메뉴 건너뛰기




Volumn 7, Issue 5, 2015, Pages 3938-3948

The subcellular location of selenoproteins and the impact on their function

Author keywords

Cancer; Compartmentalization; Peroxidases; Selenium; Selenoproteins

Indexed keywords

GLUTATHIONE PEROXIDASE 1; HYPOXIA INDUCIBLE FACTOR 1ALPHA; KELCH LIKE ECH ASSOCIATED PROTEIN 1; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; PROTEIN SERINE THREONINE KINASE; SELENIUM BINDING PROTEIN; SELENIUM BINDING PROTEIN 1; SELENOPROTEIN; SIRTUIN 3; THIOREDOXIN REDUCTASE; THIOREDOXIN REDUCTASE 1; THIOREDOXIN REDUCTASE 2; UNCLASSIFIED DRUG; GLUTATHIONE PEROXIDASE; SELENBP1 PROTEIN, HUMAN; SELENIUM; SELENOCYSTEINE;

EID: 84930960163     PISSN: None     EISSN: 20726643     Source Type: Journal    
DOI: 10.3390/nu7053938     Document Type: Review
Times cited : (35)

References (71)
  • 1
    • 84903600136 scopus 로고    scopus 로고
    • Selenoproteins: Molecular pathways and physiological roles
    • Labunskyy, V.M.; Hatfield, D.L.; Gladyshev, V.N. Selenoproteins: Molecular pathways and physiological roles. Physiol. Rev. 2014, 94, 739–777.
    • (2014) Physiol. Rev , vol.94 , pp. 739-777
    • Labunskyy, V.M.1    Hatfield, D.L.2    Gladyshev, V.N.3
  • 3
    • 0025743489 scopus 로고
    • Recognition of UGA as a selenocysteine codon in Type I deiodinase requires sequences in the 3′ untranslated region
    • Berry, M.J.; Banu, L.; Chen, Y.; Mandel, S.J.; Kiefer, J.D.; Harney, J.W.; Larsen, P.R. Recognition of UGA as a selenocysteine codon in Type I deiodinase requires sequences in the 3′ untranslated region. Nature 1991, 353, 273–276.
    • (1991) Nature , vol.353 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Chen, Y.3    Mandel, S.J.4    Kiefer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 5
    • 68749110874 scopus 로고    scopus 로고
    • Regulation and function of selenoproteins in human disease
    • Bellinger, F.P.; Raman, A.V.; Reeves, M.A.; Berry, M.J. Regulation and function of selenoproteins in human disease. Biochem. J. 2009, 422, 11–22.
    • (2009) Biochem. J , vol.422 , pp. 11-22
    • Bellinger, F.P.1    Raman, A.V.2    Reeves, M.A.3    Berry, M.J.4
  • 6
    • 0041317009 scopus 로고    scopus 로고
    • Mechanism and regulation of selenoprotein synthesis
    • Driscoll, D.M.; Copeland, P.R. Mechanism and regulation of selenoprotein synthesis. Annu. Rev. Nutr. 2003, 23, 17–40.
    • (2003) Annu. Rev. Nutr , vol.23 , pp. 17-40
    • Driscoll, D.M.1    Copeland, P.R.2
  • 7
    • 84891464515 scopus 로고    scopus 로고
    • Molecular cross-talk between members of distinct families of selenium containing proteins
    • Ansong, E.; Yang, W.; Diamond, A.M. Molecular cross-talk between members of distinct families of selenium containing proteins. Mol. Nutr. Food Res. 2014, 58, 117–123.
    • (2014) Mol. Nutr. Food Res , vol.58 , pp. 117-123
    • Ansong, E.1    Yang, W.2    Diamond, A.M.3
  • 8
    • 73049099869 scopus 로고    scopus 로고
    • The labour pains of biochemical selenology: The history of selenoprotein biosynthesis
    • Flohe, L. The labour pains of biochemical selenology: The history of selenoprotein biosynthesis. Biochim. Biophys. Acta 2009, 1790, 1389–1403.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1389-1403
    • Flohe, L.1
  • 10
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-kappaB: Players, pathways, perspectives
    • Gilmore, T.D. Introduction to NF-kappaB: Players, pathways, perspectives. Oncogene 2006, 25, 6680–6684.
