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Volumn 70, Issue , 2018, Pages 76-86

Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis

Author keywords

Chaperone; ER stress; Inositol 1,4,5 triphosphate receptor; Protein folding; Selenium; SERCA pump

Indexed keywords

IODIDE PEROXIDASE; IODOTHYRONINE DEIODINASE 2; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SELENOPROTEIN; SELENOPROTEIN F; SELENOPROTEIN K; SELENOPROTEIN M; SELENOPROTEIN N; SELENOPROTEIN S; SELENOPROTEIN T; THYROID HORMONE; UNCLASSIFIED DRUG;

EID: 85019121274     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2017.05.001     Document Type: Review
Times cited : (116)

References (121)
  • 1
    • 84859211841 scopus 로고    scopus 로고
    • Selenium and human health
    • Rayman, M.P., Selenium and human health. Lancet 379 (2012), 1256–1268.
    • (2012) Lancet , vol.379 , pp. 1256-1268
    • Rayman, M.P.1
  • 4
    • 0030978102 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp)
    • Bosl, 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. U. S. A. 94 (1997), 5531–5534.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5531-5534
    • Bosl, M.R.1    Takaku, K.2    Oshima, M.3    Nishimura, S.4    Taketo, M.M.5
  • 5
    • 84995535984 scopus 로고    scopus 로고
    • Why 21? The significance of selenoproteins for human health revealed by inborn errors of metabolism
    • Schweizer, U., Fradejas-Villar, N., Why 21? The significance of selenoproteins for human health revealed by inborn errors of metabolism. FASEB J. 30 (2016), 3669–3681.
    • (2016) FASEB J. , vol.30 , pp. 3669-3681
    • Schweizer, U.1    Fradejas-Villar, N.2
  • 7
    • 84875729310 scopus 로고    scopus 로고
    • Selenocysteine in thiol/disulfide-like exchange reactions
    • Hondal, R.J., Marino, S.M., Gladyshev, V.N., Selenocysteine in thiol/disulfide-like exchange reactions. Antioxid. Redox Signal. 18 (2013), 1675–1689.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 1675-1689
    • Hondal, R.J.1    Marino, S.M.2    Gladyshev, V.N.3
  • 10
    • 34249728817 scopus 로고    scopus 로고
    • STIM1 knockdown reveals that store-operated Ca2+ channels located close to sarco/endoplasmic Ca2+ ATPases (SERCA) pumps silently refill the endoplasmic reticulum
    • Jousset, H., Frieden, M., Demaurex, N., STIM1 knockdown reveals that store-operated Ca2+ channels located close to sarco/endoplasmic Ca2+ ATPases (SERCA) pumps silently refill the endoplasmic reticulum. J. Biol. Chem. 282 (2007), 11456–11464.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11456-11464
    • Jousset, H.1    Frieden, M.2    Demaurex, N.3
  • 11
    • 77649256856 scopus 로고    scopus 로고
    • Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins
    • Shchedrina, V.A., Zhang, Y., Labunskyy, V.M., Hatfield, D.L., Gladyshev, V.N., Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins. Antioxid. Redox Signal. 12 (2010), 839–849.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 839-849
    • Shchedrina, V.A.1    Zhang, Y.2    Labunskyy, V.M.3    Hatfield, D.L.4    Gladyshev, V.N.5
  • 12
    • 85009830296 scopus 로고    scopus 로고
    • TRPC1, Orai1, and STIM1 in SOCE: Friends in tight spaces
    • Dec 30. pii: S0143-4160(16)30218-4. [Epub ahead of print] Review. PMID:28089266
    • Ambudkar, I.S., de Souza, L.B., Ong, H.L., TRPC1, Orai1, and STIM1 in SOCE: Friends in tight spaces. Cell Calcium, 2016, 10.1016/j.ceca.2016.12.009 Dec 30. pii: S0143-4160(16)30218-4. [Epub ahead of print] Review. PMID:28089266.
    • (2016) Cell Calcium
    • Ambudkar, I.S.1    de Souza, L.B.2    Ong, H.L.3
  • 14
    • 85009782220 scopus 로고    scopus 로고
    • Calcium remodeling in colorectal cancer
    • Jan 10. pii: S0167-4889(17)30007-1. [Epub ahead of print] Review. PMID:28087343
    • Villalobos, C., Sobradillo, D., Hernández-Morales, M., Núñez, L., Calcium remodeling in colorectal cancer. Biochim. Biophys. Acta, 2017, 10.1016/j.bbamcr.2017.01.005 Jan 10. pii: S0167-4889(17)30007-1. [Epub ahead of print] Review. PMID:28087343.
