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Volumn 288, Issue 3, 2013, Pages 1706-1716

Protein-disulfide isomerase regulates the thyroid hormone receptor-mediated gene expression via redox factor-1 through thiol reduction-oxidation

Author keywords

[No Author keywords available]

Indexed keywords

DITHIOLS; GROWTH HORMONES; OVER-EXPRESSION; OXIDOREDUCTASES; PROTEIN DISULFIDE ISOMERASES; REDOX ACTIVITY; REDOX REGULATION; REDOX STATE; REDUCTION-OXIDATION; THYROID HORMONE RECEPTOR; THYROID HORMONES; WILD TYPES;

EID: 84872740339     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.365239     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 77952584245 scopus 로고    scopus 로고
    • A role for protein disulfide isomerase in the early folding and assembly of MHC class i molecules
    • Kang, K., Park, B., Oh, C., Cho, K., and Ahn, K. (2009) A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules. Antioxid. Redox Signal. 11, 2553-2561
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2553-2561
    • Kang, K.1    Park, B.2    Oh, C.3    Cho, K.4    Ahn, K.5
  • 2
    • 0037474328 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion
    • DOI 10.1074/jbc.M205467200
    • Barbouche, R., Miquelis, R., Jones, I. M., and Fenouillet, E. (2003) Proteindisulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion. J. Biol. Chem. 278, 3131-3136 (Pubitemid 36801223)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 3131-3136
    • Barbouche, R.1    Miquelis, R.2    Jones, I.M.3    Fenouillet, E.4
  • 3
    • 34447502257 scopus 로고    scopus 로고
    • Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus
    • DOI 10.1089/ars.2007.1639
    • Fenouillet, E., Barbouche, R., and Jones, I. M. (2007) Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus. Antioxid. Redox Signal. 9, 1009-1034 (Pubitemid 47080818)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.8 , pp. 1009-1034
    • Fenouillet, E.1    Barbouche, R.2    Jones, I.M.3
  • 5
    • 34548494139 scopus 로고    scopus 로고
    • Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity
    • DOI 10.1074/jbc.M702410200
    • Versteeg, H. H., and Ruf, W. (2007) Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity. J. Biol. Chem. 282, 25416-25424 (Pubitemid 47372801)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25416-25424
    • Versteeg, H.H.1    Ruf, W.2
  • 6
    • 48449100433 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a trigger for tissue factor-dependent fibrin generation
    • Manukyan, D., von Bruehl, M. L., Massberg, S., and Engelmann, B. (2008) Protein disulfide isomerase as a trigger for tissue factor-dependent fibrin generation. Thromb. Res. 122, Suppl. 1, S19-S22
    • (2008) Thromb. Res. , vol.122 , Issue.SUPPL. 1
    • Manukyan, D.1    Von Bruehl, M.L.2    Massberg, S.3    Engelmann, B.4
  • 7
    • 0031048978 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line
    • Orlandi, P. A. (1997) Protein-disulfide isomerase-mediated reduction of the a subunit of cholera toxin in a human intestinal cell line. J. Biol. Chem. 272, 4591-4599 (Pubitemid 27078541)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 4591-4599
    • Orlandi, P.A.1
  • 8
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • DOI 10.1016/S0092-8674(01)00289-6
    • Tsai, B., Rodighiero, C., Lencer, W. I., and Rapoport, T. A. (2001) Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104, 937-948 (Pubitemid 32289285)
    • (2001) Cell , vol.104 , Issue.6 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 11
    • 34047258016 scopus 로고    scopus 로고
    • 1 2,3-epoxide reduction
    • DOI 10.1074/jbc.M608954200
    • Wajih, N., Hutson, S. M., and Wallin, R. (2007) Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction. J. Biol. Chem. 282, 2626-2635 (Pubitemid 47076752)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.4 , pp. 2626-2635