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 11
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function
    • Perkins, N.D. Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat. Rev. Mol. Cell Biol. 2007, 8, 49–62.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 12
    • 40549118822 scopus 로고    scopus 로고
    • The nuclear affairs of PTEN
    • Planchon, S.M.; Waite, K.A.; Eng, C. The nuclear affairs of PTEN. J. Cell Sci. 2008, 121 (Pt 3), 249–253.
    • (2008) J. Cell Sci , vol.121 , pp. 249-253
    • Planchon, S.M.1    Waite, K.A.2    Eng, C.3
  • 14
    • 84885944468 scopus 로고    scopus 로고
    • The emerging role of the Nrf2-Keap1 signaling pathway in cancer
    • Jaramillo, M.C.; Zhang, D.D. The emerging role of the Nrf2-Keap1 signaling pathway in cancer. Genes Dev. 2013, 27, 2179–2191.
    • (2013) Genes Dev , vol.27 , pp. 2179-2191
    • Jaramillo, M.C.1    Zhang, D.D.2
  • 15
    • 53449101213 scopus 로고    scopus 로고
    • Molecular mechanisms of natural products in chemoprevention: Induction of cytoprotective enzymes by Nrf2
    • Eggler, A.L.; Gay, K.A.; Mesecar, A.D. Molecular mechanisms of natural products in chemoprevention: Induction of cytoprotective enzymes by Nrf2. Mol. Nutr. Food Res. 2008, 52 (Suppl. 1), S84–S94.
    • (2008) Mol. Nutr. Food Res , vol.52 , pp. S84-S94
    • Eggler, A.L.1    Gay, K.A.2    Mesecar, A.D.3
  • 16
    • 84897382168 scopus 로고    scopus 로고
    • Molecular responses to hypoxia-inducible factor 1alpha and beyond
    • Brocato, J.; Chervona, Y.; Costa, M. Molecular responses to hypoxia-inducible factor 1alpha and beyond. Mol. Pharmacol. 2014, 85, 651–657.
    • (2014) Mol. Pharmacol , vol.85 , pp. 651-657
    • Brocato, J.1    Chervona, Y.2    Costa, M.3
  • 17
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza, G.L. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer 2003, 3, 721–732.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 18
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini, F.; Maiorino, M.; Gregolin, C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 1985, 839, 62–70.
    • (1985) Biochim. Biophys. Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 19
    • 0020065662 scopus 로고
    • Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides
    • Ursini, F.; Maiorino, M.; Valente, M.; Ferri, L.; Gregolin, C. Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides. Biochim. Biophys. Acta 1982, 710, 197–211.
    • (1982) Biochim. Biophys. Acta , vol.710 , pp. 197-211
    • Ursini, F.1    Maiorino, M.2    Valente, M.3    Ferri, L.4    Gregolin, C.5
  • 20
    • 0037438730 scopus 로고    scopus 로고
    • Nakagawa, Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells
    • Imai, H.Y. Nakagawa, Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic. Biol. Med. 2003, 34, 145–169.
    • (2003) Free Radic. Biol. Med , vol.34 , pp. 145-169
    • Imai, H.Y.1
  • 21
    • 35348840292 scopus 로고    scopus 로고
    • Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals
    • Conrad, M.; Schneider, M.; Seiler, A.; Bornkamm, G.W. Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals. Biol. Chem. 2007, 388, 1019–1025.
    • (2007) Biol. Chem , vol.388 , pp. 1019-1025
    • Conrad, M.1    Schneider, M.2    Seiler, A.3    Bornkamm, G.W.4
  • 22
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • Brigelius-Flohe, R. Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 1999, 27, 951–965.