    • (2017) Biochim. Biophys. Acta
    • Villalobos, C.1    Sobradillo, D.2    Hernández-Morales, M.3    Núñez, L.4
  • 15
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter, P., Ron, D., The unfolded protein response: from stress pathway to homeostatic regulation. Science 334 (2011), 1081–1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 18
    • 0033920261 scopus 로고    scopus 로고
    • ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
    • Li, M., Baumeister, P., Roy, B., Phan, T., Foti, D., Luo, S., Lee, A.S., ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol. Cell. Biol. 20 (2000), 5096–5106.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5096-5106
    • Li, M.1    Baumeister, P.2    Roy, B.3    Phan, T.4    Foti, D.5    Luo, S.6    Lee, A.S.7
  • 19
    • 84859717205 scopus 로고    scopus 로고
    • Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling
    • Selvaraj, S., Sun, Y., Watt, J.A., Wang, S., Lei, S., Birnbaumer, L., Singh, B.B., Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling. J. Clin. Invest. 122 (2012), 1354–1367.
    • (2012) J. Clin. Invest. , vol.122 , pp. 1354-1367
    • Selvaraj, S.1    Sun, Y.2    Watt, J.A.3    Wang, S.4    Lei, S.5    Birnbaumer, L.6    Singh, B.B.7
  • 21
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas, I., Ron, D., Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell Biol. 13 (2011), 184–190.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 22
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia, Z., Dickens, M., Raingeaud, J., Davis, R.J., Greenberg, M.E., Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270 (1995), 1326–1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 23
    • 33344477350 scopus 로고    scopus 로고
    • Chemical genetic analysis of the time course of signal transduction by JNK
    • Ventura, J.J., Hubner, A., Zhang, C., Flavell, R.A., Shokat, K.M., Davis, R.J., Chemical genetic analysis of the time course of signal transduction by JNK. Mol. Cell 21 (2006), 701–710.
    • (2006) Mol. Cell , vol.21 , pp. 701-710
    • Ventura, J.J.1    Hubner, A.2    Zhang, C.3    Flavell, R.A.4    Shokat, K.M.5    Davis, R.J.6
  • 24
    • 78650105442 scopus 로고    scopus 로고
    • NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis
    • Li, G., Scull, C., Ozcan, L., Tabas, I., NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis. J. Cell Biol. 191 (2010), 1113–1125.
    • (2010) J. Cell Biol. , vol.191 , pp. 1113-1125
    • Li, G.1    Scull, C.2    Ozcan, L.3    Tabas, I.4
  • 25
    • 38049155818 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis
    • Deniaud, A., Sharaf el dein, O., Maillier, E., Poncet, D., Kroemer, G., Lemaire, C., Brenner, C., Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis. Oncogene 27 (2008), 285–299.
    • (2008) Oncogene , vol.27 , pp. 285-299
    • Deniaud, A.1    Sharaf el dein, O.2    Maillier, E.3    Poncet, D.4    Kroemer, G.5    Lemaire, C.6    Brenner, C.7
  • 27
    • 84855966721 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress in metabolic disease and other disorders
    • Ozcan, L., Tabas, I., Role of endoplasmic reticulum stress in metabolic disease and other disorders. Annu. Rev. Med. 63 (2012), 317–328.
    • (2012) Annu. Rev. Med. , vol.63 , pp. 317-328
    • Ozcan, L.1    Tabas, I.2
  • 34
    • 84875632863 scopus 로고    scopus 로고
    • Subtype-selective regulation of IP(3) receptors by thimerosal via cysteine residues within the IP(3)-binding core and suppressor domain
    • Khan, S.A., Rossi, A.M., Riley, A.M., Potter, B.V., Taylor, C.W., Subtype-selective regulation of IP(3) receptors by thimerosal via cysteine residues within the IP(3)-binding core and suppressor domain. Biochem. J. 451 (2013), 177–184.
    • (2013) Biochem. J. , vol.451 , pp. 177-184
    • Khan, S.A.1    Rossi, A.M.2    Riley, A.M.3    Potter, B.V.4    Taylor, C.W.5
  • 36
    • 24344446442 scopus 로고    scopus 로고
    • Effect of selenium-supplement on the calcium signaling in human endothelial cells
    • Zheng, Y., Zhong, L., Shen, X., Effect of selenium-supplement on the calcium signaling in human endothelial cells. J. Cell. Physiol. 205 (2005), 97–106.
    • (2005) J. Cell. Physiol. , vol.205 , pp. 97-106
    • Zheng, Y.1    Zhong, L.2    Shen, X.3
  • 37
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A.J., Lodish, H.F., Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257 (1992), 1496–1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 39
    • 77953703354 scopus 로고    scopus 로고
    • Redox state of the endoplasmic reticulum is controlled by Ero1L-alpha and intraluminal calcium
    • Enyedi, B., Varnai, P., Geiszt, M., Redox state of the endoplasmic reticulum is controlled by Ero1L-alpha and intraluminal calcium. Antioxid. Redox Signal. 13 (2010), 721–729.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 721-729
    • Enyedi, B.1    Varnai, P.2    Geiszt, M.3
  • 40
    • 0347753252 scopus 로고    scopus 로고
    • Ca2+-dependent redox modulation of SERCA 2b by ERp57
    • Li, Y., Camacho, P., Ca2+-dependent redox modulation of SERCA 2b by ERp57. J. Cell Biol. 164 (2004), 35–46.
