Cytotoxicity induced by inhibition of thioredoxin reductases via multiple signaling pathways: Role of cytosolic phospholipase A<sub>2</sub>α‐dependent and ‐independent release of arachidonic acid

Kurosawa, Tohru; Nakamura, Hiroyuki; Yamaura, Erika; Fujino, Hiromichi; Mori, Yasuo; Kawashima, Tatsuo; Murayama, Toshihiko

doi:10.1002/jcp.21703

Cited by 21 publications

(23 citation statements)

References 53 publications

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“…The modification of ARA release and metabolism in response to selenoprotein activity in cultured cells has been reported previously. For example, TrxR reduced cPLA2 activity and ARA release in mouse fibrosarcoma cells (Kurosawa et al 2009) and GPX inhibited effectively 5-LOX activity and reduced the oxidation of 5-HETE to 5-HPETE in human peripheral blood monocytes (Straif et al 2000). In this study, we found that pretreatment of BMECs with Se markedly inhibited H 2 O 2 -induced increase of cPLA2 expression and activity and ARA release.…”

Section: Discussionsupporting

confidence: 52%

“…Se supplementation in bovine endothelial cells exhibited a significantly higher 15-hydroxyeicosatetraenoic acid (HETE) to 15-HPETE ratio compared with Se-deficient cells (Funk and Cyrus 2001). Some studies showed that Se-dependent GPX is directly involved in the reduction of 5-HPETE to 5-HETE in human peripheral blood monocytes (Straif et al 2000) and TrxR reduced cPLA2 activity and ARA content in mouse fibrosarcoma cells (Kurosawa et al 2009). The cPLA2 is a downstream substrate of mitogenactivated protein kinase (MAPK) pathway, which can be activated by ROS (Camps et al 2000).…”

Section: Doi: 1017221/76/2017-cjasmentioning

confidence: 99%

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Protection of bovine mammary epithelial cells from hydrogen peroxide-induced oxidative cell damage by selenium

Guo¹,

Gong²,

Zheng³

et al. 2018

CZECH J ANIM SCI

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The uncontrolled release of arachidonic acid (ARA) and its metabolism by lipoxygenase (LOX) pathway can induce and aggravate cellular oxidative stress. Selenium (Se) is an integral part of some antioxidative selenoproteins and may protect cells from oxidative damage by modulating ARA release and metabolism. The present study aimed to investigate the protective response of Se against hydrogen peroxide (H 2 O 2 )-induced oxidative damage in bovine mammary epithelial cells (BMECs). The BMECs were incubated for 24 h in serum-free medium and then divided into four groups randomly. The cells in groups 1 and 2 were subsequently incubated for 30 h in serum-free medium containing 0 (control) and 50 nM Se (Se treatment group). The cells in groups 3 and 4 were incubated for 24 h in serum-free medium containing 0 and 50 nM Se, and then treated with 600 μM H 2 O 2 for 6 h (H 2 O 2 damage group and Se prevention group). The results showed that Se attenuated the H 2 O 2 -induced production of reactive oxygen species and the decrease of antioxidative enzymes as glutathione peroxidase (GPX), thioredoxin reductase (TrxR), selenoprotein P (SelP), superoxide dismutase, and catalase in BMECs. The preventive effects of Se on the decrease of selenoprotein activity were demonstrated further by the increase of mRNA expression for GPX1, TrxR1, and SelP, and protein expression for GPX1 and TrxR1. Pretreatment of cells with Se inhibited the H 2 O 2 -induced increase of mRNA expressions and activities for cytosolic phospholipase A2 and 5-lipoxygenase, ARA release, and 15-hydroperoxyeicosatetraenoic acid production. Se also blocked the H 2 O 2 -induced activation of p38 mitogen-activated protein kinase (MAPK) and c-Jun N-terminal kinase but not that of extracellular signal-regulated kinase. These results suggested that Se may protect BMECs against H 2 O 2 -induced oxidative damage by increasing selenoproteins synthesis, inhibiting MAPK pathway, and then decreasing ARA release and its metabolism by LOX pathway.Keywords: selenomethionine; selenoprotein synthesis; arachidonic acid metabolism; mitogen-activated protein kinase List of abbreviations: ROS = reactive oxygen species, Se = selenium, GPX = glutathione peroxidase, TrxR = thioredoxin reductase, SelP = selenoprotein P, ARA = arachidonic acid, cPLA2 = cytosolic phospholipase A2, LPS = lipopolysaccharides, LOX = lipoxygenase, HPETE = hydroperoxyeicosatetraenoic acid, HETE = hydroxyeicosatetraenoic acid, MAPK = mitogen-activated protein kinase, BMECs = bovine mammary epithelial cells, PBS = phosphate balanced solution, DMEM = Dulbecco's modified Eagle medium, FBS = fetal bovine serum, SeMet = selenomethionine, MTT = 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, DMSO = dimethyl sulfoxide, SOD = superoxide dismutase, CAT = catalase, ERK = extracellular signal-regulated kinase, JNK = c-Jun N-terminal kinase K