    • (1999) Free Radic. Biol. Med , vol.27 , pp. 951-965
    • Brigelius-Flohe, R.1
  • 23
    • 0030583593 scopus 로고    scopus 로고
    • Import into mitochondria of phospholipid hydroperoxide glutathione peroxidase requires a leader sequence
    • Arai, M.; Imai, H.; Sumi, D.; Imanaka, T.; Takano, T.; Chiba, N.; Nakagawa, Y. Import into mitochondria of phospholipid hydroperoxide glutathione peroxidase requires a leader sequence. Biochem. Biophys. Res. Commun. 1996, 227, 433–439.
    • (1996) Biochem. Biophys. Res. Commun , vol.227 , pp. 433-439
    • Arai, M.1    Imai, H.2    Sumi, D.3    Imanaka, T.4    Takano, T.5    Chiba, N.6    Nakagawa, Y.7
  • 24
    • 0028825467 scopus 로고
    • Rat phospholipid-hydroperoxide glutathione peroxidase. CDNA cloning and identification of multiple transcription and translation start sites
    • Pushpa-Rekha, T.R.; Burdsall, A.L.; Oleksa, L.M.; Chisolm, G.M.; Driscoll, D.M. Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites. J. Biol. Chem. 1995, 270, 26993–26999.
    • (1995) J. Biol. Chem , vol.270 , pp. 26993-26999
    • Pushpa-Rekha, T.R.1    Burdsall, A.L.2    Oleksa, L.M.3    Chisolm, G.M.4    Driscoll, D.M.5
  • 27
    • 34250887134 scopus 로고    scopus 로고
    • Tissue expression and cellular localization of phospholipid hydroperoxide glutathione peroxidase (PHGPx) mRNA in male mice
    • Baek, I.J.; Seo, D.S.; Yon, J.M.; Lee, S.R.; Jin, Y.; Nahm, S.S.; Jeong, J.H.; Choo, Y.K.; Kang, J.K.; Lee, B.J.; et al. Tissue expression and cellular localization of phospholipid hydroperoxide glutathione peroxidase (PHGPx) mRNA in male mice. J. Mol. Histol. 2007, 38, 237–244.
    • (2007) J. Mol. Histol , vol.38 , pp. 237-244
    • Baek, I.J.1    Seo, D.S.2    Yon, J.M.3    Lee, S.R.4    Jin, Y.5    Nahm, S.S.6    Jeong, J.H.7    Choo, Y.K.8    Kang, J.K.9    Lee, B.J.10
  • 28
    • 71449113005 scopus 로고    scopus 로고
    • Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions
    • Liang, H.; Yoo, S.E.; Na, R.; Walter, C.A.; Richardson, A.; Ran, Q. Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions. J. Biol. Chem. 2009, 284, 30836–30844.
    • (2009) J. Biol. Chem , vol.284 , pp. 30836-30844
    • Liang, H.1    Yoo, S.E.2    Na, R.3    Walter, C.A.4    Richardson, A.5    Ran, Q.6
  • 29
    • 0037508927 scopus 로고    scopus 로고
    • Testis-specific expression of the nuclear form of phospholipid hydroperoxide glutathione peroxidase (PHGPx)
    • Moreno, S.G.; Laux, G.; Brielmeier, M.; Bornkamm, G.W.; Conrad, M. Testis-specific expression of the nuclear form of phospholipid hydroperoxide glutathione peroxidase (PHGPx). Biol. Chem. 2003, 384, 635–643.
    • (2003) Biol. Chem , vol.384 , pp. 635-643
    • Moreno, S.G.1    Laux, G.2    Brielmeier, M.3    Bornkamm, G.W.4    Conrad, M.5
  • 30
    • 0141706719 scopus 로고    scopus 로고
    • Distinct promoters determine alternative transcription of gpx-4 into phospholipid-hydroperoxide glutathione peroxidase variants
    • Maiorino, M.; Scapin, M.; Ursini, F.; Biasolo, M.; Bosello, V.; Flohe, L. Distinct promoters determine alternative transcription of gpx-4 into phospholipid-hydroperoxide glutathione peroxidase variants. J. Biol. Chem. 2003, 278, 34286–34290.
