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Volumn 205, Issue 1, 2005, Pages 97-106

Effect of selenium-supplement on the calcium signaling in human endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CARBONYL CYANIDE 4 (TRIFLUOROMETHOXY)PHENYLHYDRAZONE; CYCLOSPORIN A; GLUTATHIONE PEROXIDASE; HISTAMINE; INOSITOL 1,4,5 TRISPHOSPHATE; PHOSPHOLIPASE C; SELENIUM; SELENOPROTEIN; THAPSIGARGIN; THIOREDOXIN REDUCTASE; TRACE ELEMENT;

EID: 24344446442     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.20378     Document Type: Article
Times cited : (27)

References (56)
  • 2
    • 0033567403 scopus 로고    scopus 로고
    • Thioredoxin reductase is the major selenoprotein expressed in human umbilical-vein endothelial cells and is regulated by protein kinase C
    • Anema SM, Walker SW, Howie AF, Arthur JR, Nicol F, Beckett GJ. 1999. Thioredoxin reductase is the major selenoprotein expressed in human umbilical-vein endothelial cells and is regulated by protein kinase C. Biochem J 342:111-117.
    • (1999) Biochem J , vol.342 , pp. 111-117
    • Anema, S.M.1    Walker, S.W.2    Howie, A.F.3    Arthur, J.R.4    Nicol, F.5    Beckett, G.J.6
  • 3
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér ES, Holmgren A. 2000. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267:6102-6109.
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arnér, E.S.1    Holmgren, A.2
  • 4
    • 0028344174 scopus 로고
    • A novel phospholipase C inhibitor and phorbol esters reveal selective regulation of thrombin- and parathyroid hormone-stimulated signaling pathways in rat osteosarcoma cells
    • Babich M, Alford GE, Nissenson RA. 1994. A novel phospholipase C inhibitor and phorbol esters reveal selective regulation of thrombin- and parathyroid hormone-stimulated signaling pathways in rat osteosarcoma cells. J Pharmacol Exp Ther 269:172-177.
    • (1994) J Pharmacol Exp Ther , vol.269 , pp. 172-177
    • Babich, M.1    Alford, G.E.2    Nissenson, R.A.3
  • 5
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore: A cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi P, Broekemeyer KM, Pfeiffer DR. 1994. Recent progress on regulation of the mitochondrial permeability transition pore: A cyclosporin-sensitive pore in the inner mitochondrial membrane. J Bioenerg Biomembr 26:509-517.
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeyer, K.M.2    Pfeiffer, D.R.3
  • 6
    • 0032531818 scopus 로고    scopus 로고
    • Calcium - A life and death signal
    • Berridge MJ, Bootman MD, Lipp P. 1998. Calcium - a life and death signal. Nature 395:645-658.
    • (1998) Nature , vol.395 , pp. 645-658
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 7
  • 8
    • 0025743489 scopus 로고
    • Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region
    • Berry MJ, Banu L, Chen YY, Mandel SJ, Kieffer JD, Harney JW, Larsen PR. 1991. Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region. Nature 353:273-276.
    • (1991) Nature , vol.353 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Chen, Y.Y.3    Mandel, S.J.4    Kieffer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 9
    • 0028152513 scopus 로고
    • Thioredoxin increases the proliferation of human B-cell lines through a protein kinase C-dependent mechanism
    • Biguet C, Wakasugi N, Mishal Z, Holmgren A, Chouaib S, Tursz T, Wakasugi H. 1994. Thioredoxin increases the proliferation of human B-cell lines through a protein kinase C-dependent mechanism. J Biol Chem 269:28865-28870.
    • (1994) J Biol Chem , vol.269 , pp. 28865-28870
    • Biguet, C.1    Wakasugi, N.2    Mishal, Z.3    Holmgren, A.4    Chouaib, S.5    Tursz, T.6    Wakasugi, H.7
  • 11
    • 0021360660 scopus 로고
    • Mechanism of selenium-glutathione peroxidase and its inhibition by mercaptocarboxylic acids and other mercaptans
    • Chaudiere J, Wilhelmsen EC, Tappel AL. 1984. Mechanism of selenium-glutathione peroxidase and its inhibition by mercaptocarboxylic acids and other mercaptans. J Biol Chem 259:1043-1050.
    • (1984) J Biol Chem , vol.259 , pp. 1043-1050
    • Chaudiere, J.1    Wilhelmsen, E.C.2    Tappel, A.L.3
  • 12
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. 1999. The mitochondrial permeability transition pore and its role in cell death. Biochem J 341:234-249.
    • (1999) Biochem J , vol.341 , pp. 234-249
    • Crompton, M.1
  • 13
    • 0023821864 scopus 로고    scopus 로고
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem J 255:357-360.
    • (1998) Biochem J , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 14
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton M, Virji S, Ward JM. 1998b. Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur J Biochem 258:729-735.
