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Volumn 312, Issue 4, 2003, Pages 1005-1010

Reduction of Sulindac to its active metabolite, sulindac sulfide: Assay and role of the methionine sulfoxide reductase system

Author keywords

Methionine sulfoxide reductase; Sulindac; Sulindac sulfide

Indexed keywords

METHIONINE SULFOXIDE; OXIDOREDUCTASE; SULINDAC; SULINDAC SULFIDE;

EID: 0345357813     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.10.203     Document Type: Article
Times cited : (51)

References (47)
  • 2
    • 0032564345 scopus 로고    scopus 로고
    • Overexpression of peptide methionine sulfoxide reductase (MsrA) in Saccharomyces cerevisiae and human T-cells provide them with high resistance with oxidative stress
    • Moskovitz J., Flescher E., Berlett B.S., Azare J.A., Poston M., Stadtman E.R. Overexpression of peptide methionine sulfoxide reductase (MsrA) in Saccharomyces cerevisiae and human T-cells provide them with high resistance with oxidative stress. Proc. Natl. Acad. Sci. USA. 95:1998;14071-14075.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14071-14075
    • Moskovitz, J.1    Flescher, E.2    Berlett, B.S.3    Azare, J.A.4    Poston, M.5    Stadtman, E.R.6
  • 4
    • 0026752653 scopus 로고
    • Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene
    • Rahman M.A., Nelson H., Weissbach H., Brot N. Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene. J. Biol. Chem. 267:1992;15549-15551.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15549-15551
    • Rahman, M.A.1    Nelson, H.2    Weissbach, H.3    Brot, N.4
  • 5
    • 0034619554 scopus 로고    scopus 로고
    • Structure and mechanism of methionine sulfoxide reductase, an "anti-oxidation" enzyme
    • Lowther W.T., Brot N., Weissbach H., Matthews B.W. Structure and mechanism of methionine sulfoxide reductase, an "anti-oxidation" enzyme. Biochemistry. 39:2000;13307-13312.
    • (2000) Biochemistry , vol.39 , pp. 13307-13312
    • Lowther, W.T.1    Brot, N.2    Weissbach, H.3    Matthews, B.W.4
  • 6
    • 0029935647 scopus 로고    scopus 로고
    • Cloning and expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins
    • Moskovitz J., Weissbach H., Brot N. Cloning and expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc. Natl. Acad. Sci. USA. 93:1996;2095-2099.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2095-2099
    • Moskovitz, J.1    Weissbach, H.2    Brot, N.3
  • 7
    • 0032815727 scopus 로고    scopus 로고
    • Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase
    • Sharov V.S., Ferrington D.A., Squier T.C., Schoneich C. Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase. FEBS Lett. 455:1999;247-250.
    • (1999) FEBS Lett. , vol.455 , pp. 247-250
    • Sharov, V.S.1    Ferrington, D.A.2    Squier, T.C.3    Schoneich, C.4
  • 8
    • 0034640506 scopus 로고    scopus 로고
    • Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
    • Moskovitz J., Poston M., Berlett B.S., Nosworthy J.N., Szczepanowski R., Stadtman E.R. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J. Biol. Chem. 275:2000;14167-14172.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14167-14172
    • Moskovitz, J.1    Poston, M.2    Berlett, B.S.3    Nosworthy, J.N.4    Szczepanowski, R.5    Stadtman, E.R.6
  • 10
    • 0036239041 scopus 로고    scopus 로고
    • The "mirrored" methionine sulfoxide reductases of Neisseria gonorrhoeae pilB
    • Lowther W.T., Weissbach H., Etienne F., Brot N., Matthews B.W. The "mirrored" methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nat. Struct. Biol. 9(5):2002;348-352.
