S-Glutathionylation of mouse selenoprotein W prevents oxidative stress-induced cell death by blocking the formation of an intramolecular disulfide bond

Ko, Kwan Young; Lee, Jea Hwang; Jang, Jun Ki; Jin, Yunjung; Kang, Hyunwoo; Kim, Ick Young

doi:10.1016/j.freeradbiomed.2019.07.007

Cited by 9 publications

(7 citation statements)

References 55 publications

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“…This holds especially true for selenoproteins such as selenoprotein H (SelenoH) and SelenoW which contain selenocysteine (Sec) as part of a CXXU motif, indicating that they are putative oxidoreductases. In addition, SelenoW has been shown to act in an antioxidant manner after its glutathionylation [ 3 ]. During selenoprotein synthesis, Se is cotranslationally incorporated as Sec which is encoded by the base triplet UGA.…”

Section: Introductionmentioning

confidence: 99%

Copper interferes with selenoprotein synthesis and activity

et al. 2020

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Selenium and copper are essential trace elements for humans, needed for the biosynthesis of enzymes contributing to redox homeostasis and redox-dependent signaling pathways. Selenium is incorporated as selenocysteine into the active site of redox-relevant selenoproteins including glutathione peroxidases (GPX) and thioredoxin reductases (TXNRD). Copper-dependent enzymes mediate electron transfer and other redox reactions. As selenoprotein expression can be modulated e.g. by H 2 O 2 , we tested the hypothesis that copper status affects selenoprotein expression. To this end, hepatocarcinoma HepG2 cells and mice were exposed to a variable copper and selenium supply in a physiologically relevant concentration range, and transcript and protein expression as well as GPX and TXNRD activities were compared. Copper suppressed selenoprotein mRNA levels of GPX1 and SELENOW, downregulated GPX and TXNRD activities and decreased UGA recoding efficiency in reporter cells. The interfering effects were successfully suppressed by applying the copper chelators bathocuproinedisulfonic acid or tetrathiomolybdate. In mice, a decreased copper supply moderately decreased the copper status and negatively affected hepatic TXNRD activity. We conclude that there is a hitherto unknown interrelationship between copper and selenium status, and that copper negatively affects selenoprotein expression and activity most probably via limiting UGA recoding. This interference may be of physiological relevance during aging, where a particular shift in the selenium to copper ratio has been reported. An increased concentration of copper in face of a downregulated selenoprotein expression may synergize and negatively affect the cellular redox homeostasis contributing to disease processes.

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Section: Introductionmentioning

confidence: 99%

Copper interferes with selenoprotein synthesis and activity

et al. 2020

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“…These results suggest that the 14-3-3β signaling pathway can be cooperatively regulated by Trx1 and SELENOW. There is no interaction between Trx1 and SELENOW [ 27 ].…”

Section: Discussionmentioning

confidence: 99%

“…Briefly, BL21 (DE3) competent cells were transformed with mouse GST-SELENOW and human Trx1-His mutants in pGEX 4T-1 (Amersham Biosciences, Chalfont, UK) and pET26B (Novagen, Madison, WI, USA) plasmids. The proteins were induced by 1 mM IPTG for 16 h at 18 °C and purified using glutathione and Ni-NTA beads as described previously [ 27 , 30 ].…”

Section: Methodsmentioning

confidence: 99%

“…Purified proteins were incubated with cell lysate or recombinant proteins in pull-down buffer containing 20 mM HEPES (pH 7.5), 1 mM EDTA and 1 mM for 2 h at 4 °C with rotation, followed by glutathione and NI-NTA beads for 1 h. The beads were washed three times with the wash buffer and then eluted [ 27 , 30 ].…”

Section: Methodsmentioning

confidence: 99%

“…mRNA and protein expression of SELENOW is upregulated in the early stage of skeletal muscle cell differentiation [ 22 ]. Additionally, SELENOW is involved in the protection of cells from oxidative stress-induced cell death in a glutathione-dependent manner [ 23 , 24 , 25 , 26 , 27 ]. SELENOW interacts with the 14-3-3 protein and inhibits its interaction with other target proteins.…”