    • (1998) Eur J Biochem , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 15
    • 0037588974 scopus 로고    scopus 로고
    • 12 receptor by thiol reagents requires interaction with both extracellular cysteine residues. Cys17 and Cys270
    • 12 receptor by thiol reagents requires interaction with both extracellular cysteine residues. Cys17 and Cys270. Blood 101:3908-3914.
    • (2003) Blood , vol.101 , pp. 3908-3914
    • Ding, Z.1    Kim, S.2    Dorsam, R.T.3    Jin, J.4    Kunapuli, S.P.5
  • 16
    • 0026071055 scopus 로고
    • Inositol trisphosphate receptor: Phosphorylation by protein kinase C and calcium calmodulin-dependent protein kinases in reconstituted lipid vesicles
    • Ferris CD, Huganir RL, Bredt DS, Cameron AM, Snyder SH. 1991. Inositol trisphosphate receptor: Phosphorylation by protein kinase C and calcium calmodulin-dependent protein kinases in reconstituted lipid vesicles. Proc Natl Acad Sci 88:2232-2235.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 2232-2235
    • Ferris, C.D.1    Huganir, R.L.2    Bredt, D.S.3    Cameron, A.M.4    Snyder, S.H.5
  • 17
    • 0030731916 scopus 로고    scopus 로고
    • Mechanisms of the regulation of thioredoxin reductase activity in cancer cells by the chemopreventive agent selenium
    • Gallegos A, Berggren M, Gasdaska JR, Powis G. 1997. Mechanisms of the regulation of thioredoxin reductase activity in cancer cells by the chemopreventive agent selenium. Cancer Res 57:4965-4970.
    • (1997) Cancer Res , vol.57 , pp. 4965-4970
    • Gallegos, A.1    Berggren, M.2    Gasdaska, J.R.3    Powis, G.4
  • 18
    • 0032848137 scopus 로고    scopus 로고
    • Selenium metabolism, selenoproteins and mechanisms of cancer prevention: Complexities with thioredoxin reductase
    • Ganther HE. 1999. Selenium metabolism, selenoproteins and mechanisms of cancer prevention: Complexities with thioredoxin reductase. Carcinogenesis 20:1657-1666.
    • (1999) Carcinogenesis , vol.20 , pp. 1657-1666
    • Ganther, H.E.1
  • 19
    • 0034242495 scopus 로고    scopus 로고
    • Effect of signaling inhibitors on the release of lysozyme from human neutrophils activated by Sambucus nigra agglutinin
    • Gorudko IV, Timoshenko AV. 2000. Effect of signaling inhibitors on the release of lysozyme from human neutrophils activated by Sambucus nigra agglutinin. Biochemistry (Mosc) 65:940-945.
    • (2000) Biochemistry (Mosc) , vol.65 , pp. 940-945
    • Gorudko, I.V.1    Timoshenko, A.V.2
  • 20
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds
    • Gromer S, Arscott LD, Williams CHJ, Schirmer RH, Becker K. 1998. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem 273:20096-20101.
    • (1998) J Biol Chem , vol.273 , pp. 20096-20101
    • Gromer, S.1    Arscott, L.D.2    Williams, C.H.J.3    Schirmer, R.H.4    Becker, K.5
  • 21
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart
    • Halestrap AP, Kerr PM, Javadov S, Woodfield K. 1998. Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart. Biochim Biophys Acta 1366:79-94.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 79-94
    • Halestrap, A.P.1    Kerr, P.M.2    Javadov, S.3    Woodfield, K.4
  • 22
    • 0034600003 scopus 로고    scopus 로고
    • Effect of selenium supplementation on the activities of glutathione metabolizing enzymes in human hepatoma Hep G2 cell line
    • Helmy MH, Ismail SS, Fayed H, El-Bassiouni EA. 2000. Effect of selenium supplementation on the activities of glutathione metabolizing enzymes in human hepatoma Hep G2 cell line. Toxicology 144:57-61.
    • (2000) Toxicology , vol.144 , pp. 57-61
    • Helmy, M.H.1    Ismail, S.S.2    Fayed, H.3    El-Bassiouni, E.A.4
  • 23
    • 0031282148 scopus 로고    scopus 로고
    • Determination of thioredoxin reductase activity in rat liver supernatant
    • Hill KE, McCollum GW, Burk RF. 1997. Determination of thioredoxin reductase activity in rat liver supernatant. Anal Biochem 253:123-125.
    • (1997) Anal Biochem , vol.253 , pp. 123-125
    • Hill, K.E.1    McCollum, G.W.2    Burk, R.F.3
  • 26
    • 0032493935 scopus 로고    scopus 로고
    • 2+ homeostasis in the agonist-sensitive internal store: Functional interactions between mitochondria and the ER measured in situ in intact cells
    • 2+ homeostasis in the agonist-sensitive internal store: Functional interactions between mitochondria and the ER measured in situ in intact cells. J Cell Biol 142:1235-1243.