    • (2004) J. Cell Biol. , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 41
    • 0032502777 scopus 로고    scopus 로고
    • A new human selenium-containing protein. Purification, characterization, and cDNA sequence
    • Gladyshev, V.N., Jeang, K.T., Wootton, J.C., Hatfield, D.L., A new human selenium-containing protein. Purification, characterization, and cDNA sequence. J. Biol. Chem. 273 (1998), 8910–8915.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8910-8915
    • Gladyshev, V.N.1    Jeang, K.T.2    Wootton, J.C.3    Hatfield, D.L.4
  • 42
    • 0035805615 scopus 로고    scopus 로고
    • Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells
    • Korotkov, K.V., Kumaraswamy, E., Zhou, Y., Hatfield, D.L., Gladyshev, V.N., Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. J. Biol. Chem. 276 (2001), 15330–15336.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15330-15336
    • Korotkov, K.V.1    Kumaraswamy, E.2    Zhou, Y.3    Hatfield, D.L.4    Gladyshev, V.N.5
  • 43
    • 27844454857 scopus 로고    scopus 로고
    • A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase
    • Labunskyy, V.M., Ferguson, A.D., Fomenko, D.E., Chelliah, Y., Hatfield, D.L., Gladyshev, V.N., A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase. J. Biol. Chem. 280 (2005), 37839–37845.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37839-37845
    • Labunskyy, V.M.1    Ferguson, A.D.2    Fomenko, D.E.3    Chelliah, Y.4    Hatfield, D.L.5    Gladyshev, V.N.6
  • 46
    • 69749100361 scopus 로고    scopus 로고
    • Sep15 a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses
    • Labunskyy, V.M., Yoo, M.H., Hatfield, D.L., Gladyshev, V.N., Sep15 a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses. Biochemistry 48 (2009), 8458–8465.
    • (2009) Biochemistry , vol.48 , pp. 8458-8465
    • Labunskyy, V.M.1    Yoo, M.H.2    Hatfield, D.L.3    Gladyshev, V.N.4
  • 50
    • 80053208250 scopus 로고    scopus 로고
    • Deficiency in the 15 kDa selenoprotein inhibits human colon cancer cell growth
    • Tsuji, P.A., Naranjo-Suarez, S., Carlson, B.A., Tobe, R., Yoo, M.H., Davis, C.D., Deficiency in the 15 kDa selenoprotein inhibits human colon cancer cell growth. Nutrients 3 (2011), 805–817.
    • (2011) Nutrients , vol.3 , pp. 805-817
    • Tsuji, P.A.1    Naranjo-Suarez, S.2    Carlson, B.A.3    Tobe, R.4    Yoo, M.H.5    Davis, C.D.6
  • 53
    • 79951831744 scopus 로고    scopus 로고
    • Selenoprotein K knockout mice exhibit deficient calcium flux in immune cells and impaired immune responses
    • Verma, S., Hoffmann, F.W., Kumar, M., Huang, Z., Roe, K., Nguyen-Wu, E., Hashimoto, A.S., Hoffmann, P.R., Selenoprotein K knockout mice exhibit deficient calcium flux in immune cells and impaired immune responses. J. Immunol. 186 (2011), 2127–2137.
    • (2011) J. Immunol. , vol.186 , pp. 2127-2137
    • Verma, S.1    Hoffmann, F.W.2    Kumar, M.3    Huang, Z.4    Roe, K.5    Nguyen-Wu, E.6    Hashimoto, A.S.7    Hoffmann, P.R.8
  • 54
    • 84942790786 scopus 로고    scopus 로고
    • Membrane-bound selenoproteins
    • Liu, J., Rozovsky, S., Membrane-bound selenoproteins. Antioxid. Redox Signal. 23 (2015), 795–813.
    • (2015) Antioxid. Redox Signal. , vol.23 , pp. 795-813
    • Liu, J.1    Rozovsky, S.2
  • 55
    • 84959081629 scopus 로고    scopus 로고
    • Deducing the functional characteristics of the human selenoprotein SELK from the structural properties of its intrinsically disordered C-terminal domain
    • Polo, A., Colonna, G., Guariniello, S., Ciliberto, G., Costantini, S., Deducing the functional characteristics of the human selenoprotein SELK from the structural properties of its intrinsically disordered C-terminal domain. Mol. Biosyst. 12 (2016), 758–772.
    • (2016) Mol. Biosyst. , vol.12 , pp. 758-772
    • Polo, A.1    Colonna, G.2    Guariniello, S.3    Ciliberto, G.4    Costantini, S.5
  • 56
    • 77956343086 scopus 로고    scopus 로고
    • SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis
    • Du, S., Zhou, J., Jia, Y., Huang, K., SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis. Arch. Biochem. Biophys. 502 (2010), 137–143.