    • (2002) Nat. Struct. Biol. , vol.9 , Issue.5 , pp. 348-352
    • Lowther, W.T.1    Weissbach, H.2    Etienne, F.3    Brot, N.4    Matthews, B.W.5
  • 11
    • 0037023730 scopus 로고    scopus 로고
    • Characterization of the methionine sufoxide reductase activities of pilB, a probable virulence factor from Neisseria meningitides
    • Orly A., Boschi-Muller S., Marrand M., Sanglier-Cianferani S., Van Dorsselear A., Branlant G. Characterization of the methionine sufoxide reductase activities of pilB, a probable virulence factor from Neisseria meningitides. J. Biol. Chem. 277:2002;12022-12106.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12022-12106
    • Orly, A.1    Boschi-Muller, S.2    Marrand, M.3    Sanglier-Cianferani, S.4    Van Dorsselear, A.5    Branlant, G.6
  • 12
    • 0036297758 scopus 로고    scopus 로고
    • Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
    • Moskovitz J., Singh V.K., Requena J., Wilkinson B.J., Jayaswal R.K., Stadtman E.R. Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity. Biochem. Biophys. Res. Commun. 290:2002;62-65.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 62-65
    • Moskovitz, J.1    Singh, V.K.2    Requena, J.3    Wilkinson, B.J.4    Jayaswal, R.K.5    Stadtman, E.R.6
  • 13
    • 0037007089 scopus 로고    scopus 로고
    • Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase
    • Kryukov G.V., Kumara A., Koc A., Sun Z., Gladyshev V.N. Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc. Natl. Acad. Sci. USA. 99:2002;4245-4250.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4245-4250
    • Kryukov, G.V.1    Kumara, A.2    Koc, A.3    Sun, Z.4    Gladyshev, V.N.5
  • 14
    • 0037427533 scopus 로고    scopus 로고
    • A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide
    • Etienne F., Spector D., Brot N., Weissbach H. A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide. Biochem. Biophys. Res. Commun. 300:2003;378-382.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 378-382
    • Etienne, F.1    Spector, D.2    Brot, N.3    Weissbach, H.4
  • 15
    • 0037428256 scopus 로고    scopus 로고
    • New membrane associated and soluble peptide methionine sulfoxide reductases in Escherichia coli
    • Spector D., Etienne F., Brot N., Weissbach H. New membrane associated and soluble peptide methionine sulfoxide reductases in Escherichia coli. Biochem. Biophys. Res. Commun. 302:2003;284-289.
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 284-289
    • Spector, D.1    Etienne, F.2    Brot, N.3    Weissbach, H.4
  • 16
    • 0015237292 scopus 로고
    • Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs
    • Vane J.R. Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nat. New Biol. 231:1971;232-235.
    • (1971) Nat. New Biol. , vol.231 , pp. 232-235
    • Vane, J.R.1
  • 18
    • 0032556188 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibitors in tumorigenesis (part 1)
    • Taketo M.M. Cyclooxygenase-2 inhibitors in tumorigenesis (part 1). J. Natl. Cancer Inst. 90:1998;1529-1536.
    • (1998) J. Natl. Cancer Inst. , vol.90 , pp. 1529-1536
    • Taketo, M.M.1
  • 19
    • 0032483712 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibitors in tumorigenesis (part 2)
    • Taketo M.M. Cyclooxygenase-2 inhibitors in tumorigenesis (part 2). J. Natl. Cancer Inst. 90:1998;1609-1620.
    • (1998) J. Natl. Cancer Inst. , vol.90 , pp. 1609-1620
    • Taketo, M.M.1
  • 21
    • 0038543824 scopus 로고    scopus 로고
    • Chemoprevention of colorectal cancer
    • Janne P.A., Mayer R.J. Chemoprevention of colorectal cancer. N. Engl. J. Med. 342:2000;1960-1968.
    • (2000) N. Engl. J. Med. , vol.342 , pp. 1960-1968
    • Janne, P.A.1    Mayer, R.J.2
  • 23
    • 0037032482 scopus 로고    scopus 로고
    • Selective cyclooxygenase-2 inhibitors show a differential ability to inhibit proliferation and induce apoptosis of colon adenocarcinoma cells
    • Yamazaki R., Kusunoki N., Matsuzaki T., Hashimoto S., Kawai S. Selective cyclooxygenase-2 inhibitors show a differential ability to inhibit proliferation and induce apoptosis of colon adenocarcinoma cells. FEBS Lett. 531:2002;278-284.
