메뉴 건너뛰기




Volumn 7, Issue 6, 2008, Pages 313-324

S-glutathionylation: Indicator of cell stress and regulator of the unfolded protein response

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; APOPTOSIS SIGNAL REGULATING KINASE 1; C EBP HOMOLOGOUS PROTEIN; CISPLATIN; CYSTEINE PROTEINASE; DOXORUBICIN; FREE RADICAL; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE TRANSFERASE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; NOV 002; PANCREATIC ENDOPLASMIC RETICULUM KINASE; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN DISULFIDE ISOMERASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UNCLASSIFIED DRUG;

EID: 38349049487     PISSN: 15340384     EISSN: 15432548     Source Type: Journal    
DOI: 10.1124/mi.7.6.7     Document Type: Review
Times cited : (186)

References (94)
  • 1
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant DEFENSE
    • Beer, S.M., Taylor, E.R., Brown, S.E., Dahm, C.C., Costa, N.J., Runswick, M.J., and Murphy, M.P. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant DEFENSE. J. Biol. Chem. 279, 47939-47951 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 2
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton, M.D., Chock, P.B., and Mieyal, J.J. Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid. Redox. Signal. 7, 348-366 (2005).
    • (2005) Antioxid. Redox. Signal , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 4
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew, K.D. Glutathione-associated enzymes in anticancer drug resistance. Cancer Res. 54, 4313-4320 (1994).
    • (1994) Cancer Res , vol.54 , pp. 4313-4320
    • Tew, K.D.1
  • 5
    • 0033105414 scopus 로고    scopus 로고
    • Regulation of JNK signaling by GSTp
    • Adler, V., Yin, Z., Fuchs, S.Y. et al. Regulation of JNK signaling by GSTp. EMBO J. 18, 1321-1334 (1999).
    • (1999) EMBO J , vol.18 , pp. 1321-1334
    • Adler, V.1    Yin, Z.2    Fuchs, S.Y.3
  • 6
    • 0035877779 scopus 로고    scopus 로고
    • Wang, T., Arifoglu, P., Ronai, Z., and Tew, K.D. Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus. J. Biol. Chem. 276, 20999-21003 (2001). This work, along with reference (5), establishes that pi GST is more than a Phase II detoxification enzyme. The non-catalytic properties of pi GST encompass kinase regulation and mediation of S-glutathionylation reactions. As such, GST is a regulator of multiple signaling pathways that govern survival and apoptotic pathways.
    • Wang, T., Arifoglu, P., Ronai, Z., and Tew, K.D. Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus. J. Biol. Chem. 276, 20999-21003 (2001). This work, along with reference (5), establishes that pi GST is more than a Phase II detoxification enzyme. The non-catalytic properties of pi GST encompass kinase regulation and mediation of S-glutathionylation reactions. As such, GST is a regulator of multiple signaling pathways that govern survival and apoptotic pathways.
  • 7
    • 0033896832 scopus 로고    scopus 로고
    • Glutathione S-transferase p elicits protection against H2O2-induced cell death via coordinated regulation of stress kinases
    • Yin, Z., Ivanov, V.N., Habelha, H., Tew, K., and Ronai, Z. Glutathione S-transferase p elicits protection against H2O2-induced cell death via coordinated regulation of stress kinases. Cancer Res. 60, 4053-4057 (2000).
    • (2000) Cancer Res , vol.60 , pp. 4053-4057
    • Yin, Z.1    Ivanov, V.N.2    Habelha, H.3    Tew, K.4    Ronai, Z.5
  • 8
    • 4344686072 scopus 로고    scopus 로고
    • Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain
    • Cross, J.V. and Templeton, D.J. Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain. Biochem J. 381, 675-683 (2004).
    • (2004) Biochem J , vol.381 , pp. 675-683
    • Cross, J.V.1    Templeton, D.J.2
  • 9
    • 0036371627 scopus 로고    scopus 로고
    • c-Jun regulation by S-glutathionylation
    • Klatt, P. and Lamas, S. c-Jun regulation by S-glutathionylation. Methods Enzymol. 348, 157-174 (2002).
    • (2002) Methods Enzymol , vol.348 , pp. 157-174
    • Klatt, P.1    Lamas, S.2
  • 11
    • 33751115477 scopus 로고    scopus 로고
    • Human GSTA1-1 reduces c-Jun N-terminal kinase signaling and apoptosis in Caco-2 cells
    • Romero, L., Andrews, K., Ng, L., O'Rourke, K., Maslen, A., and Kirby, G. Human GSTA1-1 reduces c-Jun N-terminal kinase signaling and apoptosis in Caco-2 cells. Biochem. J. 400, 135-141 (2006).