    • (2010) Arch. Biochem. Biophys. , vol.502 , pp. 137-143
    • Du, S.1    Zhou, J.2    Jia, Y.3    Huang, K.4
  • 57
    • 83355169736 scopus 로고    scopus 로고
    • Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis
    • Shchedrina, V.A., Everley, R.A., Zhang, Y., Gygi, S.P., Hatfield, D.L., Gladyshev, V.N., Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis. J. Biol. Chem. 286 (2011), 42937–42948.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42937-42948
    • Shchedrina, V.A.1    Everley, R.A.2    Zhang, Y.3    Gygi, S.P.4    Hatfield, D.L.5    Gladyshev, V.N.6
  • 58
    • 84949662465 scopus 로고    scopus 로고
    • Selenoprotein S-dependent selenoprotein K binding to p97(VCP) protein is essential for endoplasmic reticulum-associated degradation
    • Lee, J.H., Park, K.J., Jang, J.K., Jeon, Y.H., Ko, K.Y., Kwon, J.H., Lee, S.R., Kim, I.Y., Selenoprotein S-dependent selenoprotein K binding to p97(VCP) protein is essential for endoplasmic reticulum-associated degradation. J. Biol. Chem. 290 (2015), 29941–29952.
    • (2015) J. Biol. Chem. , vol.290 , pp. 29941-29952
    • Lee, J.H.1    Park, K.J.2    Jang, J.K.3    Jeon, Y.H.4    Ko, K.Y.5    Kwon, J.H.6    Lee, S.R.7    Kim, I.Y.8
  • 59
    • 84919487651 scopus 로고    scopus 로고
    • Stable expression and function of the inositol 1,4,5-triphosphate receptor requires palmitoylation by a DHHC6/selenoprotein K complex
    • Fredericks, G.J., Hoffmann, F.W., Rose, A.H., Osterheld, H.J., Hess, F.M., Mercier, F., Hoffmann, P.R., Stable expression and function of the inositol 1,4,5-triphosphate receptor requires palmitoylation by a DHHC6/selenoprotein K complex. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 16478–16483.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 16478-16483
    • Fredericks, G.J.1    Hoffmann, F.W.2    Rose, A.H.3    Osterheld, H.J.4    Hess, F.M.5    Mercier, F.6    Hoffmann, P.R.7
  • 60
    • 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
  • 61
    • 84908669654 scopus 로고    scopus 로고
    • Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential
    • Liu, J., Zhang, Z., Rozovsky, S., Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential. FEBS Lett. 588 (2014), 3311–3321.
    • (2014) FEBS Lett. , vol.588 , pp. 3311-3321
    • Liu, J.1    Zhang, Z.2    Rozovsky, S.3
  • 62
    • 85011826492 scopus 로고    scopus 로고
    • Selenoprotein K modulate intracellular free Ca2+ by regulating expression of calcium homoeostasis endoplasmic reticulum protein
    • Wang, C., Li, R., Huang, Y., Wang, M., Yang, F., Huang, D., Wu, C., Li, Y., Tang, Y., Zhang, R., Cheng, J., Selenoprotein K modulate intracellular free Ca2+ by regulating expression of calcium homoeostasis endoplasmic reticulum protein. Biochem. Biophys. Res. Commun. 484 (2017), 734–739.
    • (2017) Biochem. Biophys. Res. Commun. , vol.484 , pp. 734-739
    • Wang, C.1    Li, R.2    Huang, Y.3    Wang, M.4    Yang, F.5    Huang, D.6    Wu, C.7    Li, Y.8    Tang, Y.9    Zhang, R.10    Cheng, J.11
  • 63
    • 0036170524 scopus 로고    scopus 로고
    • Mammalian selenoprotein in which selenocysteine (Sec) incorporation is supported by a new form of Sec insertion sequence element
    • Korotkov, K.V., Novoselov, S.V., Hatfield, D.L., Gladyshev, V.N., Mammalian selenoprotein in which selenocysteine (Sec) incorporation is supported by a new form of Sec insertion sequence element. Mol. Cell. Biol. 22 (2002), 1402–1411.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1402-1411
    • Korotkov, K.V.1    Novoselov, S.V.2    Hatfield, D.L.3    Gladyshev, V.N.4
  • 65
    • 84961063116 scopus 로고    scopus 로고
    • Characterization of selenoprotein M and its response to selenium deficiency in chicken brain
    • Huang, J.Q., Ren, F.Z., Jiang, Y.Y., Lei, X., Characterization of selenoprotein M and its response to selenium deficiency in chicken brain. Biol. Trace Elem. Res. 170 (2016), 449–458.