    • Wajih, N.1    Hutson, S.M.2    Wallin, R.3
  • 12
    • 77957007036 scopus 로고    scopus 로고
    • Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners
    • Schulman, S., Wang, B., Li, W., and Rapoport, T. A. (2010) Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners. Proc. Natl. Acad. Sci. U.S.A. 107, 15027-15032
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15027-15032
    • Schulman, S.1    Wang, B.2    Li, W.3    Rapoport, T.A.4
  • 15
    • 0032481380 scopus 로고    scopus 로고
    • The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • DOI 10.1093/emboj/17.4.927
    • Klappa, P., Ruddock, L. W., Darby, N. J., and Freedman, R. B. (1998) The bα domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J. 17, 927-935 (Pubitemid 28077647)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 16
    • 0023865390 scopus 로고
    • Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the β-subunit of prolyl-4-hydroxylase
    • Obata, T., Kitagawa, S., Gong, Q. H., Pastan, I., and Cheng, S. Y. (1988) Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the α-subunit of prolyl-4-hydroxylase. J. Biol. Chem. 263, 782-785 (Pubitemid 18044704)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.2 , pp. 782-785
    • Obata, T.1    Kitagawa, S.2    Gong, Q.-H.3    Pastan, I.4    Cheng, S.-Y.5
  • 18
    • 0035808319 scopus 로고    scopus 로고
    • Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum
    • DOI 10.1074/jbc.M007670200
    • Primm, T. P., and Gilbert, H. F. (2001) Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum. J. Biol. Chem. 276, 281-286 (Pubitemid 32050318)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 281-286
    • Primm, T.P.1    Gilbert, H.F.2
  • 19
    • 0035868331 scopus 로고    scopus 로고
    • The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands
    • DOI 10.1042/0264-6021:3540553
    • Klappa, P., Freedman, R. B., Langenbuch, M., Lan, M. S., Robinson, G. K., and Ruddock, L. W. (2001) The pancreas-specific protein disulphideisomerase PDIp interacts with a hydroxyaryl group in ligands. Biochem. J. 354, 553-559 (Pubitemid 32269718)
    • (2001) Biochemical Journal , vol.354 , Issue.3 , pp. 553-559
    • Klappa, P.1    Freedman, R.B.2    Langenbuch, M.3    Lan, M.S.4    Robinson, G.K.5    Ruddock, L.W.6
  • 20
    • 67349236074 scopus 로고    scopus 로고
    • Human pancreas-specific protein disulfide isomerase homolog (PDIp) is an intracellular estrogen-binding protein that modulates estrogen levels and actions in target cells
    • Fu, X. M., and Zhu, B. T. (2009) Human pancreas-specific protein disulfide isomerase homolog (PDIp) is an intracellular estrogen-binding protein that modulates estrogen levels and actions in target cells. J. Steroid Biochem. Mol. Biol. 115, 20-29
    • (2009) J. Steroid Biochem. Mol. Biol. , vol.115 , pp. 20-29
    • Fu, X.M.1    Zhu, B.T.2
  • 21
    • 33646342053 scopus 로고    scopus 로고
    • Inhibitory effects of environmental chemicals on protein bisulfide isomerase in vitro
    • Okada, K., Hiroi, T., Imaoka, S., and Funae, Y. (2005) Inhibitory effects of environmental chemicals on protein disulfide isomerase in vitro. Osaka City Med. J. 51, 51-63 (Pubitemid 44330596)
    • (2005) Osaka City Medical Journal , vol.51 , Issue.2 , pp. 51-63
    • Okada, K.1    Hiroi, T.2    Imaoka, S.3    Funae, Y.4
  • 22
    • 55949099615 scopus 로고    scopus 로고
    • Interaction between bisphenol derivatives and protein disulphide isomerase (PDI) and inhibition of PDI functions: Requirement of chemical structure for binding to PDI
    • Hashimoto, S., Okada, K., and Imaoka, S. (2008) Interaction between bisphenol derivatives and protein disulphide isomerase (PDI) and inhibition of PDI functions: requirement of chemical structure for binding to PDI. J. Biochem. 144, 335-342
    • (2008) J. Biochem. , vol.144 , pp. 335-342
    • Hashimoto, S.1    Okada, K.2    Imaoka, S.3