    • (2006) Biochem. J , vol.400 , pp. 135-141
    • Romero, L.1    Andrews, K.2    Ng, L.3    O'Rourke, K.4    Maslen, A.5    Kirby, G.6
  • 12
    • 1642326559 scopus 로고    scopus 로고
    • Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST
    • Manevich, Y., Feinstein, S.I., and Fisher, A.B. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc. Natl. Acad. Sci. USA 101, 3780-3785 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3780-3785
    • Manevich, Y.1    Feinstein, S.I.2    Fisher, A.B.3
  • 13
    • 30744437425 scopus 로고    scopus 로고
    • Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes
    • Ralat, L.A., Manevich, Y., Fisher, A.B., and Colman, R.F. Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Biochemistry 45, 360-372 (2006).
    • (2006) Biochemistry , vol.45 , pp. 360-372
    • Ralat, L.A.1    Manevich, Y.2    Fisher, A.B.3    Colman, R.F.4
  • 14
    • 33746878405 scopus 로고    scopus 로고
    • Prx1 suppresses radiation-induced c-Jun NH2-terminal kinase signaling in lung cancer cells through interaction with the glutathione S-transferase Pi/c-Jun NH2-terminal kinase complex
    • Kim, Y.J., Lee, W.S., Ip, C., Chae, H.Z., Park, E.M., and Park, Y.M. Prx1 suppresses radiation-induced c-Jun NH2-terminal kinase signaling in lung cancer cells through interaction with the glutathione S-transferase Pi/c-Jun NH2-terminal kinase complex. Cancer Res. 66, 7136-7142 (2006).
    • (2006) Cancer Res , vol.66 , pp. 7136-7142
    • Kim, Y.J.1    Lee, W.S.2    Ip, C.3    Chae, H.Z.4    Park, E.M.5    Park, Y.M.6
  • 15
    • 33748919803 scopus 로고    scopus 로고
    • Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals
    • Wu, Y., Fan, Y., Xue, B., Luo, L., Shen, J., Zhang, S., Jiang, Y., and Yin, Z. Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals. Oncogene 25, 5787-5800 (2006).
    • (2006) Oncogene , vol.25 , pp. 5787-5800
    • Wu, Y.1    Fan, Y.2    Xue, B.3    Luo, L.4    Shen, J.5    Zhang, S.6    Jiang, Y.7    Yin, Z.8
  • 16
    • 38349003562 scopus 로고    scopus 로고
    • Unpublished results
    • Townsend, D.M. (Unpublished results.)
    • Townsend, D.M.1
  • 17
    • 33747362096 scopus 로고    scopus 로고
    • Redox regulation of beta-actin during integrin-mediated cell adhesion
    • Fiaschi, T., Cozzi, G., Raugei, G., Formigli, L., Ramponi, G., and Chiarugi, P. Redox regulation of beta-actin during integrin-mediated cell adhesion. J. Biol. Chem. 281, 22983-22991 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 22983-22991
    • Fiaschi, T.1    Cozzi, G.2    Raugei, G.3    Formigli, L.4    Ramponi, G.5    Chiarugi, P.6
  • 18
    • 33645456962 scopus 로고    scopus 로고
    • Decline of contractility during ischemia-reperfusion injury: Actin glutathionylation and its effect on allosteric interaction with tropomyosin
    • Chen, F.C. and Ogut, O. Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin. Am. J. Physiol. Cell Physiol. 290, C719-727 (2006).
    • (2006) Am. J. Physiol. Cell Physiol , vol.290
    • Chen, F.C.1    Ogut, O.2
  • 19
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 (2002).
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 20
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu, B.P. and Weissman, J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164, 341-346 (2004).
    • (2004) J. Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 21
    • 28844470269 scopus 로고    scopus 로고
    • Feldman, D.E., Chauhan, V. and Koong, A.C. The unfolded protein response: A novel component of the hypoxic stress response in tumors. Mol. Cancer Res. 3, 597-605 (2005). ER stress is a molecular signature of tumor hypoxia. Proteins critical to UPR-induced apoptosis are novel targets for chemotherapeutic strategies.
    • Feldman, D.E., Chauhan, V. and Koong, A.C. The unfolded protein response: A novel component of the hypoxic stress response in tumors. Mol. Cancer Res. 3, 597-605 (2005). ER stress is a molecular signature of tumor hypoxia. Proteins critical to UPR-induced apoptosis are novel targets for chemotherapeutic strategies.
  • 22
    • 0038293080 scopus 로고    scopus 로고
    • Prognostic significance of tumor oxygenation in humans
    • Evans, S.M. and Koch, C.J. Prognostic significance of tumor oxygenation in humans. Cancer Lett. 195, 1-16 (2003).