    • (2016) Biol. Trace Elem. Res. , vol.170 , pp. 449-458
    • Huang, J.Q.1    Ren, F.Z.2    Jiang, Y.Y.3    Lei, X.4
  • 66
    • 77649242103 scopus 로고    scopus 로고
    • The neuroprotective functions of selenoprotein M and its role in cytosolic calcium regulation
    • Reeves, M.A., Bellinger, F.P., Berry, M.J., The neuroprotective functions of selenoprotein M and its role in cytosolic calcium regulation. Antioxid. Redox Signal. 12 (2010), 809–818.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 809-818
    • Reeves, M.A.1    Bellinger, F.P.2    Berry, M.J.3
  • 67
    • 27644459819 scopus 로고    scopus 로고
    • Differentially expressed genes in transgenic mice carrying human mutant presenilin-2 (N141I): correlation of selenoprotein M with Alzheimer's disease
    • Hwang, D.Y., Cho, J.S., Oh, J.H., Shim, S.B., Jee, S.W., Lee, S.H., Seo, S.J., Lee, S.K., Lee, S.H., Kim, Y.K., Differentially expressed genes in transgenic mice carrying human mutant presenilin-2 (N141I): correlation of selenoprotein M with Alzheimer's disease. Neurochem. Res. 30 (2005), 1009–1019.
    • (2005) Neurochem. Res. , vol.30 , pp. 1009-1019
    • Hwang, D.Y.1    Cho, J.S.2    Oh, J.H.3    Shim, S.B.4    Jee, S.W.5    Lee, S.H.6    Seo, S.J.7    Lee, S.K.8    Lee, S.H.9    Kim, Y.K.10
  • 68
    • 77449105037 scopus 로고    scopus 로고
    • Presenilin-2 dampens intracellular Ca2+ stores by increasing Ca2+ leakage and reducing Ca2+ uptake
    • Brunello, L., Zampese, E., Florean, C., Pozzan, T., Pizzo, P., Fasolato, C., Presenilin-2 dampens intracellular Ca2+ stores by increasing Ca2+ leakage and reducing Ca2+ uptake. J. Cell. Mol. Med. 13 (2009), 3358–3369.
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 3358-3369
    • Brunello, L.1    Zampese, E.2    Florean, C.3    Pozzan, T.4    Pizzo, P.5    Fasolato, C.6
  • 70
    • 43649083316 scopus 로고    scopus 로고
    • The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway
    • Ferreiro, E., Oliveira, C.R., Pereira, C.M., The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway. Neurobiol. Dis. 30 (2008), 331–342.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 331-342
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.M.3
  • 71
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1–42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • Resende, R., Ferreiro, E., Pereira, C., Resende de Oliveira, C., Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1–42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death. Neuroscience 155 (2008), 725–737.
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Resende de Oliveira, C.4
  • 72
    • 84875065421 scopus 로고    scopus 로고
    • Different forms of selenoprotein M differentially affect abeta aggregation and ROS generation
    • Chen, P., Wang, R.R., Ma, X.J., Liu, Q., Ni, J.Z., Different forms of selenoprotein M differentially affect abeta aggregation and ROS generation. Int. J. Mol. Sci. 14 (2013), 4385–4399.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 4385-4399
    • Chen, P.1    Wang, R.R.2    Ma, X.J.3    Liu, Q.4    Ni, J.Z.5
  • 73
    • 84879861295 scopus 로고    scopus 로고
    • Selenoprotein P and selenoprotein M block Zn2+ -mediated Abeta42 aggregation and toxicity
    • Du, X., Li, H., Wang, Z., Qiu, S., Liu, Q., Ni, J., Selenoprotein P and selenoprotein M block Zn2+ -mediated Abeta42 aggregation and toxicity. Metallomics 5 (2013), 861–870.
    • (2013) Metallomics , vol.5 , pp. 861-870
    • Du, X.1    Li, H.2    Wang, Z.3    Qiu, S.4    Liu, Q.5    Ni, J.6
  • 74
    • 67649552785 scopus 로고    scopus 로고
    • ERK activation induced by selenium treatment significantly downregulates beta/gamma-secretase activity and Tau phosphorylation in the transgenic rat overexpressing human selenoprotein M
    • Yim, S.Y., Chae, K.R., Shim, S.B., Hong, J.T., Park, J.Y., Lee, C.Y., Son, H.J., Sheen, Y.Y., Hwang, D.Y., ERK activation induced by selenium treatment significantly downregulates beta/gamma-secretase activity and Tau phosphorylation in the transgenic rat overexpressing human selenoprotein M. Int. J. Mol. Med. 24 (2009), 91–96.