    • (2002) FEBS Lett. , vol.531 , pp. 278-284
    • Yamazaki, R.1    Kusunoki, N.2    Matsuzaki, T.3    Hashimoto, S.4    Kawai, S.5
  • 24
    • 0035135598 scopus 로고    scopus 로고
    • Growth inhibition and induction of apoptosis in colorectal tumor cells by cyclooxygenase inhibitors
    • Richter M., Weiss M., Weinberger I., Furstenberger G., Marian B. Growth inhibition and induction of apoptosis in colorectal tumor cells by cyclooxygenase inhibitors. Carcinogenesis. 22:2001;17-25.
    • (2001) Carcinogenesis , vol.22 , pp. 17-25
    • Richter, M.1    Weiss, M.2    Weinberger, I.3    Furstenberger, G.4    Marian, B.5
  • 25
    • 0034816925 scopus 로고    scopus 로고
    • Cyclooxygenase-independent actions of cyclooxygenase inhibitors
    • Tegeder I., Pfeilschifter J., Geisslinger G. Cyclooxygenase-independent actions of cyclooxygenase inhibitors. FASEB J. 15:2001;2057-2072.
    • (2001) FASEB J. , vol.15 , pp. 2057-2072
    • Tegeder, I.1    Pfeilschifter, J.2    Geisslinger, G.3
  • 26
    • 0035650943 scopus 로고    scopus 로고
    • Cox-2 independent induction of cell cycle arrest and apoptosis in colon cancer cells by the selective cox-2 inhibitor celecoxib
    • Grosch S., Tegeder I., Niederberger E., Brautigam L., Geisslinger G. Cox-2 independent induction of cell cycle arrest and apoptosis in colon cancer cells by the selective cox-2 inhibitor celecoxib. FASEB J. 15:2001;2742-2744.
    • (2001) FASEB J. , vol.15 , pp. 2742-2744
    • Grosch, S.1    Tegeder, I.2    Niederberger, E.3    Brautigam, L.4    Geisslinger, G.5
  • 28
    • 0033575760 scopus 로고    scopus 로고
    • Malignant transformation and antineoplastic actions of nonsteroidal anti-inflammatory drugs (NSAIDs) on cyclooxygenase-null embryo fibroblasts
    • Zhang X., Morham S.G., Langenbach R., Young D.A. Malignant transformation and antineoplastic actions of nonsteroidal anti-inflammatory drugs (NSAIDs) on cyclooxygenase-null embryo fibroblasts. J. Exp. Med. 190:1999;451-459.
    • (1999) J. Exp. Med. , vol.190 , pp. 451-459
    • Zhang, X.1    Morham, S.G.2    Langenbach, R.3    Young, D.A.4
  • 29
    • 0033139531 scopus 로고    scopus 로고
    • Sulindac sulfide, but not sulindac sulfone, inhibits colorectal cancer growth
    • Williams C.S., Goldman A.P., Sheng H., Morrow J.D., DuBois R.N. Sulindac sulfide, but not sulindac sulfone, inhibits colorectal cancer growth. Neoplasia. 1:1999;170-176.