    • (2003) Cancer Lett , vol.195 , pp. 1-16
    • Evans, S.M.1    Koch, C.J.2
  • 23
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer, J.W. and Diehl, J.A. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc. Natl. Acad. Sci. USA 97, 12625-12630 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 24
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao, R.V. and Bredesen, D.E. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr. Opin. Cell Biol. 16, 653-662 (2004).
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 25
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase
    • Wang, X.Z. and Ron, D. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase. Science 272, 1347-1349 (1996).
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 26
    • 33646237823 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha
    • Hetz, C., Bernasconi, P., Fisher, J. et al. Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha. Science 312, 572-576 (2006).
    • (2006) Science , vol.312 , pp. 572-576
    • Hetz, C.1    Bernasconi, P.2    Fisher, J.3
  • 29
    • 0023303619 scopus 로고
    • Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllylä, R., Huhtala, M.L., Koivu, J., and Kivirikko, K.I. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6, 643-6649 (1987).
    • (1987) EMBO J , vol.6 , pp. 643-6649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllylä, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 30
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari, D.M. and Soling, H.D. The protein disulphide-isomerase family: Unravelling a string of folds. Biochem. J. 339, 1-10 (1999).
    • (1999) Biochem. J , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.D.2
  • 31
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • Tian, G., Xiang, S., Noiva, R., Lennarz, W.J., and Schindelin, H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124, 61-73 (2006).
    • (2006) Cell , vol.124 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 32
    • 0018814871 scopus 로고
    • Simultaneous characterizations of 3-prolylhydroxylase and 4-prolylhydroxylase activities by ion exchange chromatography
    • Farjanel, J., Perier, C., Szymanovicz, G., and Frey, J. Simultaneous characterizations of 3-prolylhydroxylase and 4-prolylhydroxylase activities by ion exchange chromatography. Biochimie 62, 195-199 (1980).
    • (1980) Biochimie , vol.62 , pp. 195-199
    • Farjanel, J.1    Perier, C.2    Szymanovicz, G.3    Frey, J.4
  • 33
    • 0035815678 scopus 로고    scopus 로고
    • Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57
    • Pirneskoski, A., Ruddock, L.W., Klappa, P., Freedman, R.B., Kivirikko, K.I., and Koivunen, P. Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57. J. Biol. Chem. 276, 11287-11293 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 11287-11293
    • Pirneskoski, A.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4    Kivirikko, K.I.5    Koivunen, P.6
  • 34
    • 0028036401 scopus 로고
    • The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins
    • Landel, C.C., Kushner, P.J. and Greene, G.L. The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins. Mol. Endocrinol. 8, 1407-1419 (1994).
    • (1994) Mol. Endocrinol , vol.8 , pp. 1407-1419
    • Landel, C.C.1    Kushner, P.J.2    Greene, G.L.3
  • 35
    • 33747838884 scopus 로고    scopus 로고
    • Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function
    • Schultz-Norton, J.R., McDonald, W.H., Yates, J.R., and Nardulli A.M. Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function. Mol. Endocrinol. 20, 1982-1995 (2006).
    • (2006) Mol. Endocrinol , vol.20 , pp. 1982-1995
    • Schultz-Norton, J.R.1    McDonald, W.H.2    Yates, J.R.3    Nardulli, A.M.4
  • 36
    • 33745315287 scopus 로고    scopus 로고
    • Uehara, T., Nakamura, T., Yao, D., Shi, Z.Q., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., and Lipton, S.A. S-nitrosylated protein disulphide isomerase links protein misfolding to neurodegeneration. Nature 441, 513-517 (2006). Nitrosylation of PDI in the brains of patients with Parkinson's and Alzheimer's disease underscores the importance of this protein to normal cellular function.
    • Uehara, T., Nakamura, T., Yao, D., Shi, Z.Q., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., and Lipton, S.A. S-nitrosylated protein disulphide isomerase links protein misfolding to neurodegeneration. Nature 441, 513-517 (2006). Nitrosylation of PDI in the brains of patients with Parkinson's and Alzheimer's disease underscores the importance of this protein to normal cellular function.
  • 37
    • 31044436627 scopus 로고    scopus 로고
    • Townsend, D.M., Findlay, V.J., Fazilev. F., Ogle. M., Fraser. J., Saavedra, J.E., Ji, X., Keefer, L.K., and Tew, K.D. A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins. Mol. Pharmacol. 69, 501-508 (2006). Exploitation of PDI through drug-induced S-glutathionylation is a unique strategy to target cancer cells.
    • Townsend, D.M., Findlay, V.J., Fazilev. F., Ogle. M., Fraser. J., Saavedra, J.E., Ji, X., Keefer, L.K., and Tew, K.D. A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins. Mol. Pharmacol. 69, 501-508 (2006). Exploitation of PDI through drug-induced S-glutathionylation is a unique strategy to target cancer cells.
