메뉴 건너뛰기




Volumn 172, Issue 3, 2018, Pages 409-422.e21

Selenium Utilization by GPX4 Is Required to Prevent Hydroperoxide-Induced Ferroptosis

(24)  Ingold, Irina a   Berndt, Carsten b   Schmitt, Sabine c   Doll, Sebastian a   Poschmann, Gereon b   Buday, Katalin a   Roveri, Antonella d   Peng, Xiaoxiao e   Porto Freitas, Florencio a   Seibt, Tobias f   Mehr, Lisa a   Aichler, Michaela a   Walch, Axel a   Lamp, Daniel a,g   Jastroch, Martin a,g   Miyamoto, Sayuri h   Wurst, Wolfgang a,c,i   Ursini, Fulvio d   Arnér, Elias S J j   Fradejas Villar, Noelia k   more..


Author keywords

ACSL4; ferroptosis; glutathione peroxidase; GPX4; lipid peroxidation; mouse genetics; selenium; selenocysteine; selenoproteins; Trsp

Indexed keywords

CALBINDIN; CALRETININ; CYSTEINE; GLIAL FIBRILLARY ACIDIC PROTEIN; MESSENGER RNA; PEROXIREDOXIN 3; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; SELENOCYSTEINE; THIOREDOXIN REDUCTASE 1; THIOREDOXIN REDUCTASE 2; GLUTATHIONE PEROXIDASE; GLUTATHIONE PEROXIDASE 4, MOUSE; HYDROGEN PEROXIDE; SELENIUM;

EID: 85041924851     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2017.11.048     Document Type: Article
Times cited : (1092)