    • (2003) J. Biol. Chem , vol.278 , pp. 34286-34290
    • Maiorino, M.1    Scapin, M.2    Ursini, F.3    Biasolo, M.4    Bosello, V.5    Flohe, L.6
  • 31
    • 84855719823 scopus 로고    scopus 로고
    • The nuclear form of glutathione peroxidase 4 is associated with sperm nuclear matrix and is required for proper paternal chromatin decondensation at fertilization
    • Puglisi, R.; Maccari, I.; Pipolo, S.; Conrad, M.; Mangia, F.; Boitani, C. The nuclear form of glutathione peroxidase 4 is associated with sperm nuclear matrix and is required for proper paternal chromatin decondensation at fertilization. J. Cell Physiol. 2012, 227, 1420–1427.
    • (2012) J. Cell Physiol , vol.227 , pp. 1420-1427
    • Puglisi, R.1    Maccari, I.2    Pipolo, S.3    Conrad, M.4    Mangia, F.5    Boitani, C.6
  • 32
    • 85008196287 scopus 로고    scopus 로고
    • The nuclear form of glutathione peroxidase 4 colocalizes and directly interacts with protamines in the nuclear matrix during mouse sperm chromatin assembly
    • Puglisi, R.; Maccari, I.; Pipolo, S.; Mangia, F.; Boitani, C. The nuclear form of glutathione peroxidase 4 colocalizes and directly interacts with protamines in the nuclear matrix during mouse sperm chromatin assembly. Spermatogenesis 2014, 4, e28460.
    • (2014) Spermatogenesis , vol.4
    • Puglisi, R.1    Maccari, I.2    Pipolo, S.3    Mangia, F.4    Boitani, C.5
  • 33
    • 23844508188 scopus 로고    scopus 로고
    • The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability
    • Conrad, M.; Moreno, S.G.; Sinowatz, F.; Ursini, F.; Kolle, S.; Roveri, A.; Brielmeier, M.; Wurst, W.; Maiorino, M.; Bornkamm, G.W. The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability. Mol. Cell. Biol. 2005, 25, 7637–7644.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 7637-7644
    • Conrad, M.1    Moreno, S.G.2    Sinowatz, F.3    Ursini, F.4    Kolle, S.5    Roveri, A.6    Brielmeier, M.7    Wurst, W.8    Maiorino, M.9    Bornkamm, G.W.10
  • 35
    • 80052000670 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 in health and disease: From molecular mechanisms to therapeutic opportunities
    • Lubos, E.; Loscalzo, J.; Handy, D.E. Glutathione peroxidase-1 in health and disease: From molecular mechanisms to therapeutic opportunities. Antioxid. Redox Signal. 2011, 15, 1957–1997.
    • (2011) Antioxid. Redox Signal , vol.15 , pp. 1957-1997
    • Lubos, E.1    Loscalzo, J.2    Handy, D.E.3
  • 36
    • 0025770091 scopus 로고
    • Exact ultrastructural localization of glutathione peroxidase in normal rat hepatocytes: Advantages of microwave fixation
    • Utsunomiya, H.; Komatsu, N.; Yoshimura, S.; Tsutsumi, Y.; Watanabe, K. Exact ultrastructural localization of glutathione peroxidase in normal rat hepatocytes: Advantages of microwave fixation. J. Histochem. Cytochem. 1991, 39, 1167–1174.
    • (1991) J. Histochem. Cytochem , vol.39 , pp. 1167-1174
    • Utsunomiya, H.1    Komatsu, N.2    Yoshimura, S.3    Tsutsumi, Y.4    Watanabe, K.5
  • 37
    • 0028169847 scopus 로고
    • Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: Quantitative analysis by postembedding method
    • Asayama, K.; Yokota, S.; Dobashi, K.; Hayashibe, H.; Kawaoi, A.; Nakazawa, S. Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: Quantitative analysis by postembedding method. Histochemistry 1994, 102, 213–219.
    • (1994) Histochemistry , vol.102 , pp. 213-219
    • Asayama, K.1    Yokota, S.2    Dobashi, K.3    Hayashibe, H.4    Kawaoi, A.5    Nakazawa, S.6
  • 38
    • 0031128356 scopus 로고    scopus 로고
    • The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver
    • Esworthy, R.S.; Ho, Y.S.; Chu, F.F. The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver. Arch. Biochem. Biophys. 1997, 340, 59–63.