    • (1999) Neoplasia , vol.1 , pp. 170-176
    • Williams, C.S.1    Goldman, A.P.2    Sheng, H.3    Morrow, J.D.4    Dubois, R.N.5
  • 30
    • 0036839817 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-g is a target of nonsteroidal anti-inflammatory drugs mediating cyclooxygenase-independent inhibition of lung cancer cell growth
    • Wick M., Hurteau G., Dessev C., Chan D., Geraci M.W., Winn R.A., Heasley L.E., Nemenoff R.A. Peroxisome proliferator-activated receptor-g is a target of nonsteroidal anti-inflammatory drugs mediating cyclooxygenase-independent inhibition of lung cancer cell growth. Mol. Pharmacol. 62:2002;1207-1214.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1207-1214
    • Wick, M.1    Hurteau, G.2    Dessev, C.3    Chan, D.4    Geraci, M.W.5    Winn, R.A.6    Heasley, L.E.7    Nemenoff, R.A.8
  • 31
    • 0029115954 scopus 로고
    • Sulindac sulfide, an aspirin-like compound, inhibits proliferation, causes cell cycle quiescence, and induces apoptosis in HT-29 colon adenocarcinoma cells
    • Shiff S.J., Qiao L., Tsai L.L., Rigas B. Sulindac sulfide, an aspirin-like compound, inhibits proliferation, causes cell cycle quiescence, and induces apoptosis in HT-29 colon adenocarcinoma cells. J. Clin. Invest. 96:1995;491-503.
    • (1995) J. Clin. Invest. , vol.96 , pp. 491-503
    • Shiff, S.J.1    Qiao, L.2    Tsai, L.L.3    Rigas, B.4
  • 33
    • 0035881870 scopus 로고    scopus 로고
    • Autophagy delays sulindac sulfide-induced apoptosis in the human intestinal colon cancer cell line HT-29
    • Bauvy C., Gane P., Arico S., Codogno P., Ogier-Denis E. Autophagy delays sulindac sulfide-induced apoptosis in the human intestinal colon cancer cell line HT-29. Exp. Cell Res. 268:2001;139-149.
    • (2001) Exp. Cell Res. , vol.268 , pp. 139-149
    • Bauvy, C.1    Gane, P.2    Arico, S.3    Codogno, P.4    Ogier-Denis, E.5
  • 34
    • 0035884187 scopus 로고    scopus 로고
    • Sulindac sulfide-induced apoptosis involves death receptor 5 and the caspase 8-dependent pathway in human colon and prostate cancer cells
    • Huang Y., He Q., Hillman M.J., Rong R., Sheikh M.S. Sulindac sulfide-induced apoptosis involves death receptor 5 and the caspase 8-dependent pathway in human colon and prostate cancer cells. Mol. Biol. Gen. 61(18):2001;6918-6924.
    • (2001) Mol. Biol. Gen. , vol.61 , Issue.18 , pp. 6918-6924
    • Huang, Y.1    He, Q.2    Hillman, M.J.3    Rong, R.4    Sheikh, M.S.5
  • 35
    • 0037085935 scopus 로고    scopus 로고
    • Requirement for BAX for TRAIL/ Apo2L-induced apoptosis of colorectal cancers
    • Ravi R., Bedi A. Requirement for BAX for TRAIL/ Apo2L-induced apoptosis of colorectal cancers. Cancer Res. 62:2002;1583-1587.
    • (2002) Cancer Res. , vol.62 , pp. 1583-1587
    • Ravi, R.1    Bedi, A.2
  • 36
    • 0035881570 scopus 로고    scopus 로고
    • Dietary indoles and isothiocyanates that are generated from cruciferous vegetables can both stimulate apoptosis and confer protection against DNA damage in colon cell lines
    • Bonnesen C., Eggleston I.M., Hayes J.D. Dietary indoles and isothiocyanates that are generated from cruciferous vegetables can both stimulate apoptosis and confer protection against DNA damage in colon cell lines. Cancer Res. 61:2001;6120-6130.
    • (2001) Cancer Res. , vol.61 , pp. 6120-6130
    • Bonnesen, C.1    Eggleston, I.M.2    Hayes, J.D.3
  • 38
    • 0037814982 scopus 로고    scopus 로고
    • Gene modulation by the cyclooxygenase inhibitor, sulindac sulfide, in human colorectal carcinoma cells
    • Bottone F.G. Jr., Martinez J.M., Collins J.B., Afshari C.A., Eling T.E. Gene modulation by the cyclooxygenase inhibitor, sulindac sulfide, in human colorectal carcinoma cells. Biol. Chem. 278:2003;25790-25801.