    • (1998) J Cell Biol , vol.142 , pp. 1235-1243
    • Landolfi, B.1    Curci, S.2    Debellis, L.3    Pozzan, T.4    Aldebaran, M.5    Hofer, A.M.6
  • 27
    • 0037121551 scopus 로고    scopus 로고
    • Selenium supplementation acting through the induction of thioredoxin reductase and glutathione peroxidase protects the human endothelial cell line EAhy926 from damage by lipid hydroperoxides
    • Lewin MH, Arthur JR, Riemersma RA, Nicol F, Walker SW, Millar EM, Howie AF, Beckett GJ. 2002. Selenium supplementation acting through the induction of thioredoxin reductase and glutathione peroxidase protects the human endothelial cell line EAhy926 from damage by lipid hydroperoxides. Biochim Biophys Acta 1593:85-92.
    • (2002) Biochim Biophys Acta , vol.1593 , pp. 85-92
    • Lewin, M.H.1    Arthur, J.R.2    Riemersma, R.A.3    Nicol, F.4    Walker, S.W.5    Millar, E.M.6    Howie, A.F.7    Beckett, G.J.8
  • 29
    • 0033613871 scopus 로고    scopus 로고
    • Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function
    • Makino Y, Yoshikawa N, Okamoto K, Hirota K, Yodoi J, Makino I, Tanaka H. 1999. Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J Biol Chem 274:3182-3188.
    • (1999) J Biol Chem , vol.274 , pp. 3182-3188
    • Makino, Y.1    Yoshikawa, N.2    Okamoto, K.3    Hirota, K.4    Yodoi, J.5    Makino, I.6    Tanaka, H.7
  • 30
    • 0030055822 scopus 로고    scopus 로고
    • Selenium-mediated inhibition of transcription factor NF-kappa B and HIV-1 LTR promoter activity
    • Makropoulos V, Bruning T, Schulze-Osthoff K. 1996. Selenium-mediated inhibition of transcription factor NF-kappa B and HIV-1 LTR promoter activity. Arch Toxicol 70:277-283.
    • (1996) Arch Toxicol , vol.70 , pp. 277-283
    • Makropoulos, V.1    Bruning, T.2    Schulze-Osthoff, K.3
  • 31
    • 0036092524 scopus 로고    scopus 로고
    • 2+ buffering regulates synaptic transmission between retinal amacrine cells
    • 2+ buffering regulates synaptic transmission between retinal amacrine cells. J Neurophysiol 87:1426-1439.
    • (2002) J Neurophysiol , vol.87 , pp. 1426-1439
    • Medler, K.1    Gleason, E.L.2
  • 34
    • 0033957283 scopus 로고    scopus 로고
    • Mitochondria buffer non-toxic calcium loads and release calcium through the mitochondrial permeability transition pore and sodium calcium exchanger in rat basal forebrain neurons
    • Murchison D, Griffith WH. 2000. Mitochondria buffer non-toxic calcium loads and release calcium through the mitochondrial permeability transition pore and sodium calcium exchanger in rat basal forebrain neurons. Brain Res 854:139-151.
    • (2000) Brain Res , vol.854 , pp. 139-151
    • Murchison, D.1    Griffith, W.H.2
  • 35
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J, Arner ESJ. 2001. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31:1287-1312.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.J.2
  • 36
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocytes glutathion peroxidase
    • Paglia ED, Valentine WN. 1979. Studies on the quantitative and qualitative characterization of erythrocytes glutathion peroxidase. J Lab Clin Med 70:158-169.
    • (1979) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, E.D.1    Valentine, W.N.2
  • 37
    • 0032530396 scopus 로고    scopus 로고
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum. EMBO J 17:5298-5308.
    • (1998) EMBO J , vol.17 , pp. 5298-5308
    • Pinton, P.1    Pozzan, T.2    Rizzuto, R.3
  • 38
    • 2142830974 scopus 로고    scopus 로고
    • Cell sensitivity assay: The MTT assay
    • Plumb JA. 2004. Cell sensitivity assay: The MTT assay. Methods Mol Med 88:165-169.
    • (2004) Methods Mol Med , vol.88 , pp. 165-169
    • Plumb, J.A.1
  • 40
    • 0034662094 scopus 로고    scopus 로고
    • The importance of selenium to human health
    • Rayman MP. 2000. The importance of selenium to human health. Lancet 356 :233-241.
    • (2000) Lancet , vol.356 , pp. 233-241
    • Rayman, M.P.1
  • 41
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isozymes
    • Rhee SG, Bae YS. 1997. Regulation of phosphoinositide-specific phospholipase C isozymes. J Biol Chem 272:15045-15048.