References (66)
  • 1
    • 44849125526 scopus 로고    scopus 로고
    • Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells
    • Anestål, K., Prast-Nielsen, S., Cenas, N., Arnér, E.S., Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells. PLoS ONE, 3, 2008, e1846.
    • (2008) PLoS ONE , vol.3 , pp. e1846
    • Anestål, K.1    Prast-Nielsen, S.2    Cenas, N.3    Arnér, E.S.4
  • 3
    • 84964928007 scopus 로고    scopus 로고
    • Lipid unsaturation and organelle dynamics
    • Barelli, H., Antonny, B., Lipid unsaturation and organelle dynamics. Curr. Opin. Cell Biol. 41 (2016), 25–32.
    • (2016) Curr. Opin. Cell Biol. , vol.41 , pp. 25-32
    • Barelli, H.1    Antonny, B.2
  • 4
    • 0002356471 scopus 로고
    • Undersökning af en ny Mineral-kropp, funnen i de orenare sorterna af det i Falun tillverkade svaflet
    • Berzelius, J.J., Undersökning af en ny Mineral-kropp, funnen i de orenare sorterna af det i Falun tillverkade svaflet. Afhandlingar i fysik, kemi och mineralogi, 6, 1818, 42.
    • (1818) Afhandlingar i fysik, kemi och mineralogi , vol.6 , pp. 42
    • Berzelius, J.J.1
  • 6
    • 0030978102 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp)
    • Bösl, M.R., Takaku, K., Oshima, M., Nishimura, S., Taketo, M.M., Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp). Proc. Natl. Acad. Sci. USA 94 (1997), 5531–5534.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5531-5534
    • Bösl, M.R.1    Takaku, K.2    Oshima, M.3    Nishimura, S.4    Taketo, M.M.5
  • 7
    • 84917725056 scopus 로고    scopus 로고
    • Easy quantitative assessment of genome editing by sequence trace decomposition
    • Brinkman, E.K., Chen, T., Amendola, M., van Steensel, B., Easy quantitative assessment of genome editing by sequence trace decomposition. Nucleic Acids Res., 42, 2014, e168.
    • (2014) Nucleic Acids Res. , vol.42 , pp. e168
    • Brinkman, E.K.1    Chen, T.2    Amendola, M.3    van Steensel, B.4
  • 8
    • 84921357948 scopus 로고    scopus 로고
    • Expression of inactive glutathione peroxidase 4 leads to embryonic lethality, and inactivation of the Alox15 gene does not rescue such knock-in mice
    • Brutsch, S.H., Wang, C.C., Li, L., Stender, H., Neziroglu, N., Richter, C., Kuhn, H., Borchert, A., Expression of inactive glutathione peroxidase 4 leads to embryonic lethality, and inactivation of the Alox15 gene does not rescue such knock-in mice. Antioxid. Redox. Signal. 22 (2015), 281–293.
    • (2015) Antioxid. Redox. Signal. , vol.22 , pp. 281-293
    • Brutsch, S.H.1    Wang, C.C.2    Li, L.3    Stender, H.4    Neziroglu, N.5    Richter, C.6    Kuhn, H.7    Borchert, A.8
  • 9
    • 84894038619 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in the pathophysiology of renal diseases
    • Che, R., Yuan, Y., Huang, S., Zhang, A., Mitochondrial dysfunction in the pathophysiology of renal diseases. Am. J. Physiol. Renal Physiol. 306 (2014), F367–F378.
    • (2014) Am. J. Physiol. Renal Physiol. , vol.306 , pp. F367-F378
    • Che, R.1    Yuan, Y.2    Huang, S.3    Zhang, A.4
  • 14
    • 0342310833 scopus 로고
    • Evolutionary adaptation of membranes to temperature
    • Cossins, A.R., Prosser, C.L., Evolutionary adaptation of membranes to temperature. Proc. Natl. Acad. Sci. USA 75 (1978), 2040–2043.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2040-2043
    • Cossins, A.R.1    Prosser, C.L.2
  • 15
    • 0001066006 scopus 로고
    • A chrome-osmium fixative for eectron microscopy
    • Dalton, A.J., A chrome-osmium fixative for eectron microscopy. Anat. Rec., 121, 1955, 281.
    • (1955) Anat. Rec. , vol.121 , pp. 281
    • Dalton, A.J.1
  • 21
    • 78649629122 scopus 로고    scopus 로고
    • Redox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse
    • Godoy, J.R., Funke, M., Ackermann, W., Haunhorst, P., Oesteritz, S., Capani, F., Elsässer, H.P., Lillig, C.H., Redox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse. Biochim. Biophys. Acta 1810 (2011), 2–92.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 2-92
    • Godoy, J.R.1    Funke, M.2    Ackermann, W.3    Haunhorst, P.4    Oesteritz, S.5    Capani, F.6    Elsässer, H.P.7    Lillig, C.H.8
  • 22
    • 34248595963 scopus 로고    scopus 로고