  • 38
    • 24944483028 scopus 로고    scopus 로고
    • Proteomic analysis on multi-drug resistant cells HL-60/DOX of acute myeloblastic leukemia
    • Chen, C.Y., Jia, J.H., Zhang, M.X., Meng, Y.S., Kong, D.X., Pan, X.L., and Yu, XP. Proteomic analysis on multi-drug resistant cells HL-60/DOX of acute myeloblastic leukemia. Chin. J. Physiol. 48,. 115-120 (2005).
    • (2005) Chin. J. Physiol , vol.48 , pp. 115-120
    • Chen, C.Y.1    Jia, J.H.2    Zhang, M.X.3    Meng, Y.S.4    Kong, D.X.5    Pan, X.L.6    Yu, X.P.7
  • 39
    • 23744499653 scopus 로고    scopus 로고
    • Diversity of the protein disulfide isomerase family: Identification of breast tumor induced Hag2 and Hag3 as novel members of the protein family
    • Persson, S., Rosenquist, M., Knoblach, B., Khosravi-Far, R., Sommarin, M., and Michalak, M. Diversity of the protein disulfide isomerase family: identification of breast tumor induced Hag2 and Hag3 as novel members of the protein family. Mol. Phylogenet. Evol. 36, 734-740 (2005).
    • (2005) Mol. Phylogenet. Evol , vol.36 , pp. 734-740
    • Persson, S.1    Rosenquist, M.2    Knoblach, B.3    Khosravi-Far, R.4    Sommarin, M.5    Michalak, M.6
  • 40
    • 0037470247 scopus 로고    scopus 로고
    • Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function
    • Shin, B.K., Wang, H., Yim, A.M.et al. Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. J. Biol. Chem. 278, 7607-7616 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 7607-7616
    • Shin, B.K.1    Wang, H.2    Yim, A.M.3
  • 41
    • 0037043123 scopus 로고    scopus 로고
    • Proteomics reveals protein profile changes in doxorubicin-treated MCF-7 human breast cancer cells
    • Chen, S.T., Pan, T.L., Tsai, Y.C., and Huang, C. M. Proteomics reveals protein profile changes in doxorubicin-treated MCF-7 human breast cancer cells. Cancer Lett. 181, 95-107 (2002).
    • (2002) Cancer Lett , vol.181 , pp. 95-107
    • Chen, S.T.1    Pan, T.L.2    Tsai, Y.C.3    Huang, C.M.4
  • 42
    • 0031473848 scopus 로고    scopus 로고
    • Protein expression profiles in human breast ductal carcinoma and histologically normal tissue
    • Bini, L., Magi, B., Marzocchi, B. et al. Protein expression profiles in human breast ductal carcinoma and histologically normal tissue. Electrophoresis 18, 2832-2841 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2832-2841
    • Bini, L.1    Magi, B.2    Marzocchi, B.3
  • 43
    • 0030790275 scopus 로고    scopus 로고
    • Nitric oxide in the vasculature: Physiology and pathophysiology
    • Moncada, S. Nitric oxide in the vasculature: Physiology and pathophysiology. Ann. NY Acad. Sci. 811, 60-67 (1997).
    • (1997) Ann. NY Acad. Sci , vol.811 , pp. 60-67
    • Moncada, S.1
  • 44
    • 0032786731 scopus 로고    scopus 로고
    • Oxidative stress indicators are elevated in de novo Parkinson's disease patients
    • Ilic, T.V., Jovanovic, M., Jovicic, A., and Tomovic, M. Oxidative stress indicators are elevated in de novo Parkinson's disease patients. Funct. Neurol. 14, 141-147 (1999).
    • (1999) Funct. Neurol , vol.14 , pp. 141-147
    • Ilic, T.V.1    Jovanovic, M.2    Jovicic, A.3    Tomovic, M.4
  • 45
    • 0042528615 scopus 로고    scopus 로고
    • Nitric oxide and reactive oxygen species in Parkinson's disease
    • Tieu, K., Ischiropoulos, H., and Przedborski, S. Nitric oxide and reactive oxygen species in Parkinson's disease. IUBMB Life 55, 329-335 (2003).
    • (2003) IUBMB Life , vol.55 , pp. 329-335
    • Tieu, K.1    Ischiropoulos, H.2    Przedborski, S.3
  • 46
    • 0038345017 scopus 로고    scopus 로고
    • Cancer drugs, genetic variation and the glutathione-S-transferase gene family
    • Townsend, D. and Tew, K. Cancer drugs, genetic variation and the glutathione-S-transferase gene family. Am. J. Pharmacogenomics 3, 157-172 (2003).