    • (1997) Arch. Biochem. Biophys , vol.340 , pp. 59-63
    • Esworthy, R.S.1    Ho, Y.S.2    Chu, F.F.3
  • 39
    • 84907546630 scopus 로고    scopus 로고
    • Natural allelic variations in glutathione peroxidase-1 affect its subcellular localization and function
    • Bera, S.; Weinberg, F.; Ekoue, D.N.; Ansenberger-Fricano, K.; Mao, M.; Bonini, M.G.; Diamond, A.M. Natural allelic variations in glutathione peroxidase-1 affect its subcellular localization and function. Cancer Res. 2014, 74, 5118–5126.
    • (2014) Cancer Res , vol.74 , pp. 5118-5126
    • Bera, S.1    Weinberg, F.2    Ekoue, D.N.3    Ansenberger-Fricano, K.4    Mao, M.5    Bonini, M.G.6    Diamond, A.M.7
  • 41
    • 0038068938 scopus 로고    scopus 로고
    • Role of glutathione peroxidase 1 in breast cancer: Loss of heterozygosity and allelic differences in the response to selenium
    • Hu, Y.J.; Diamond, A.M. Role of glutathione peroxidase 1 in breast cancer: Loss of heterozygosity and allelic differences in the response to selenium. Cancer Res. 2003, 63, 3347–3351.
    • (2003) Cancer Res , vol.63 , pp. 3347-3351
    • Hu, Y.J.1    Diamond, A.M.2
  • 42
    • 74549209572 scopus 로고    scopus 로고
    • Chronic ethanol consumption induces global hepatic protein hyperacetylation
    • Shepard, B.D.; Tuma, D.J.; Tuma, P.L. Chronic ethanol consumption induces global hepatic protein hyperacetylation. Alcohol. Clin. Exp. Res. 2010, 34, 280–291.
    • (2010) Alcohol. Clin. Exp. Res , vol.34 , pp. 280-291
    • Shepard, B.D.1    Tuma, D.J.2    Tuma, P.L.3
  • 44
    • 84857883360 scopus 로고    scopus 로고
    • Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice
    • Fritz, K.S.; Galligan, J.J.; Hirschey, M.D.; Verdin, E.; Petersen, D.R. Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice. J. Proteome Res. 2012, 11, 1633–1643.
    • (2012) J. Proteome Res , vol.11 , pp. 1633-1643
    • Fritz, K.S.1    Galligan, J.J.2    Hirschey, M.D.3    Verdin, E.4    Petersen, D.R.5
  • 45
    • 0141994844 scopus 로고    scopus 로고
    • Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases
    • Cao, C.; Leng, Y.; Huang, W.; Liu, X.; Kufe, D. Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases. J. Biol. Chem. 2003, 278, 39609–39614.
    • (2003) J. Biol. Chem , vol.278 , pp. 39609-39614
    • Cao, C.1    Leng, Y.2    Huang, W.3    Liu, X.4    Kufe, D.5
  • 47
    • 33748882312 scopus 로고    scopus 로고
    • Gene x Gene interaction between MnSOD and GPX-1 and breast cancer risk: A nested case-control study
    • Cox, D.G.; Tamimi, R.M.; Hunter, D.J. Gene x Gene interaction between MnSOD and GPX-1 and breast cancer risk: A nested case-control study. BMC Cancer 2006, 6, 217.
    • (2006) BMC Cancer , vol.6
    • Cox, D.G.1    Tamimi, R.M.2    Hunter, D.J.3
  • 48
    • 77955410455 scopus 로고    scopus 로고
    • Functional and physical interaction between the selenium-binding protein 1 (SBP1) and the glutathione peroxidase 1 selenoprotein
    • Fang, W.; Goldberg, M.L.; Pohl, N.M.; Bi, X.; Tong, C.; Xiong, B.; Koh, T.J.; Diamond, A.M.; Yang, W. Functional and physical interaction between the selenium-binding protein 1 (SBP1) and the glutathione peroxidase 1 selenoprotein. Carcinogenesis 2010, 31, 1360–1366.