    • (2009) Int. J. Mol. Med. , vol.24 , pp. 91-96
    • Yim, S.Y.1    Chae, K.R.2    Shim, S.B.3    Hong, J.T.4    Park, J.Y.5    Lee, C.Y.6    Son, H.J.7    Sheen, Y.Y.8    Hwang, D.Y.9
  • 75
    • 84908069727 scopus 로고    scopus 로고
    • Identification of the responsible proteins for increased selenium bioavailability in the brain of transgenic rats overexpressing selenoprotein M
    • Kim, Y., Goo, J.S., Kim, I.Y., Kim, J.E., Kwak, M.H., Go, J., Shim, S., Hong, J.T., Hwang, D.Y., Seong, J.K., Identification of the responsible proteins for increased selenium bioavailability in the brain of transgenic rats overexpressing selenoprotein M. Int. J. Mol. Med. 34 (2014), 1688–1698.
    • (2014) Int. J. Mol. Med. , vol.34 , pp. 1688-1698
    • Kim, Y.1    Goo, J.S.2    Kim, I.Y.3    Kim, J.E.4    Kwak, M.H.5    Go, J.6    Shim, S.7    Hong, J.T.8    Hwang, D.Y.9    Seong, J.K.10
  • 76
    • 0033621335 scopus 로고    scopus 로고
    • Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif
    • Lescure, A., Gautheret, D., Carbon, P., Krol, A., Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J. Biol. Chem. 274 (1999), 38147–38154.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38147-38154
    • Lescure, A.1    Gautheret, D.2    Carbon, P.3    Krol, A.4
  • 77
    • 84867330926 scopus 로고    scopus 로고
    • Selenoprotein N in skeletal muscle: from diseases to function
    • Castets, P., Lescure, A., Guicheney, P., Allamand, V., Selenoprotein N in skeletal muscle: from diseases to function. J Mol Med (Berl) 90 (2012), 1095–1107.
    • (2012) J Mol Med (Berl) , vol.90 , pp. 1095-1107
    • Castets, P.1    Lescure, A.2    Guicheney, P.3    Allamand, V.4
  • 81
    • 77649249653 scopus 로고    scopus 로고
    • Selenoproteins and protection against oxidative stress: selenoprotein N as a novel player at the crossroads of redox signaling and calcium homeostasis
    • Arbogast, S., Ferreiro, A., Selenoproteins and protection against oxidative stress: selenoprotein N as a novel player at the crossroads of redox signaling and calcium homeostasis. Antioxid. Redox Signal. 12 (2010), 893–904.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 893-904
    • Arbogast, S.1    Ferreiro, A.2
  • 83
    • 84926475413 scopus 로고    scopus 로고
    • SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activity
    • Marino, M., Stoilova, T., Giorgi, C., Bachi, A., Cattaneo, A., Auricchio, A., Pinton, P., Zito, E., SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activity. Hum. Mol. Genet. 24 (2015), 1843–1855.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 1843-1855
    • Marino, M.1    Stoilova, T.2    Giorgi, C.3    Bachi, A.4    Cattaneo, A.5    Auricchio, A.6    Pinton, P.7    Zito, E.8
  • 84
    • 67650066807 scopus 로고    scopus 로고
    • Oxidative stress in SEPN1-related myopathy: from pathophysiology to treatment
    • Arbogast, S., Beuvin, M., Fraysse, B., Zhou, H., Muntoni, F., Ferreiro, A., Oxidative stress in SEPN1-related myopathy: from pathophysiology to treatment. Ann. Neurol. 65 (2009), 677–686.
    • (2009) Ann. Neurol. , vol.65 , pp. 677-686
    • Arbogast, S.1    Beuvin, M.2    Fraysse, B.3    Zhou, H.4    Muntoni, F.5    Ferreiro, A.6
  • 85
    • 85009912613 scopus 로고    scopus 로고
    • ER-luminal thiol/selenol-mediated regulation of Ca2+ signalling
    • Appenzeller-Herzog, C., Simmen, T., ER-luminal thiol/selenol-mediated regulation of Ca2+ signalling. Biochem. Soc. Trans. 44 (2016), 452–459.
    • (2016) Biochem. Soc. Trans. , vol.44 , pp. 452-459
    • Appenzeller-Herzog, C.1    Simmen, T.2
  • 86
    • 85007499651 scopus 로고    scopus 로고
    • Targeted next generation sequencing identifies two novel mutations in SEPN1 in rigid spine muscular dystrophy 1
    • Dai, Y., Liang, S., Huang, Y., Chen, L., Banerjee, S., Targeted next generation sequencing identifies two novel mutations in SEPN1 in rigid spine muscular dystrophy 1. Oncotarget 7 (2016), 83843–83849.
    • (2016) Oncotarget , vol.7 , pp. 83843-83849
    • Dai, Y.1    Liang, S.2    Huang, Y.3    Chen, L.4    Banerjee, S.5
  • 88
    • 84923922028 scopus 로고    scopus 로고
    • Calcium binding proteins and calcium signaling in prokaryotes
    • Dominguez, D.C., Guragain, M., Patrauchan, M., Calcium binding proteins and calcium signaling in prokaryotes. Cell Calcium 57 (2015), 151–165.