    • (2003) Am. J. Pharmacogenomics , vol.3 , pp. 157-172
    • Townsend, D.1    Tew, K.2
  • 47
    • 0028302827 scopus 로고
    • Activated murine macrophages induce apoptosis in tumor cells through nitric oxide-dependent or -independent mechanisms
    • Cui, S., Reichner, J.S., Mateo, R.B., and Albina, J.E. Activated murine macrophages induce apoptosis in tumor cells through nitric oxide-dependent or -independent mechanisms. Cancer Res. 54, 2462-2467 (1994).
    • (1994) Cancer Res , vol.54 , pp. 2462-2467
    • Cui, S.1    Reichner, J.S.2    Mateo, R.B.3    Albina, J.E.4
  • 48
    • 0030918451 scopus 로고    scopus 로고
    • Targeting nitric oxide (NO) delivery in vivo. Design of a liver-selective NO donor prodrug that blocks tumor necrosis factor-alpha-induced apoptosis and toxicity in the liver
    • Saavedra, J.E., Billiar, T.R., Williams, D.L., Kim, Y.M., Watkins, S.C., and Keefer, LK. Targeting nitric oxide (NO) delivery in vivo. Design of a liver-selective NO donor prodrug that blocks tumor necrosis factor-alpha-induced apoptosis and toxicity in the liver. J. Med. Chem. 40, 1947-1954 (1997).
    • (1997) J. Med. Chem , vol.40 , pp. 1947-1954
    • Saavedra, J.E.1    Billiar, T.R.2    Williams, D.L.3    Kim, Y.M.4    Watkins, S.C.5    Keefer, L.K.6
  • 49
    • 0033928781 scopus 로고    scopus 로고
    • The influence of coordinate over-expression of glutathione phase II detoxification gene products on drug resistance
    • O'Brien, M., Kruh, G.D. and Tew, K.D. The influence of coordinate over-expression of glutathione phase II detoxification gene products on drug resistance. J. Pharmacol. Exp. Ther. 294, 480-487 (2000).
    • (2000) J. Pharmacol. Exp. Ther , vol.294 , pp. 480-487
    • O'Brien, M.1    Kruh, G.D.2    Tew, K.D.3
  • 50
    • 38349072452 scopus 로고    scopus 로고
    • Unpublished results
    • Townsend, D.M. (Unpublished results.)
    • Townsend, D.M.1
  • 51
    • 33746111275 scopus 로고    scopus 로고
    • A novel role for human sulfiredoxin in the reversal of glutathionylation
    • Findlay, V.J., Townsend, D.M., Morris, T.E., Fraser, J.P., He, L., and Tew, K.D. A novel role for human sulfiredoxin in the reversal of glutathionylation. Cancer Res. 66, 6800-6806 (2006).
    • (2006) Cancer Res , vol.66 , pp. 6800-6806
    • Findlay, V.J.1    Townsend, D.M.2    Morris, T.E.3    Fraser, J.P.4    He, L.5    Tew, K.D.6
  • 52
    • 27744569935 scopus 로고    scopus 로고
    • A novel thiol oxidation-based mechanism for adriamycin-induced cell injury in human macrophages
    • Asmis, R., Wang, Y., Xu, L., Kisgati, M., Begley, J.G., and Mieyal, J.J. A novel thiol oxidation-based mechanism for adriamycin-induced cell injury in human macrophages. FASEB J. 19, 1866-1868 (2005).
    • (2005) FASEB J , vol.19 , pp. 1866-1868
    • Asmis, R.1    Wang, Y.2    Xu, L.3    Kisgati, M.4    Begley, J.G.5    Mieyal, J.J.6
  • 53
    • 34548082036 scopus 로고    scopus 로고
    • Redox pathways in cancer drug discovery
    • Tew, K.D. and Ali-Osman, F. Redox pathways in cancer drug discovery. Curr. Opin. Pharmacol. 7, 353-354 (2007).
    • (2007) Curr. Opin. Pharmacol , vol.7 , pp. 353-354
    • Tew, K.D.1    Ali-Osman, F.2
  • 54
    • 42349109794 scopus 로고    scopus 로고
    • NOV-002, a glutathione disulfide mimetic,as a modulator of cellular redox balance
    • in press
    • Townsend, D.M., et al. NOV-002, a glutathione disulfide mimetic,as a modulator of cellular redox balance. Cancer Res. (in press).
    • Cancer Res
    • Townsend, D.M.1
  • 57
    • 33750803208 scopus 로고    scopus 로고
    • Membrane skeletal protein S-glutathionylation and hemolysis in human red blood cells
    • Rossi, R., Giustarini, D., Milzani, A., and Dalle-Donne, I. Membrane skeletal protein S-glutathionylation and hemolysis in human red blood cells. Blood Cells Mol. Dis. 37, 180-187 (2006).