    • (2010) Carcinogenesis , vol.31 , pp. 1360-1366
    • Fang, W.1    Goldberg, M.L.2    Pohl, N.M.3    Bi, X.4    Tong, C.5    Xiong, B.6    Koh, T.J.7    Diamond, A.M.8    Yang, W.9
  • 49
    • 0025173296 scopus 로고
    • DNA sequencing of a mouse liver protein that binds selenium: Implications for selenium’s mechanism of action in cancer prevention
    • Bansal, M.P.; Mukhopadhyay, T.; Scott, J.; Cook, R.G.; Mukhopadhyay, R.; Medina, D. DNA sequencing of a mouse liver protein that binds selenium: Implications for selenium’s mechanism of action in cancer prevention. Carcinogenesis 1990, 11, 2071–2073.
    • (1990) Carcinogenesis , vol.11 , pp. 2071-2073
    • Bansal, M.P.1    Mukhopadhyay, T.2    Scott, J.3    Cook, R.G.4    Mukhopadhyay, R.5    Medina, D.6
  • 50
    • 0024565927 scopus 로고
    • Evidence for two selenium-binding proteins distinct from glutathione peroxidase in mouse liver
    • Bansal, M.P.; Oborn, C.J.; Danielson, K.G.; Medina, D. Evidence for two selenium-binding proteins distinct from glutathione peroxidase in mouse liver. Carcinogenesis 1989, 10, 541–546.
    • (1989) Carcinogenesis , vol.10 , pp. 541-546
    • Bansal, M.P.1    Oborn, C.J.2    Danielson, K.G.3    Medina, D.4
  • 51
    • 70649112334 scopus 로고    scopus 로고
    • Transcriptional regulation and biological functions of selenium-binding protein 1 in colorectal cancer in vitro and in nude mouse xenografts
    • Pohl, N.M.; Tong, C.; Fang, W.; Bi, X.; Li, T.; Yang, W. Transcriptional regulation and biological functions of selenium-binding protein 1 in colorectal cancer in vitro and in nude mouse xenografts. PLoS ONE 2009, 4, e7774.
    • (2009) Plos ONE , vol.4
    • Pohl, N.M.1    Tong, C.2    Fang, W.3    Bi, X.4    Li, T.5    Yang, W.6
  • 52
    • 84861786781 scopus 로고    scopus 로고
    • Decreased Selenium-Binding Protein 1 Enhances Glutathione Peroxidase 1 Activity and Downregulates HIF-1alpha to Promote Hepatocellular Carcinoma Invasiveness
    • Huang, C.; Ding, G.; Gu, C.; Zhou, J.; Kuang, M.; Ji, Y.; He, Y.; Kondo, T.; Fan, J. Decreased Selenium-Binding Protein 1 Enhances Glutathione Peroxidase 1 Activity and Downregulates HIF-1alpha to Promote Hepatocellular Carcinoma Invasiveness. Clin. Cancer Res. 2012, 18, 3042–3053.
    • (2012) Clin. Cancer Res , vol.18 , pp. 3042-3053
    • Huang, C.1    Ding, G.2    Gu, C.3    Zhou, J.4    Kuang, M.5    Ji, Y.6    He, Y.7    Kondo, T.8    Fan, J.9
  • 53
    • 84877990763 scopus 로고    scopus 로고
    • Reduced selenium-binding protein 1 in breast cancer correlates with poor survival and resistance to the anti-proliferative effects of selenium
    • Zhang, S.; Li, F.; Younes, M.; Liu, H.; Chen, C.; Yao, Q. Reduced selenium-binding protein 1 in breast cancer correlates with poor survival and resistance to the anti-proliferative effects of selenium. PLoS ONE 2013, 8, e63702.