    • (2015) Cell Calcium , vol.57 , pp. 151-165
    • Dominguez, D.C.1    Guragain, M.2    Patrauchan, M.3
  • 90
    • 33845784175 scopus 로고    scopus 로고
    • Loss of selenoprotein N function causes disruption of muscle architecture in the zebrafish embryo
    • Deniziak, M., Thisse, C., Rederstorff, M., Hindelang, C., Thisse, B., Lescure, A., Loss of selenoprotein N function causes disruption of muscle architecture in the zebrafish embryo. Exp. Cell Res. 313 (2007), 156–167.
    • (2007) Exp. Cell Res. , vol.313 , pp. 156-167
    • Deniziak, M.1    Thisse, C.2    Rederstorff, M.3    Hindelang, C.4    Thisse, B.5    Lescure, A.6
  • 92
    • 84876183504 scopus 로고    scopus 로고
    • Alternative transcripts and 3’UTR elements govern the incorporation of selenocysteine into selenoprotein S
    • Bubenik, J.L., Miniard, A.C., Driscoll, D.M., Alternative transcripts and 3’UTR elements govern the incorporation of selenocysteine into selenoprotein S. PLoS One, 8, 2013, e62102.
    • (2013) PLoS One , vol.8 , pp. e62102
    • Bubenik, J.L.1    Miniard, A.C.2    Driscoll, D.M.3
  • 93
    • 84901003345 scopus 로고    scopus 로고
    • Pro178 and Pro183 of selenoprotein S are essential residues for interaction with p97(VCP) during endoplasmic reticulum-associated degradation
    • Lee, J.H., Kwon, J.H., Jeon, Y.H., Ko, K.Y., Lee, S.R., Kim, I.Y., Pro178 and Pro183 of selenoprotein S are essential residues for interaction with p97(VCP) during endoplasmic reticulum-associated degradation. J. Biol. Chem. 289 (2014), 13758–13768.
    • (2014) J. Biol. Chem. , vol.289 , pp. 13758-13768
    • Lee, J.H.1    Kwon, J.H.2    Jeon, Y.H.3    Ko, K.Y.4    Lee, S.R.5    Kim, I.Y.6
  • 94
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D., Rapoport, T.A., A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429 (2004), 841–847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 95
    • 84963617847 scopus 로고    scopus 로고
    • Structure and function of the AAA+ ATPase p97/Cdc48p
    • Xia, D., Tang, W.K., Ye, Y., Structure and function of the AAA+ ATPase p97/Cdc48p. Gene 583 (2016), 64–77.
    • (2016) Gene , vol.583 , pp. 64-77
    • Xia, D.1    Tang, W.K.2    Ye, Y.3
  • 96
    • 84877320659 scopus 로고    scopus 로고
    • The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro
    • Liu, J., Li, F., Rozovsky, S., The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro. Biochemistry 52 (2013), 3051–3061.
    • (2013) Biochemistry , vol.52 , pp. 3051-3061
    • Liu, J.1    Li, F.2    Rozovsky, S.3
  • 97
    • 84882599837 scopus 로고    scopus 로고
    • Contribution of selenocysteine to the peroxidase activity of selenoprotein S
    • Liu, J., Rozovsky, S., Contribution of selenocysteine to the peroxidase activity of selenoprotein S. Biochemistry 52 (2013), 5514–5516.
    • (2013) Biochemistry , vol.52 , pp. 5514-5516
    • Liu, J.1    Rozovsky, S.2
  • 98
    • 84864390276 scopus 로고    scopus 로고
    • The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region
    • Christensen, L.C., Jensen, N.W., Vala, A., Kamarauskaite, J., Johansson, L., Winther, J.R., Hofmann, K., Teilum, K., Ellgaard, L., The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region. J. Biol. Chem. 287 (2012), 26388–26399.
    • (2012) J. Biol. Chem. , vol.287 , pp. 26388-26399
    • Christensen, L.C.1    Jensen, N.W.2    Vala, A.3    Kamarauskaite, J.4    Johansson, L.5    Winther, J.R.6    Hofmann, K.7    Teilum, K.8    Ellgaard, L.9
  • 101
    • 1842737643 scopus 로고    scopus 로고
    • Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress − SelS is a novel glucose-regulated protein
    • Gao, Y., Feng, H.C., Walder, K., Bolton, K., Sunderland, T., Bishara, N., Quick, M., Kantham, L., Collier, G.R., Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress − SelS is a novel glucose-regulated protein. FEBS Lett. 563 (2004), 185–190.