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Section: Discussionsupporting

confidence: 52%

Section: Doi: 1017221/76/2017-cjasmentioning

confidence: 99%

Protection of bovine mammary epithelial cells from hydrogen peroxide-induced oxidative cell damage by selenium

Guo¹,

Gong²,

Zheng³

et al. 2018

CZECH J ANIM SCI

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“…Membranes were incubated in 1% non-fat dry milk for 16 h at 4°C, and the washed membranes were then incubated with anti-phosphotyrosine antibody (4G10; Upstate, Lake Placid, NY, USA), and the immunoreactive bands were visualized using a chemiluminescent reagent (Thermo Scientific, Waltham, MA, USA). The viability of cells was estimated from the leakage of lactate dehydrogenase and from the counting of attached cells on dishes, as described previously (19,28).…”

Section: Western Blotting and Measurement Of Cell Toxicitymentioning

confidence: 99%

Activation of Ceramidase and Ceramide Kinase by Vanadate via a Tyrosine Kinase–Mediated Pathway

Tada¹,

Toyomura²,

Nakamura³

et al. 2010

J Pharmacol Sci

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Abstract. Ceramide, a key molecule in the metabolism of sphingolipids, is converted by ceramidase to sphingosine, and phosphorylated by ceramide kinase to form ceramide-1-phosphate (C1P). In this study, we improved on a method of thin-layer chromatography using a fluorescent ceramide, 4-nitrobenzo-2-oxa-1,3-diazole-labeled C6-ceramide (NBD-ceramide) by adding another step for separation of extracted ceramide metabolites by lipophilicity, and determined levels of C1P, caproic acid, sphingomyelin, and glucosylceramide simultaneously. Also we found that 1) treatment of NBD-ceramide-labeled cells (human lung adenocarcinoma A549 cells and Chinese hamster ovary cells) with Na 3 VO 4 increased the amount of NBD-C1P formed within 30 min, 2) the treatment increased production of NBD-caproic acid, a counterpart of sphingosine, by ceramidase within 2 h, 3) expression of ceramide kinase enhanced the Na 3 VO 4 -induced formation of NBD-C1P, and tyrosine kinase inhibitors (herbimycin and genistein) decreased the response, 4) the production of NBD-caproic acid in A549 cells was inhibited by genistein, and 5) the responses for 2 h after Na 3 VO 4 treatment were accompanied by a decrease in the production of NBD-sphingomyelin, not a loss of NBD-ceramide. The improved thin-layer chromatography method was useful for the simultaneous determination of enzymatic activities for ceramide metabolism in cells.

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“…Taking all of these factors into consideration, RA-induced protection from H 2 O 2 -induced oxidative damage may be associated with lower ARA production resulting from increased TRXR activity. Kurosawa et al (2009) suggested that TRXR inhibited the activity of CPLA2 and release of ARA as well as prevented toxic effects in L929 mouse fibrosarcoma cells. Kelavkar et al (2001) indicated that TRXR could directly reduce the lipid hydroperoxide 15-HPETE and potentially limit its accumulation in cells that express 15-LOX.…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, regulating the release and metabolism of ARA is the key to protecting cells from oxidative stress-induced damage. Kurosawa et al (2009) investigated the role of TRXR in inhibiting the release of ARA, and their results suggested that TRXR suppressed the activity of CPLA2 and release of ARA, avoiding toxic effects in L929 mouse fibrosarcoma cells. Therefore, we propose that RA may protect BMEC from oxidative stress by promoting TRXR activity, which results in inhibition of the MAPK signaling pathway, leading to suppression of ARA release.…”

mentioning

confidence: 99%

Retinoic acid attenuates oxidative injury in bovine mammary epithelial cells induced by hydrogen peroxide

