Selenoprotein S, associated with the lumen of ER, is able to influence the VCP protein, which ensures the incorporation of selenoprotein K into the ER membrane. Selenoprotein M, as an ER lumen protein, affects the phosphorylation of STAT3 by leptin, which confirms that Sel M is a positive regulator of leptin signaling. Selenoprotein S also related to luminal selenoproteins ER is a modulator of the IRE1α-sXBP1 signaling pathway. Nuclear selenoprotein H will directly affect the suppressor of malignant tumours, p53 protein, the activation of which increases with Sel H deficiency. The same selenoprotein is involved in redox regulation. Among the cytoplasmic selenoproteins, abundant investigations are devoted to SelP, which affects the PI3K/Akt/Erk signaling pathway during ischemia/reperfusion, is transported into the myoblasts through the plasmalemma after binding to the apoER2 receptor, and into the neurons to the megaline receptor and in general, selenoprotein P plays the role of a pool that stores the necessary trace element and releases it, if necessary, for vital selenoproteins. The thioredoxin reductase family plays a key role in the invasion and metastasis of salivary adenoid cystic carcinoma through the influence on the TGF-β-Akt/GSK-3β pathway during epithelial-mesenchymal transition. The deletion of thioredoxin reductase 1 affects the levels of messengers of the Wnt/β-catenin signaling pathway. No less studied is the glutathione peroxidase group, of which GPX3 is able to inhibit signaling in the Wnt/β-catenin pathway and thereby inhibit thyroid metastasis, as well as suppress protein levels in the PI3K/Akt/c-fos pathway. A key observation is that in cases of carcinogenesis, a decrease in GPX3 and its hypermethylation are almost always found. Among deiodinases, deiodinase 3 acts as a promoter of the oncogenes BRAF, MEK or p38, while stimulating a decrease in the expression of cyclin D1. The dependence of the level of deiodinase 3 on the Hedgehog (SHH) signaling pathway is also noted. Methionine sulfoxide reductase A can compete for the uptake of ubiquitin, reduce p38, JNK and ERK promoters of the MAPK signaling pathway; methionine sulfoxide reductase B1 suppresses MAPK signaling messengers, and also increases PARP and caspase 3.

scholarly journals Effects of Selenium and Cadmium on Breast Muscle Fatty-Acid Composition and Gene Expression of Liver Antioxidant Proteins in Broilers

Antioxidants ◽  
2019 ◽  
Vol 8 (5) ◽  
pp. 147 ◽  
Author(s):  
Evangelos Zoidis ◽  
George Papadomichelakis ◽  
Athanasios C. Pappas ◽  
Georgios Theodorou ◽  
Kostas Fegeros
Keyword(s):  
Gene Expression ◽  
Fatty Acid ◽  
Messenger Rna ◽  
Broiler Chickens ◽  
Thioredoxin Reductase ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Breast Muscle ◽  
Iodothyronine Deiodinase ◽  
Organic Selenium

The present work was part of a project intended to evaluate whether organic selenium (Se) has the potential to protect against toxic effects exerted by cadmium (Cd). For this reason, 300 as-hatched, one-day-old broiler chickens were randomly allocated in four dietary treatments with five replicate pens per treatment. Chickens in T1 treatment, were offered a diet supplemented with 0.3 ppm Se (as Se-yeast), without added Cd; in T2 treatment, they were offered a diet with 0.3 ppm Se and 10 ppm Cd; in T3 treatment, they were offered a diet with 0.3 ppm Se and 100 ppm Cd; in T4 treatment, chickens were offered a diet supplemented with 3 ppm Se and 100 ppm Cd. Cadmium was added to the diets in T2, T3, and T4 as CdCl2. On the fourth and sixth weeks, liver and breast samples were obtained from two broilers per replicate pen. Relative gene expression levels of catalase (CAT), superoxide dismutase 1 (SOD1) and 2 (SOD2), methionine sulfoxide reductase A (MSRA) and B3 (MSRB3), iodothyronine deiodinase 1 (DIO1), 2 (DIO2), and 3 (DIO3), glutathione peroxidase 1 (GPX1) and 4 (GPX4), thioredoxin reductase 1 (TXNRD1) and 3 (TXNRD3), and metallothionein 3 (MT3) were analyzed by real-time quantitative PCR in liver, whereas the fatty-acid (FA) profile of breast muscle was determined by gas chromatography. Broilers supplemented with 0.3 ppm Se could tolerate low levels of Cd present in the diets, as there were no significant changes in the breast muscle FA profile, whereas excess Cd led to decreased polyunsaturated fatty acids (PUFAs), and in particular n-6 PUFA. Furthermore, treatments mainly affected the messenger RNA (mRNA) expression of SOD2, TXNRD3, and MT3, while age affected CAT, MSRB3, DIO2, DIO3, GPX4, TXNRD1, and MT3. In conclusion, dietary Se may help against the negative effects of Cd, but cannot be effective when Cd is present at excessive amounts in the diet.

scholarly journals Protein Repair and Degradation during Aging

2002 ◽  
Vol 2 ◽  
pp. 248-254 ◽  
Author(s):  
Bertrand Friguet
Keyword(s):  
Oxidative Damage ◽  
Protein Degradation ◽  
State Level ◽  
Methionine Sulfoxide ◽  
Cellular Aging ◽  
Methionine Sulfoxide Reductase ◽  
Protein Repair ◽  
Age Related ◽  
Oxidatively Modified ◽  
Peptide Methionine Sulfoxide Reductase

Cellular aging is characterized by a build-up of oxidatively modified proteins. The steady-state level of oxidized proteins depends on the balance between the rate of protein oxidative damage and the rates of protein degradation and repair. Therefore, the accumulation of oxidized protein with age can be due to increased protein damage, decreased oxidized protein degradation and repair, or the combination of both mechanisms. The proteasomal system is the major intracellular proteolytic pathway implicated in the degradation of oxidized protein, and the peptide methionine sulfoxide reductase catalyzes the reduction of methionine sulfoxide (i.e., oxidized methionine) to methionine within proteins. A short summary on protein oxidative damage and oxidized protein degradation is given, and evidence for a decline of proteasome function with age is presented. Arguments for the implication of peptide methionine sulfoxide reductase in the age-related accumulation of oxidized protein are also discussed.

Sign in / Sign up

Export Citation Format

Share Document