    • (2004) FEBS Lett. , vol.563 , pp. 185-190
    • Gao, Y.1    Feng, H.C.2    Walder, K.3    Bolton, K.4    Sunderland, T.5    Bishara, N.6    Quick, M.7    Kantham, L.8    Collier, G.R.9
  • 103
    • 0033607529 scopus 로고    scopus 로고
    • New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements
    • Kryukov, G.V., Kryukov, V.M., Gladyshev, V.N., New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements. J. Biol. Chem. 274 (1999), 33888–33897.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33888-33897
    • Kryukov, G.V.1    Kryukov, V.M.2    Gladyshev, V.N.3
  • 111
    • 0036191639 scopus 로고    scopus 로고
    • Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases
    • Bianco, A.C., Salvatore, D., Gereben, B., Berry, M.J., Larsen, P.R., Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases. Endocr. Rev. 23 (2002), 38–89.
    • (2002) Endocr. Rev. , vol.23 , pp. 38-89
    • Bianco, A.C.1    Salvatore, D.2    Gereben, B.3    Berry, M.J.4    Larsen, P.R.5
  • 112
    • 80052266598 scopus 로고    scopus 로고
    • Type 2 deiodinase at the crossroads of thyroid hormone action
    • Arrojo, E.D.R., Bianco, A.C., Type 2 deiodinase at the crossroads of thyroid hormone action. Int. J. Biochem. Cell Biol. 43 (2011), 1432–1441.
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1432-1441
    • Arrojo, E.D.R.1    Bianco, A.C.2
  • 113
    • 0033680077 scopus 로고    scopus 로고
    • Distinct subcellular localization of transiently expressed types 1 and 2 iodothyronine deiodinases as determined by immunofluorescence confocal microscopy
    • Baqui, M.M., Gereben, B., Harney, J.W., Larsen, P.R., Bianco, A.C., Distinct subcellular localization of transiently expressed types 1 and 2 iodothyronine deiodinases as determined by immunofluorescence confocal microscopy. Endocrinology 141 (2000), 4309–4312.
    • (2000) Endocrinology , vol.141 , pp. 4309-4312
    • Baqui, M.M.1    Gereben, B.2    Harney, J.W.3    Larsen, P.R.4    Bianco, A.C.5
  • 116
    • 84888371632 scopus 로고    scopus 로고
    • The type II deiodinase is retrotranslocated to the cytoplasm and proteasomes via p97/Atx3 complex
    • Arrojo, E.D.R., Egri, P., Jo, S., Gereben, B., Bianco, A.C., The type II deiodinase is retrotranslocated to the cytoplasm and proteasomes via p97/Atx3 complex. Mol. Endocrinol. 27 (2013), 2105–2115.
    • (2013) Mol. Endocrinol. , vol.27 , pp. 2105-2115
    • Arrojo, E.D.R.1    Egri, P.2    Jo, S.3    Gereben, B.4    Bianco, A.C.5
  • 117
    • 85047690484 scopus 로고    scopus 로고
    • Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation
    • Curcio-Morelli, C., Zavacki, A.M., Christofollete, M., Gereben, B., de Freitas, B.C., Harney, J.W., Li, Z., Wu, G., Bianco, A.C., Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation. J. Clin. Invest. 112 (2003), 189–196.
    • (2003) J. Clin. Invest. , vol.112 , pp. 189-196
    • Curcio-Morelli, C.1    Zavacki, A.M.2    Christofollete, M.3    Gereben, B.4    de Freitas, B.C.5    Harney, J.W.6    Li, Z.7    Wu, G.8    Bianco, A.C.9
  • 118
    • 82055194436 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress decreases intracellular thyroid hormone activation via an eIF2a-mediated decrease in type 2 deiodinase synthesis
    • Arrojo, E.D.R., Fonseca, T.L., Castillo, M., Salathe, M., Simovic, G., Mohacsik, P., Gereben, B., Bianco, A.C., Endoplasmic reticulum stress decreases intracellular thyroid hormone activation via an eIF2a-mediated decrease in type 2 deiodinase synthesis. Mol. Endocrinol. 25 (2011), 2065–2075.
    • (2011) Mol. Endocrinol. , vol.25 , pp. 2065-2075
    • Arrojo, E.D.R.1    Fonseca, T.L.2    Castillo, M.3    Salathe, M.4    Simovic, G.5    Mohacsik, P.6    Gereben, B.7    Bianco, A.C.8
  • 119
    • 84976320028 scopus 로고    scopus 로고
    • Tissue thyroid hormones and thyronamines
    • Accorroni, A., Saponaro, F., Zucchi, R., Tissue thyroid hormones and thyronamines. Heart Fail. Rev. 21 (2016), 373–390.
    • (2016) Heart Fail. Rev. , vol.21 , pp. 373-390
    • Accorroni, A.1    Saponaro, F.2    Zucchi, R.3
  • 120
    • 23744445796 scopus 로고    scopus 로고
    • Thyroid hormone action in the heart
    • Kahaly, G.J., Dillmann, W.H., Thyroid hormone action in the heart. Endocr. Rev. 26 (2005), 704–728.
    • (2005) Endocr. Rev. , vol.26 , pp. 704-728
    • Kahaly, G.J.1    Dillmann, W.H.2


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