Jin¹,

Yan²,

Shi³

et al. 2017

CZECH J ANIM SCI

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Jin L., Yan S., Shi B., Shi H., Guo X., Li J. (2017): Retinoic acid attenuates oxidative injury in bovine mammary epithelial cells induced by hydrogen peroxide. Czech J. Anim. Sci., 62, 539-548.The objective of this study was to explore how retinoic acid (RA) attenuates oxidative injury induced by hydrogen peroxide (H 2 O 2 ) in bovine mammary epithelial cells (BMEC). Subconfluence BMEC were randomly divided into four groups with six replicates: the control group (incubated in serum-free medium without RA or H 2 O 2 for 30 h), H 2 O 2 group (pre-incubated for 24 h without RA, then for another 6 h with 600 μM H 2 O 2 ), RA group (incubated with 1 mg/ml RA for 30 h without H 2 O 2 ), and RA + H 2 O 2 group (RA prevention group, pre-incubated with 1 mg/ml RA for 24 h and then for another 6 h with 600 mM H 2 O 2 ). The results showed that the H 2 O 2 treatment significantly decreased several measured traits, including the cell viability, glutathione peroxidase (GPX) and thioredoxin reductase (TRXR) activities, selenoprotein P (SELP) content, catalase and superoxide dismutase activities, total antioxidant capacity, and GPX1, TRXR1, and SELP gene expression, as well as GPX1 and TRXR1 protein expression. H 2 O 2 treatment also increased the malondialdehyde and reactive oxygen species contents and induced a marked increase of several measured traits, including the arachidonic acid (ARA) concentration, cytosolic phospholipase A2 and 5-lipoxygenase gene expression and activity, and 15-hydroxy twenty-four arachidonic acid and hydroxy peroxide tetracosenic arachidonic acid contents. RA pre-treatment prevented corresponding increases in parameters related to ARA metabolism and increased the activity of TRXR. Moreover, RA pre-treatment attenuated the phosphorylation levels of p38 mitogen-activated protein kinase (MAPK) and c-Jun N-terminal kinase and effectively decreased the ARA content. These results suggest that RA protected BMEC from oxidative stress by elevating TRXR activity, which inhibited the MAPK signaling pathway and led to a decreased concentration of ARA.Keywords: vitamin A; thioredoxin reductase; oxidative injury; arachidonic acid; p38 mitogen-activated protein kinase List of abbreviations: RA = retinoic acid, ROS = reactive oxygen species, VA = vitamin A, BMEC = bovine mammary epithelial cells, GPX1 = glutathione peroxidase 1, TRXR1 = thioredoxin reductases 1, ARA = arachidonic acid, CPLA2 = cytosolic phospholipase A2, MAPK = mitogen-activated protein kinase, H 2 O 2 = hydrogen peroxide, DMSO = dimethyl sulfoxide, MTT = 5-diphenyltetrazolium bromide, DMEM/F12 = Dulbecco's Modified Eagle's Medium/F12, 5-LOX = 5-lipoxygenase, PGE2 = prostaglandin E2, COX-2 = cyclooxygenase-2, LTB4 = leukotriene B4, 12-or 15-HETE = 12-or 15-hydroxyeicosatetraenoic acid, 12-or 15-HPETE = 12-or 15-hydroperoxyeicosatetraenoic acid, ERK1/2 = extracellular signal-regulated kinase ½, JNK = c-Jun N-terminal kinase, PBS = phosphate buffered solution, RGR = relative growth rate, T-AOC = total antioxidant capacity, SOD = superoxide ...

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Cytotoxicity induced by inhibition of thioredoxin reductases via multiple signaling pathways: Role of cytosolic phospholipase A₂α‐dependent and ‐independent release of arachidonic acid

Cited by 21 publications

References 53 publications

Protection of bovine mammary epithelial cells from hydrogen peroxide-induced oxidative cell damage by selenium

Protection of bovine mammary epithelial cells from hydrogen peroxide-induced oxidative cell damage by selenium

Activation of Ceramidase and Ceramide Kinase by Vanadate via a Tyrosine Kinase–Mediated Pathway

Retinoic acid attenuates oxidative injury in bovine mammary epithelial cells induced by hydrogen peroxide

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Cytotoxicity induced by inhibition of thioredoxin reductases via multiple signaling pathways: Role of cytosolic phospholipase A2α‐dependent and ‐independent release of arachidonic acid

Cited by 21 publications

References 53 publications

Protection of bovine mammary epithelial cells from hydrogen peroxide-induced oxidative cell damage by selenium

Protection of bovine mammary epithelial cells from hydrogen peroxide-induced oxidative cell damage by selenium

Activation of Ceramidase and Ceramide Kinase by Vanadate via a Tyrosine Kinase–Mediated Pathway

Retinoic acid attenuates oxidative injury in bovine mammary epithelial cells induced by hydrogen peroxide

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Cytotoxicity induced by inhibition of thioredoxin reductases via multiple signaling pathways: Role of cytosolic phospholipase A₂α‐dependent and ‐independent release of arachidonic acid