  • 23
    • 84855253249 scopus 로고    scopus 로고
    • The binding site of bisphenol A to protein disulfide isomerase (PDI)
    • Hashimoto, S., Shiomoto, K., Okada, K., and Imaoka, S. (2012) The binding site of bisphenol A to protein disulfide isomerase (PDI). J. Biochem. 151, 35-45
    • (2012) J. Biochem. , vol.151 , pp. 35-45
    • Hashimoto, S.1    Shiomoto, K.2    Okada, K.3    Imaoka, S.4
  • 24
    • 0030039013 scopus 로고    scopus 로고
    • An in vitro test system for thyroid hormone action
    • DOI 10.1006/abio.1996.0049
    • Hohenwarter, O., Waltenberger, A., and Katinger, H. (1996) An in vitro test system for thyroid hormone action. Anal. Biochem. 234, 56-59 (Pubitemid 26045752)
    • (1996) Analytical Biochemistry , vol.234 , Issue.1 , pp. 56-59
    • Hohenwarter, O.1    Waltenberger, A.2    Katinger, H.3
  • 26
    • 36549002171 scopus 로고    scopus 로고
    • 3
    • DOI 10.1016/j.mce.2007.08.005, PII S0303720707003115
    • Okada, K., Imaoka, S., Hashimoto, S., Hiroi, T., and Funae, Y. (2007) Overexpression of protein disulfide isomerase reduces the release of growth hormone induced by bisphenol A and/or T3. Mol. Cell. Endocrinol. 278, 44-51 (Pubitemid 350183942)
    • (2007) Molecular and Cellular Endocrinology , vol.278 , Issue.1-2 , pp. 44-51
    • Okada, K.1    Imaoka, S.2    Hashimoto, S.3    Hiroi, T.4    Funae, Y.5
  • 27
    • 33646798398 scopus 로고    scopus 로고
    • Bisphenol A binds to protein disulfide isomerase and inhibits its enzymatic and hormone-binding activities
    • DOI 10.1210/en.2005-1235
    • Hiroi, T., Okada, K., Imaoka, S., Osada, M., and Funae, Y. (2006) Bisphenol A binds to protein disulfide isomerase and inhibits its enzymatic and hormone-binding activities. Endocrinology 147, 2773-2780 (Pubitemid 43764614)
    • (2006) Endocrinology , vol.147 , Issue.6 , pp. 2773-2780
    • Hiroi, T.1    Okada, K.2    Imaoka, S.3    Osada, M.4    Funae, Y.5
  • 28
    • 84858651741 scopus 로고    scopus 로고
    • Effects of polybrominated diphenyl ethers (PBDEs) and their derivatives on protein disulfide isomerase activity and growth hormone release of GH3 cells
    • Hashimoto, S., Yoshimura, H., Okada, K., Uramaru, N., Sugihara, K., Kitamura, S., and Imaoka, S. (2012) Effects of polybrominated diphenyl ethers (PBDEs) and their derivatives on protein disulfide isomerase activity and growth hormone release of GH3 cells. Chem. Res. Toxicol. 25, 656-663
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 656-663
    • Hashimoto, S.1    Yoshimura, H.2    Okada, K.3    Uramaru, N.4    Sugihara, K.5    Kitamura, S.6    Imaoka, S.7
  • 29
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1α in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • Ema, M., Hirota, K., Mimura, J., Abe, H., Yodoi, J., Sogawa, K., Poellinger, L., and Fujii-Kuriyama, Y. (1999) Molecular mechanisms of transcription activation by HLF and HIF1α in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J. 18, 1905-1914 (Pubitemid 29158534)
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 30
    • 6944236323 scopus 로고    scopus 로고
    • Ref-1/Ape is critical for formation of the hypoxia-inducible transcriptional complex on the hypoxic response element of the rat pulmonary artery endothelial cell VEGF gene
    • DOI 10.1096/fj.03-1160fje
    • Ziel, K. A., Campbell, C. C., Wilson, G. L., and Gillespie, M. N. (2004) Ref-1/Ape is critical for formation of the hypoxia-inducible transcriptional complex on the hypoxic response element of the rat pulmonary artery endothelial cell VEGF gene. FASEB J. 18, 986-988 (Pubitemid 39561500)
    • (2004) FASEB Journal , vol.18 , Issue.9 , pp. 986-988
    • Ziel, K.A.1    Campbell, C.C.2    Wilson, G.L.3    Gillespie, M.N.4
  • 31
    • 0030585150 scopus 로고    scopus 로고
    • The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal
    • Qin, J., Clore, G. M., Kennedy, W. P., Kuszewski, J., and Gronenborn, A. M. (1996) The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure 4, 613-620 (Pubitemid 126657553)
    • (1996) Structure , vol.4 , Issue.5 , pp. 613-620
    • Qin, J.1    Clore, G.M.2    Kennedy, W.P.3    Kuszewski, J.4    Gronenborn, A.M.5
  • 33
    • 33748329644 scopus 로고    scopus 로고
    • Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors
    • DOI 10.1016/j.freeradbiomed.2006.06.016, PII S0891584906004199
    • Grillo, C., D'Ambrosio, C., Scaloni, A., Maceroni, M., Merluzzi, S., Turano, C., and Altieri, F. (2006) Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors. Free Radic. Biol. Med. 41, 1113-1123 (Pubitemid 44331573)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.7 , pp. 1113-1123
    • Grillo, C.1    D'Ambrosio, C.2    Scaloni, A.3    Maceroni, M.4    Merluzzi, S.5    Turano, C.6    Altieri, F.7
  • 36
    • 0033991530 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor 1: Mechanisms and consequences
    • Semenza, G. L. (2000) Expression of hypoxia-inducible factor 1: mechanisms and consequences. Biochem. Pharmacol. 59, 47-53
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 47-53
    • Semenza, G.L.1
  • 37
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease a by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles, M. M., and Gilbert, H. F. (1991) Catalysis of the oxidative folding of ribonuclease a by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30, 613-619
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 38
    • 69449094081 scopus 로고    scopus 로고
    • Apurinic/apyrimidinic endonuclease 1 alters estrogen receptor activity and estrogen-responsive gene expression
    • Curtis, C. D., Thorngren, D. L., Ziegler, Y. S., Sarkeshik, A., Yates, J. R., and Nardulli, A. M. (2009) Apurinic/apyrimidinic endonuclease 1 alters estrogen receptor activity and estrogen-responsive gene expression. Mol. Endocrinol. 23, 1346-1359
    • (2009) Mol. Endocrinol. , vol.23 , pp. 1346-1359
    • Curtis, C.D.1    Thorngren, D.L.2    Ziegler, Y.S.3    Sarkeshik, A.4    Yates, J.R.5    Nardulli, A.M.6
  • 39
    • 0037177840 scopus 로고    scopus 로고
    • Redox effector factor-1 regulates the activity of thyroid transcription factor 1 by controlling the redox state of the N transcriptional activation domain
    • DOI 10.1074/jbc.M200582200
    • Tell, G., Pines, A., Paron, I., D'Elia, A., Bisca, A., Kelley, M. R., Manzini, G., and Damante, G. (2002) Redox effector factor-1 regulates the activity of thyroid transcription factor 1 by controlling the redox state of the N transcriptional activation domain. J. Biol. Chem. 277, 14564-14574 (Pubitemid 34952523)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14564-14574
    • Tell, G.1    Pines, A.2    Paron, I.3    D'Elia, A.4    Bisca, A.5    Kelley, M.R.6    Manzini, G.7    Damante, G.8
  • 41
    • 48349107170 scopus 로고    scopus 로고
    • A new APE1/Ref-1-dependent pathway leading to reduction of NF-αB and AP-1, and activation of their DNA-binding activity
    • Ando, K., Hirao, S., Kabe, Y., Ogura, Y., Sato, I., Yamaguchi, Y., Wada, T., and Handa, H. (2008) A new APE1/Ref-1-dependent pathway leading to reduction of NF-αB and AP-1, and activation of their DNA-binding activity. Nucleic Acids Res. 36, 4327-4336
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4327-4336
    • Ando, K.1    Hirao, S.2    Kabe, Y.3    Ogura, Y.4    Sato, I.5    Yamaguchi, Y.6    Wada, T.7    Handa, H.8
  • 42
    • 0018196480 scopus 로고
    • Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay
    • Holmgren, A., and Luthman, M. (1978) Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay. Biochemistry 17, 4071-4077 (Pubitemid 9036527)
    • (1978) Biochemistry , vol.17 , Issue.19 , pp. 4071-4077
    • Holmgren, A.1    Luthman, M.2


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