    • (2006) Blood Cells Mol. Dis , vol.37 , pp. 180-187
    • Rossi, R.1    Giustarini, D.2    Milzani, A.3    Dalle-Donne, I.4
  • 58
    • 0347635415 scopus 로고    scopus 로고
    • Modulation of the redox state of tubulin by the glutathione/glutaredoxin reductase system
    • Landino, L.M., Moynihan, K.L., Todd, J.V., Kennett, K.L. Modulation of the redox state of tubulin by the glutathione/glutaredoxin reductase system. Biochem. Biophys. Res. Commun. 314, 555-560 (2004).
    • (2004) Biochem. Biophys. Res. Commun , vol.314 , pp. 555-560
    • Landino, L.M.1    Moynihan, K.L.2    Todd, J.V.3    Kennett, K.L.4
  • 59
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli, M., Demol, H., Puype, M. et al. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc. Natl. Acad. Sci. USA 99, 3505-3510 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3
  • 60
    • 0036369545 scopus 로고    scopus 로고
    • S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: Role of thiol oxidation and catalysis by glutaredoxin
    • Cotgreave, I.A., Gerdes, R., Schuppe-Koistinen, I., and Lind, C. S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: role of thiol oxidation and catalysis by glutaredoxin. Methods Enzymol. 348, 175-182 (2002).
    • (2002) Methods Enzymol , vol.348 , pp. 175-182
    • Cotgreave, I.A.1    Gerdes, R.2    Schuppe-Koistinen, I.3    Lind, C.4
  • 61
    • 0345146921 scopus 로고    scopus 로고
    • Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status
    • Nulton-Persson, A.C. Starke, D.W., Mieyal, J.J., and Sweda, L.I. Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status. Biochemistry 42, 4235-4242 (2003).
    • (2003) Biochemistry , vol.42 , pp. 4235-4242
    • Nulton-Persson, A.C.1    Starke, D.W.2    Mieyal, J.J.3    Sweda, L.I.4
  • 62
    • 0037490142 scopus 로고    scopus 로고
    • Reversible glutathionylation of complex I increases mitochondrial superoxide formation
    • Taylor, E.R., Hurrell, F., Shannon, R.J., Lin, T.K., Hirst, J., and Murphy, M.P. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J. Biol. Chem. 278, 19603-19610 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 19603-19610
    • Taylor, E.R.1    Hurrell, F.2    Shannon, R.J.3    Lin, T.K.4    Hirst, J.5    Murphy, M.P.6
  • 63
    • 15444367716 scopus 로고    scopus 로고
    • Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation
    • Kil, I.S. and Park, J.W. Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation. J. Biol. Chem. 280, 10846-10854 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 10846-10854
    • Kil, I.S.1    Park, J.W.2
  • 64
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr, S., Hallak, H., de Boitte, A., Lapetina, E.G., and Brüne, B. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 274, 9427-94230 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 9427-94230
    • Mohr, S.1    Hallak, H.2    de Boitte, A.3    Lapetina, E.G.4    Brüne, B.5
  • 66
    • 0034662178 scopus 로고    scopus 로고
    • Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation
    • Klatt, P., Pineda Molena, E., Perez-Sala, D., and Lamas, S. Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation. Biochem J. 349, 567-578 (2000).
    • (2000) Biochem J , vol.349 , pp. 567-578
    • Klatt, P.1    Pineda Molena, E.2    Perez-Sala, D.3    Lamas, S.4
  • 67
    • 2542483699 scopus 로고    scopus 로고
    • Oxidative inhibition of human soluble catechol-O-methyltransferase
    • Cotton, N.J., Stoddard, B. and Parson, W.W. Oxidative inhibition of human soluble catechol-O-methyltransferase. J. Biol. Chem. 279, 23710-23718 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 23710-23718
    • Cotton, N.J.1    Stoddard, B.2    Parson, W.W.3
  • 68
    • 0034953329 scopus 로고    scopus 로고
    • Bcl-2-dependent oxidation of pyruvate dehydrogenase-E2, a primary biliary cirrhosis autoantigen, during apoptosis
    • Odin, J.A., Huebert, R.C., Casciola-Rosen, L., LaRusso, N.F., and Rosen, A. Bcl-2-dependent oxidation of pyruvate dehydrogenase-E2, a primary biliary cirrhosis autoantigen, during apoptosis. J. Clin. Invest. 108, 223-232 (2001).
    • (2001) J. Clin. Invest , vol.108 , pp. 223-232
    • Odin, J.A.1    Huebert, R.C.2    Casciola-Rosen, L.3    LaRusso, N.F.4    Rosen, A.5
  • 69
    • 23944468310 scopus 로고    scopus 로고
    • Redox regulation of PTEN by S-nitrosothiols
    • Yu, C.X., Li, S., and Whorton, A.R. Redox regulation of PTEN by S-nitrosothiols. Mol. Pharmacol. 68, 847-854 (2005).