    • (2013) Plos ONE , vol.8
    • Zhang, S.1    Li, F.2    Younes, M.3    Liu, H.4    Chen, C.5    Yao, Q.6
  • 54
    • 84875992483 scopus 로고    scopus 로고
    • Selenium-binding protein 1 may decrease gastric cellular proliferation and migration
    • Zhang, C.; Xu, W.; Pan, W.; Wang, N.; Li, G.; Fan, X.; Xu, X.; Shen, S.; Das, U.N. Selenium-binding protein 1 may decrease gastric cellular proliferation and migration. Int. J. Oncol. 2013, 42, 1620–1629.
    • (2013) Int. J. Oncol , vol.42 , pp. 1620-1629
    • Zhang, C.1    Xu, W.2    Pan, W.3    Wang, N.4    Li, G.5    Fan, X.6    Xu, X.7    Shen, S.8    Das, U.N.9
  • 55
    • 77950666530 scopus 로고    scopus 로고
    • Decreased selenium-binding protein 1 in esophageal adenocarcinoma results from posttranscriptional and epigenetic regulation and affects chemosensitivity
    • Silvers, A.L.; Lin, L.; Bass, A.J.; Chen, G.; Wang, Z.; Thomas, D.G.; Lin, J.; Giordano, T.J.; Orringer, M.B.; Beer, D.G.; et al. Decreased selenium-binding protein 1 in esophageal adenocarcinoma results from posttranscriptional and epigenetic regulation and affects chemosensitivity. Clin. Cancer Res. 2010, 16, 2009–2021.
    • (2010) Clin. Cancer Res , vol.16 , pp. 2009-2021
    • Silvers, A.L.1    Lin, L.2    Bass, A.J.3    Chen, G.4    Wang, Z.5    Thomas, D.G.6    Lin, J.7    Giordano, T.J.8    Orringer, M.B.9    Beer, D.G.10
  • 56
    • 84905906253 scopus 로고    scopus 로고
    • Human selenium binding protein-1 (HSP56) is a negative regulator of HIF-1alpha and suppresses the malignant characteristics of prostate cancer cells
    • Jeong, J.Y.; Zhou, J.R.; Gao, C.; Feldman, L.; Sytkowski, A.J. Human selenium binding protein-1 (hSP56) is a negative regulator of HIF-1alpha and suppresses the malignant characteristics of prostate cancer cells. BMB Rep. 2014, 47, 411–416.
    • (2014) BMB Rep , vol.47 , pp. 411-416
    • Jeong, J.Y.1    Zhou, J.R.2    Gao, C.3    Feldman, L.4    Sytkowski, A.J.5
  • 57
    • 58249108683 scopus 로고    scopus 로고
    • Human selenium binding protein-1 (HSP56) interacts with VDU1 in a selenium-dependent manner
    • Jeong, J.Y.; Wang, Y.; Sytkowski, A.J. Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner. Biochem. Biophys. Res. Commun. 2009, 379, 583–588.
    • (2009) Biochem. Biophys. Res. Commun , vol.379 , pp. 583-588
    • Jeong, J.Y.1    Wang, Y.2    Sytkowski, A.J.3
  • 58
    • 84901933025 scopus 로고    scopus 로고
    • Selenium-binding protein 1 as a tumor suppressor and a prognostic indicator of clinical outcome
    • Yang, W.; Diamond, A.M. Selenium-binding protein 1 as a tumor suppressor and a prognostic indicator of clinical outcome. Biomark. Res. 2013, 1, 15.
    • (2013) Biomark. Res , Issue.1
    • Yang, W.1    Diamond, A.M.2
  • 60
    • 79960320129 scopus 로고    scopus 로고
    • Reduced selenium-binding protein 1 is associated with poor survival rate in gastric carcinoma
    • Zhang, J.; Dong, W.G.; Lin, J. Reduced selenium-binding protein 1 is associated with poor survival rate in gastric carcinoma. Med. Oncol. 2011, 28, 481–487.
    • (2011) Med. Oncol , vol.28 , pp. 481-487
    • Zhang, J.1    Dong, W.G.2    Lin, J.3
  • 61
    • 84655176814 scopus 로고    scopus 로고
    • Altered expression of selenium-binding protein 1 in gastric carcinoma and precursor lesions
    • Zhang, J.; Zhan, N.; Dong, W.G. Altered expression of selenium-binding protein 1 in gastric carcinoma and precursor lesions. Med. Oncol. 2011, 28, 951–957.