    • Extended longevity of queen honey bees compared to workers is associated with peroxidation-resistant membranes
    • Haddad, L.S., Kelbert, L., Hulbert, A.J., Extended longevity of queen honey bees compared to workers is associated with peroxidation-resistant membranes. Exp. Gerontol. 42 (2007), 601–609.
    • (2007) Exp. Gerontol. , vol.42 , pp. 601-609
    • Haddad, L.S.1    Kelbert, L.2    Hulbert, A.J.3
  • 23
    • 85012900626 scopus 로고    scopus 로고
    • Ablation of ferroptosis regulator glutathione peroxidase 4 in forebrain neurons promotes cognitive impairment and neurodegeneration
    • Hambright, W.S., Fonseca, R.S., Chen, L., Na, R., Ran, Q., Ablation of ferroptosis regulator glutathione peroxidase 4 in forebrain neurons promotes cognitive impairment and neurodegeneration. Redox Biol. 12 (2017), 8–17.
    • (2017) Redox Biol. , vol.12 , pp. 8-17
    • Hambright, W.S.1    Fonseca, R.S.2    Chen, L.3    Na, R.4    Ran, Q.5
  • 25
    • 34547629188 scopus 로고    scopus 로고
    • Conditional brain-specific knockdown of MAPK using Cre/loxP regulated RNA interference
    • Hitz, C., Wurst, W., Kühn, R., Conditional brain-specific knockdown of MAPK using Cre/loxP regulated RNA interference. Nucleic Acids Res., 35, 2007, e90.
    • (2007) Nucleic Acids Res. , vol.35 , pp. e90
    • Hitz, C.1    Wurst, W.2    Kühn, R.3
  • 26
    • 84901316606 scopus 로고    scopus 로고
    • Cellular mechanisms and physiological consequences of redox-dependent signalling
    • Holmström, K.M., Finkel, T., Cellular mechanisms and physiological consequences of redox-dependent signalling. Nat. Rev. Mol. Cell Biol. 15 (2014), 411–421.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 411-421
    • Holmström, K.M.1    Finkel, T.2
  • 28
    • 84930623244 scopus 로고    scopus 로고
    • Expression of a catalytically inactive mutant form of glutathione peroxidase 4 (Gpx4) confers a dominant-negative effect in male fertility
    • Ingold, I., Aichler, M., Yefremova, E., Roveri, A., Buday, K., Doll, S., Tasdemir, A., Hoffard, N., Wurst, W., Walch, A., et al. Expression of a catalytically inactive mutant form of glutathione peroxidase 4 (Gpx4) confers a dominant-negative effect in male fertility. J. Biol. Chem. 290 (2015), 14668–14678.
    • (2015) J. Biol. Chem. , vol.290 , pp. 14668-14678
    • Ingold, I.1    Aichler, M.2    Yefremova, E.3    Roveri, A.4    Buday, K.5    Doll, S.6    Tasdemir, A.7    Hoffard, N.8    Wurst, W.9    Walch, A.10
  • 30
    • 84940063163 scopus 로고    scopus 로고
    • The interneuron energy hypothesis: implications for brain disease
    • Kann, O., The interneuron energy hypothesis: implications for brain disease. Neurobiol. Dis. 90 (2016), 75–85.
    • (2016) Neurobiol. Dis. , vol.90 , pp. 75-85
    • Kann, O.1
  • 31
    • 77956198422 scopus 로고    scopus 로고
    • Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins
    • Klomsiri, C., Nelson, K.J., Bechtold, E., Soito, L., Johnson, L.C., Lowther, W.T., Ryu, S.E., King, S.B., Furdui, C.M., Poole, L.B., Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods Enzymol. 473 (2010), 77–94.
    • (2010) Methods Enzymol. , vol.473 , pp. 77-94
    • Klomsiri, C.1    Nelson, K.J.2    Bechtold, E.3    Soito, L.4    Johnson, L.C.5    Lowther, W.T.6    Ryu, S.E.7    King, S.B.8    Furdui, C.M.9    Poole, L.B.10
  • 32
    • 37549062738 scopus 로고    scopus 로고
    • Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life
    • Lobanov, A.V., Fomenko, D.E., Zhang, Y., Sengupta, A., Hatfield, D.L., Gladyshev, V.N., Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life. Genome Biol., 8, 2007, R198.
    • (2007) Genome Biol. , vol.8 , pp. R198
    • Lobanov, A.V.1    Fomenko, D.E.2    Zhang, Y.3    Sengupta, A.4    Hatfield, D.L.5    Gladyshev, V.N.6
  • 34
    • 79960191503 scopus 로고    scopus 로고
    • Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme
    • Mannes, A.M., Seiler, A., Bosello, V., Maiorino, M., Conrad, M., Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme. FASEB J. 25 (2011), 2135–2144.
    • (2011) FASEB J. , vol.25 , pp. 2135-2144
    • Mannes, A.M.1    Seiler, A.2    Bosello, V.3    Maiorino, M.4    Conrad, M.5
  • 35
    • 0030835448 scopus 로고    scopus 로고
    • Parvalbumin- and calbindin-containing neurons express c-fos protein in primary and secondary (mirror) epileptic foci of the rat neocortex