    • (2005) Mol. Pharmacol , vol.68 , pp. 847-854
    • Yu, C.X.1    Li, S.2    Whorton, A.R.3
  • 70
    • 33748339203 scopus 로고    scopus 로고
    • Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta
    • Reynaert, N.L., van der Vilet, A., Guala, A.S. et al. Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta. Proc. Natl. Acad. Sci. USA 103, 13086-13091 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13086-13091
    • Reynaert, N.L.1    van der Vilet, A.2    Guala, A.S.3
  • 71
    • 34250328361 scopus 로고    scopus 로고
    • Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Muller cells: Model of diabetic retinopathy
    • Shelton, M.D., Kern, T.S., and Mieyal, J.J. Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Muller cells: Model of diabetic retinopathy. J. Biol. Chem. 282, 12467-12474 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 12467-12474
    • Shelton, M.D.1    Kern, T.S.2    Mieyal, J.J.3
  • 72
    • 0034702868 scopus 로고    scopus 로고
    • Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): A potential mechanism of PKC isozyme regulation
    • Ward, N.E., Stewart, J.R., Ioannides, C.G., and O'Brian, C.A. Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): a potential mechanism of PKC isozyme regulation. Biochemistry 39, 10319-10329 (2000).
    • (2000) Biochemistry , vol.39 , pp. 10319-10329
    • Ward, N.E.1    Stewart, J.R.2    Ioannides, C.G.3    O'Brian, C.A.4
  • 74
    • 13244283230 scopus 로고    scopus 로고
    • Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification
    • Humphries, K.M., Deal, M.S. and Taylor, S.S. Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification. J. Biol. Chem. 280, 2750-2758 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 2750-2758
    • Humphries, K.M.1    Deal, M.S.2    Taylor, S.S.3
  • 75
    • 34648837103 scopus 로고    scopus 로고
    • The functional role of cysteine residues for c-Abl kinase activity
    • Leonberg, A.K. and Chai, Y.C.The functional role of cysteine residues for c-Abl kinase activity. Mol. Cell. Biochem. 304, 207-212 (2007).
    • (2007) Mol. Cell. Biochem , vol.304 , pp. 207-212
    • Leonberg, A.K.1    Chai, Y.C.2
  • 76
    • 34347329257 scopus 로고    scopus 로고
    • Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress
    • Velu, C.S., Niture, S.K., Doneanu, C.E., Pattabiraman, N., and Srivenugopal, K.S. Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress. Biochemistry 46, 7765-7780 (2007).
    • (2007) Biochemistry , vol.46 , pp. 7765-7780
    • Velu, C.S.1    Niture, S.K.2    Doneanu, C.E.3    Pattabiraman, N.4    Srivenugopal, K.S.5
  • 77
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi, T., Pinentel, D.R., Heilbeck, T., Hou, X., Lee, Y.J., Jiang, B. Ido, Y., and Cohen, R.A. S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J. Biol. Chem. 279, 29857-29862 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pinentel, D.R.2    Heilbeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 78
    • 18944390851 scopus 로고    scopus 로고
    • Affinity of S100A1 protein for calcium increases dramatically upon glutathionylation
    • Goch, G., Vdovenko, S., Kozlowska, H., and Bierzynski, A. Affinity of S100A1 protein for calcium increases dramatically upon glutathionylation. FEBS J. 272, 2557-2565 (2005).
    • (2005) FEBS J , vol.272 , pp. 2557-2565
    • Goch, G.1    Vdovenko, S.2    Kozlowska, H.3    Bierzynski, A.4
  • 79
    • 9144266981 scopus 로고    scopus 로고
    • S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • Adachi, T., Weisbrod, R.M., Pimental, D.R., Ying, J., Sharov, V.S., Schoneich, C., and Cohen, R.A. S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat. Med. 10, 1200-1207 (2004).
    • (2004) Nat. Med , vol.10 , pp. 1200-1207
    • Adachi, T.1    Weisbrod, R.M.2    Pimental, D.R.3    Ying, J.4    Sharov, V.S.5    Schoneich, C.6    Cohen, R.A.7
  • 80
    • 33748755208 scopus 로고    scopus 로고
    • A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation
    • Hidalgo, C., Sanchez, G., Barrientos, G., and Aracena-Parks, P. A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation. J. Biol. Chem. 281, 26473-26482 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 26473-26482
    • Hidalgo, C.1    Sanchez, G.2    Barrientos, G.3    Aracena-Parks, P.4
  • 81
    • 13544274436 scopus 로고    scopus 로고
    • Reversible silencing of CFTR chloride channels by glutathionylation
    • Wang, W., Oliva, C., Li, G., Holmgren, A., Lillig, C.H., and Kirk, K.L. Reversible silencing of CFTR chloride channels by glutathionylation. J. Gen. Physiol. 125, 127-141 (2005).