    • (2011) Med. Oncol , vol.28 , pp. 951-957
    • Zhang, J.1    Zhan, N.2    Dong, W.G.3
  • 63
    • 84861100409 scopus 로고    scopus 로고
    • Inverse association between glutathione peroxidase activity and both selenium-binding protein 1 levels and Gleason score in human prostate tissue
    • Jerome-Morais, A.; Wright, M.E.; Liu, R.; Yang, W.; Jackson, M.I.; Combs, G.F., Jr.; Diamond, A.M. Inverse association between glutathione peroxidase activity and both selenium-binding protein 1 levels and Gleason score in human prostate tissue. Prostate 2012, 72, 1006–1012.
    • (2012) Prostate , vol.72 , pp. 1006-1012
    • Jerome-Morais, A.1    Wright, M.E.2    Liu, R.3    Yang, W.4    Jackson, M.I.5    Combs, G.F.6    Diamond, A.M.7
  • 64
    • 0030020576 scopus 로고    scopus 로고
    • A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
    • Tamura, T.; Stadtman, T.C. A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity. Proc. Natl. Acad. Sci. USA 1996, 93, 1006–1011.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1006-1011
    • Tamura, T.1    Stadtman, T.C.2
  • 65
    • 61549097790 scopus 로고    scopus 로고
    • Holmgren, Selenoproteins
    • Lu, J.A. Holmgren, Selenoproteins. J. Biol. Chem. 2009, 284, 723–727.
    • (2009) J. Biol. Chem , vol.284 , pp. 723-727
    • Lu, J.A.1
  • 66
    • 0033582515 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver
    • Lee, S.R.; Kim, J.R.; Kwon, K.S.; Yoon, H.W.; Levine, R.L.; Ginsburg, A.; Rhee, S.G. Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. J. Biol. Chem. 1999, 274, 4722–4734.
    • (1999) J. Biol. Chem , vol.274 , pp. 4722-4734
    • Lee, S.R.1    Kim, J.R.2    Kwon, K.S.3    Yoon, H.W.4    Levine, R.L.5    Ginsburg, A.6    Rhee, S.G.7
  • 67
    • 0021810653 scopus 로고
    • Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats
    • Rozell, B.; Hansson, H.A.; Luthman, M.; Holmgren, A. Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats. Eur. J. Cell Biol. 1985, 38, 79–86.
    • (1985) Eur. J. Cell Biol , vol.38 , pp. 79-86
    • Rozell, B.1    Hansson, H.A.2    Luthman, M.3    Holmgren, A.4
  • 68
    • 22544451578 scopus 로고    scopus 로고
    • Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation
    • Su, D.; Novoselov, S.V.; Sun, Q.A.; Moustafa, M.E.; Zhou, Y.; Oko, R.; Hatfield, D.L.; Gladyshev, V.N. Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation. J. Biol. Chem. 2005, 280, 26491–26498.
    • (2005) J. Biol. Chem , vol.280 , pp. 26491-26498
    • Su, D.1    Novoselov, S.V.2    Sun, Q.A.3    Moustafa, M.E.4    Zhou, Y.5    Oko, R.6    Hatfield, D.L.7    Gladyshev, V.N.8
  • 69
    • 67349120863 scopus 로고    scopus 로고
    • Focus on mammalian thioredoxin reductases—Important selenoproteins with versatile functions
    • Arner, E.S. Focus on mammalian thioredoxin reductases—Important selenoproteins with versatile functions. Biochim. Biophys. Acta 2009, 1790, 495–526.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 495-526
    • Arner, E.S.1
  • 70
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D.; Powis, G. Thioredoxin reductase. Biochem. J. 2000, 15, 1–8.
    • (2000) Biochem. J , vol.15 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 71
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • Lu, J.; Holmgren, A. The thioredoxin antioxidant system. Free Radic. Biol. Med. 2014, 66, 75–87.
    • (2014) Free Radic. Biol. Med , vol.66 , pp. 75-87
    • Lu, J.1    Holmgren, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.