Section: Introductionmentioning

confidence: 99%

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Compensatory Protection of Thioredoxin-Deficient Cells from Etoposide-Induced Cell Death by Selenoprotein W via Interaction with 14-3-3

Kang

Jeon

Ham

et al. 2021

IJMS

Self Cite

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Selenoprotein W (SELENOW) is a 9.6 kDa protein containing selenocysteine (Sec, U) in a conserved Cys-X-X-Sec (CXXU) motif. Previously, we reported that SELENOW regulates various cellular processes by interacting with 14-3-3β at the U of the CXXU motif. Thioredoxin (Trx) is a small protein that plays a key role in the cellular redox regulatory system. The CXXC motif of Trx is critical for redox regulation. Recently, an interaction between Trx1 and 14-3-3 has been predicted. However, the binding mechanism and its biological effects remain unknown. In this study, we found that Trx1 interacted with 14-3-3β at the Cys32 residue in the CXXC motif, and SELENOW and Trx1 were bound at Cys191 residue of 14-3-3β. In vitro binding assays showed that SELENOW and Trx1 competed for interaction with 14-3-3β. Compared to control cells, Trx1-deficient cells and SELENOW-deficient cells showed increased levels of both the subG1 population and poly (ADP-ribose) polymerase (PARP) cleavage by etoposide treatment. Moreover, Akt phosphorylation of Ser473 was reduced in Trx1-deficient cells and was recovered by overexpression of SELENOW. These results indicate that SELENOW can protect Trx1-deficient cells from etoposide-induced cell death through its interaction with 14-3-3β.

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Comparison of Sodium Selenite and Selenium-Enriched Spirulina Supplementation Effects After Selenium Deficiency on Growth, Tissue Selenium Concentrations, Antioxidant Activities, and Selenoprotein Expression in Rats

Castel

León

Gandubert

et al. 2023

Biol Trace Elem Res

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Selenium contributes to physiological functions through its incorporation into selenoproteins. It is involved in oxidative stress defense. A selenium de ciency results in the onset or aggravation of pathologies. Following a de ciency, the repletion of selenium leads to a selenoprotein expression hierarchy still misunderstood. Moreover, spirulina, a microalgae, exhibits antioxidant properties and can be enriched in selenium during its cultivation. Our objective was to determine the effects of a sodium selenite or seleniumenriched spirulina supplementation. Thirty-two female wistar rats were fed for 12 weeks with a seleniumde cient diet. After 8 weeks, rats were divided into 4 groups of 8 rats and were fed with water, sodium selenite (20µg Se/kg body weight), spirulina (3 g/kg bw) or selenium-enriched spirulina (20µg Se/kg bw + 3g spirulina/kg bw). In parallel, another group of 8 rats were fed with normal diet during 12 weeks. Selenium concentration and antioxidant enzyme activities (GPx, SOD, CAT) were measured in plasma, urines, liver, brain, kidney, heart and soleus. Expression of GPx (1, 3), Sel (P, S, T, W), SEPHS2, TrxR1, ApoER2 and Megalin were quanti ed in liver, kidney, brain and heart. Our results showed that a selenium de ciency leads to a growth retardation, reversed by selenium supplementation. All tissues displayed a decrease in selenium concentration following de ciency. Brain seemed protected. Our results demonstrated a hierarchy in selenium distribution and selenoprotein expression depending on selenium supplementation form. A supplementation of sodium selenite improved GPx activities and selenoprotein expression while a seleniumenriched spirulina was more effective to restore selenium concentration.

show abstract

S-Glutathionylation of mouse selenoprotein W prevents oxidative stress-induced cell death by blocking the formation of an intramolecular disulfide bond

Cited by 9 publications

References 55 publications

Copper interferes with selenoprotein synthesis and activity

Copper interferes with selenoprotein synthesis and activity

Compensatory Protection of Thioredoxin-Deficient Cells from Etoposide-Induced Cell Death by Selenoprotein W via Interaction with 14-3-3

Comparison of Sodium Selenite and Selenium-Enriched Spirulina Supplementation Effects After Selenium Deficiency on Growth, Tissue Selenium Concentrations, Antioxidant Activities, and Selenoprotein Expression in Rats

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