    • (2005) J. Gen. Physiol , vol.125 , pp. 127-141
    • Wang, W.1    Oliva, C.2    Li, G.3    Holmgren, A.4    Lillig, C.H.5    Kirk, K.L.6
  • 82
    • 27244462417 scopus 로고    scopus 로고
    • Glutathiolation of the proteasome is enhanced by proteolytic inhibitors
    • Demasi, M., Shringarpure, R., and Davies, K.J. Glutathiolation of the proteasome is enhanced by proteolytic inhibitors. Arch. Biochem. Biophys. 389, 254-263 (2001).
    • (2001) Arch. Biochem. Biophys , vol.389 , pp. 254-263
    • Demasi, M.1    Shringarpure, R.2    Davies, K.J.3
  • 83
    • 33750915613 scopus 로고    scopus 로고
    • Thioredoxin-1 and posttranslational modifications
    • Haendeler, J. Thioredoxin-1 and posttranslational modifications. Antioxid. Redox Signal. 8, 1723-1728 (2006).
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1723-1728
    • Haendeler, J.1
  • 85
    • 0142211205 scopus 로고    scopus 로고
    • Actin glutathionylation increases in fibroblasts of patients with Friedreich's ataxia: A potential role in the pathogenesis of the disease
    • Pastore, A., Tozzi, G., Gaeta, L.M. et al. Actin glutathionylation increases in fibroblasts of patients with Friedreich's ataxia: a potential role in the pathogenesis of the disease. J. Biol. Chem. 278, 42588-42595 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 42588-42595
    • Pastore, A.1    Tozzi, G.2    Gaeta, L.M.3
  • 87
    • 24144493633 scopus 로고    scopus 로고
    • Structural insights into Alzheimer filament assembly pathways based on site-directed mutagenesis and S-glutathionylation of three-repeat neuronal Tau protein
    • Dinoto, L., Deture, M.A., and Purich, D.L. Structural insights into Alzheimer filament assembly pathways based on site-directed mutagenesis and S-glutathionylation of three-repeat neuronal Tau protein. Microsc. Res. Tech. 67, 156-163 (2005).
    • (2005) Microsc. Res. Tech , vol.67 , pp. 156-163
    • Dinoto, L.1    Deture, M.A.2    Purich, D.L.3
  • 89
    • 24944573462 scopus 로고    scopus 로고
    • Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy
    • Sampathkumar, R., Balasubramanyam, M., Sudarslal, S., Rema, M., Mohan, V., and Balaram, P. Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy. Clin. Biochem. 38, 892-899 (2005).
    • (2005) Clin. Biochem , vol.38 , pp. 892-899
    • Sampathkumar, R.1    Balasubramanyam, M.2    Sudarslal, S.3    Rema, M.4    Mohan, V.5    Balaram, P.6
  • 91
    • 33645114907 scopus 로고    scopus 로고
    • Absence of typical unfolded protein response in primary cultured cystic fibrosis airway epithelial cells
    • Nanua, S., Sajjan, U., Keshavjee, S., and Hershenson, M.B. Absence of typical unfolded protein response in primary cultured cystic fibrosis airway epithelial cells. Biochem. Biophys. Res. Commun. 343, 135-143 (2006).
    • (2006) Biochem. Biophys. Res. Commun , vol.343 , pp. 135-143
    • Nanua, S.1    Sajjan, U.2    Keshavjee, S.3    Hershenson, M.B.4
  • 92
    • 2642531068 scopus 로고    scopus 로고
    • The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens
    • Craghill, J., Cronshaw, A.D. and Harding, J.J. The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens. Biochem J. 379, 595-600 (2004).
    • (2004) Biochem J , vol.379 , pp. 595-600
    • Craghill, J.1    Cronshaw, A.D.2    Harding, J.J.3
  • 93
    • 28844469323 scopus 로고    scopus 로고
    • Cataracts: Role of the unfolded protein response
    • Shinohara, T., Ikesugi, K., and Mulhern, M.L. Cataracts: Role of the unfolded protein response. Med. Hypotheses 66, 365-370 (2006).
    • (2006) Med. Hypotheses , vol.66 , pp. 365-370
    • Shinohara, T.1    Ikesugi, K.2    Mulhern, M.L.3
  • 94
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide bond formation and the ER redox environment by feedback regulation of ERO1
    • Sevier, C.S., Qu, H., Heldman, N., Gross, E., Fass, D., and Kaiser, C.A. Modulation of cellular disulfide bond formation and the ER redox environment by feedback regulation of ERO1. Cell 129, 333-344 (2007).
    • (2007) Cell , vol.129 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.