    • Mihaly, A., Szente, M., Dubravcsik, Z., Boda, B., Kiraly, E., Nagy, T., Domonkos, A., Parvalbumin- and calbindin-containing neurons express c-fos protein in primary and secondary (mirror) epileptic foci of the rat neocortex. Brain Res. 761 (1997), 135–145.
    • (1997) Brain Res. , vol.761 , pp. 135-145
    • Mihaly, A.1    Szente, M.2    Dubravcsik, Z.3    Boda, B.4    Kiraly, E.5    Nagy, T.6    Domonkos, A.7
  • 37
    • 38749087624 scopus 로고    scopus 로고
    • High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates
    • Muller, F.L., Liu, Y., Abdul-Ghani, M.A., Lustgarten, M.S., Bhattacharya, A., Jang, Y.C., Van Remmen, H., High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates. Biochem. J. 409 (2008), 491–499.
    • (2008) Biochem. J. , vol.409 , pp. 491-499
    • Muller, F.L.1    Liu, Y.2    Abdul-Ghani, M.A.3    Lustgarten, M.S.4    Bhattacharya, A.5    Jang, Y.C.6    Van Remmen, H.7
  • 39
    • 84901049603 scopus 로고    scopus 로고
    • Sec-containing TrxR1 is essential for self-sufficiency of cells by control of glucose-derived H2O2
    • Peng, X., Mandal, P.K., Kaminskyy, V.O., Lindqvist, A., Conrad, M., Arnér, E.S., Sec-containing TrxR1 is essential for self-sufficiency of cells by control of glucose-derived H2O2. Cell Death Dis., 5, 2014, e1235.
    • (2014) Cell Death Dis. , vol.5 , pp. e1235
    • Peng, X.1    Mandal, P.K.2    Kaminskyy, V.O.3    Lindqvist, A.4    Conrad, M.5    Arnér, E.S.6
  • 42
    • 84966264067 scopus 로고    scopus 로고
    • Why Nature chose selenium
    • Reich, H.J., Hondal, R.J., Why Nature chose selenium. ACS Chem. Biol. 11 (2016), 821–841.
    • (2016) ACS Chem. Biol. , vol.11 , pp. 821-841
    • Reich, H.J.1    Hondal, R.J.2
  • 44
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: hydrogen peroxide as intracellular messenger
    • Rhee, S.G., Redox signaling: hydrogen peroxide as intracellular messenger. Exp. Mol. Med. 31 (1999), 53–59.
    • (1999) Exp. Mol. Med. , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 46
    • 0028291969 scopus 로고
    • Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase
    • Roveri, A., Maiorino, M., Ursini, F., Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase. Methods Enzymol. 233 (1994), 202–212.
    • (1994) Methods Enzymol. , vol.233 , pp. 202-212
    • Roveri, A.1    Maiorino, M.2    Ursini, F.3
  • 57
    • 84881657606 scopus 로고    scopus 로고
    • Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes
    • Snider, G.W., Ruggles, E., Khan, N., Hondal, R.J., Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes. Biochemistry 52 (2013), 5472–5481.
    • (2013) Biochemistry , vol.52 , pp. 5472-5481
    • Snider, G.W.1    Ruggles, E.2    Khan, N.3    Hondal, R.J.4
  • 58
    • 84958729887 scopus 로고    scopus 로고
    • A glutathione-Nrf2-Thioredoxin cross-talk ensures keratinocyte survival and efficient wound repair
    • Telorack, M., Meyer, M., Ingold, I., Conrad, M., Bloch, W., Werner, S., A glutathione-Nrf2-Thioredoxin cross-talk ensures keratinocyte survival and efficient wound repair. PLoS Genet., 12, 2016, e1005800.
    • (2016) PLoS Genet. , vol.12 , pp. e1005800
    • Telorack, M.1    Meyer, M.2    Ingold, I.3    Conrad, M.4    Bloch, W.5    Werner, S.6
  • 59
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues
    • Tietze, F., Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27 (1969), 502–522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 60
    • 0036710533 scopus 로고    scopus 로고
    • Polyunsaturated fatty acid synthesis: what will they think of next?
    • Wallis, J.G., Watts, J.L., Browse, J., Polyunsaturated fatty acid synthesis: what will they think of next?. Trends Biochem. Sci., 27, 2002, 467.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 467
    • Wallis, J.G.1    Watts, J.L.2    Browse, J.3
  • 61
    • 0025761870 scopus 로고
    • Glutathione peroxidase deficiency and childhood seizures
    • Weber, G.F., Maertens, P., Meng, X.Z., Pippenger, C.E., Glutathione peroxidase deficiency and childhood seizures. Lancet 337 (1991), 1443–1444.
    • (1991) Lancet , vol.337 , pp. 1443-1444
    • Weber, G.F.1    Maertens, P.2    Meng, X.Z.3    Pippenger, C.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.