    • (1997) J Biol Chem , vol.272 , pp. 15045-15048
    • Rhee, S.G.1    Bae, Y.S.2
  • 43
    • 0034873185 scopus 로고    scopus 로고
    • Reactive oxygen species as intracellular messengers during cell growth and differentiation
    • Sauer H, Wartenberg M, Hescheler J. 2001. Reactive oxygen species as intracellular messengers during cell growth and differentiation. Cell Physiol Biochem 11:173-186.
    • (2001) Cell Physiol Biochem , vol.11 , pp. 173-186
    • Sauer, H.1    Wartenberg, M.2    Hescheler, J.3
  • 44
    • 0032955803 scopus 로고    scopus 로고
    • Activation pattern of mitogen-activated protein kinases elicited by peroxynitrite: Attenuation by selenite supplementation
    • Schieke SM, Brivita K, Klotz LO, Sies H. 1999. Activation pattern of mitogen-activated protein kinases elicited by peroxynitrite: Attenuation by selenite supplementation. FEBS Lett 448:301-303.
    • (1999) FEBS Lett , vol.448 , pp. 301-303
    • Schieke, S.M.1    Brivita, K.2    Klotz, L.O.3    Sies, H.4
  • 45
    • 0033992162 scopus 로고    scopus 로고
    • Phosphatidylinositol 3′-kinase-mediated calcium mobilization regulates chemotaxis in phosphatidic acid-stimulated human neutrophils
    • Siddiqui RA, English D. 2000. Phosphatidylinositol 3′-kinase- mediated calcium mobilization regulates chemotaxis in phosphatidic acid-stimulated human neutrophils. Biochim Biophys Acta 1483:161-173.
    • (2000) Biochim Biophys Acta , vol.1483 , pp. 161-173
    • Siddiqui, R.A.1    English, D.2
  • 49
    • 0344142391 scopus 로고    scopus 로고
    • Selenium compounds have disparate abilities to impose oxidative stress and induce apoptosis
    • Stewart MS, Spallholz JE, Neldner KH, Pence BC. 1999. Selenium compounds have disparate abilities to impose oxidative stress and induce apoptosis. Free Radic Biol Med 26:42-48.
    • (1999) Free Radic Biol Med , vol.26 , pp. 42-48
    • Stewart, M.S.1    Spallholz, J.E.2    Neldner, K.H.3    Pence, B.C.4
  • 52
    • 0034653369 scopus 로고    scopus 로고
    • Reactive oxygen species and proinflammatory cytokine signaling in endothelial cells: Effect of selenium supplementation
    • Tolando R, Jovanovic A, Brigelius-Flohe E, Ursini F, Maiorino M. 2000. Reactive oxygen species and proinflammatory cytokine signaling in endothelial cells: Effect of selenium supplementation. Free Radic Biol Med 28:979-986.
    • (2000) Free Radic Biol Med , vol.28 , pp. 979-986
    • Tolando, R.1    Jovanovic, A.2    Brigelius-Flohe, E.3    Ursini, F.4    Maiorino, M.5
  • 53
    • 0037930840 scopus 로고    scopus 로고
    • Critical regions for activation gating of the inositol 1,4,5-trisphosphate receptor
    • Uchida K, Miyauchi H, Furuichi T, Michikawa T, Mikoshiba K. 2003. Critical regions for activation gating of the inositol 1,4,5-trisphosphate receptor. J Biol Chem 278:16551-16560.
    • (2003) J Biol Chem , vol.278 , pp. 16551-16560
    • Uchida, K.1    Miyauchi, H.2    Furuichi, T.3    Michikawa, T.4    Mikoshiba, K.5
  • 54
    • 0035815727 scopus 로고    scopus 로고
    • The Golgi PMR1 P-type ATPase of caenorhabditis elegans: Identification of the gene and demonstration of calcium and manganese transport
    • Van Baelen K, Vanoevelen J, Missiaen L, Raeymaekers L, Wuytack F. 2001. The Golgi PMR1 P-type ATPase of caenorhabditis elegans: Identification of the gene and demonstration of calcium and manganese transport. J Biol Chem 276: 10683-10691.
    • (2001) J Biol Chem , vol.276 , pp. 10683-10691
    • Van Baelen, K.1    Vanoevelen, J.2    Missiaen, L.3    Raeymaekers, L.4    Wuytack, F.5
  • 55
    • 0032401864 scopus 로고    scopus 로고
    • Evaluation of methods for the quantitation of cysteines in proteins
    • Wright SK, Viola RE. 1998. Evaluation of methods for the quantitation of cysteines in proteins. Anal Biochem 265:8-14.
    • (1998) Anal Biochem , vol.265 , pp. 8-14
    • Wright, S.K.1    Viola, R.E.2


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