    • (2003) Biol. Chem. , vol.278 , pp. 25790-25801
    • Bottone, F.G.Jr.1    Martinez, J.M.2    Collins, J.B.3    Afshari, C.A.4    Eling, T.E.5
  • 39
    • 0019980984 scopus 로고
    • Reduction of N-acetyl methionine sulfoxide: A simple assay for peptide methionine sulfoxide reductase
    • Brot N., Werth J., Koster D., Weissbach H. Reduction of N-acetyl methionine sulfoxide: a simple assay for peptide methionine sulfoxide reductase. Anal. Biochem. 122:1982;291-294.
    • (1982) Anal. Biochem. , vol.122 , pp. 291-294
    • Brot, N.1    Werth, J.2    Koster, D.3    Weissbach, H.4
  • 40
    • 0001738417 scopus 로고
    • The formation, resolution and optical properties of the diastereoisometric sulfoxides derived from L-methionine
    • Lavine F.T. The formation, resolution and optical properties of the diastereoisometric sulfoxides derived from L-methionine. J. Biol. Chem. 169:1947;477-491.
    • (1947) J. Biol. Chem. , vol.169 , pp. 477-491
    • Lavine, F.T.1
  • 41
    • 0028535189 scopus 로고
    • Reduction of DABS-L-methionine-DL-sulfoxide by protein methionine sulfoxide reductase from polymorphonuclear leukocytes: Stereospecificity towards the L-sulfoxide
    • Minetti G., Balduin C., Brovelli A. Reduction of DABS-L-methionine-DL- sulfoxide by protein methionine sulfoxide reductase from polymorphonuclear leukocytes: stereospecificity towards the L-sulfoxide. Ital. J. Biochem. 43:1994;273-283.
    • (1994) Ital. J. Biochem. , vol.43 , pp. 273-283
    • Minetti, G.1    Balduin, C.2    Brovelli, A.3
  • 42
    • 0026469612 scopus 로고
    • High level expression and purification of peptide methionine sulfoxide reductase in Escherichia coli
    • Rahman M.A., Brot N., Weissbach H. High level expression and purification of peptide methionine sulfoxide reductase in Escherichia coli. Cell. Mol. Biol. 38:1992;529-542.
    • (1992) Cell. Mol. Biol. , vol.38 , pp. 529-542
    • Rahman, M.A.1    Brot, N.2    Weissbach, H.3
  • 43
    • 0036617120 scopus 로고    scopus 로고
    • Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins
    • Hansel A., Kuschel L., Hehl S., Lemke C., Agricola H.J., Hoshi T., Heinemann S.H. Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. FASEB J. 16:2002;911-913.
    • (2002) FASEB J. , vol.16 , pp. 911-913
    • Hansel, A.1    Kuschel, L.2    Hehl, S.3    Lemke, C.4    Agricola, H.J.5    Hoshi, T.6    Heinemann, S.H.7
  • 44
    • 0041845204 scopus 로고    scopus 로고
    • Subcellular localization of methionine sulfoxide reductase a (MsrA): Evidence for mitochondrial and cytosolic isoforms in rat liver cells
    • Vougier S., Mary J., Friguet B. Subcellular localization of methionine sulfoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. Biochem. J. 373:2003;531-537.
    • (2003) Biochem. J. , vol.373 , pp. 531-537
    • Vougier, S.1    Mary, J.2    Friguet, B.3
  • 45
    • 0029912239 scopus 로고    scopus 로고
    • Chromosomal localization of the mammalian peptide methionine sulfoxide reductase gene and its differential expression in various tissues
    • Moskovitz J., Jenkins N., Gilbert D.J., Copeland N.G., Jursky F., Weissbach H., Brot N. Chromosomal localization of the mammalian peptide methionine sulfoxide reductase gene and its differential expression in various tissues. Proc. Natl. Acad. Sci. USA. 93:1996;3205-3208.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3205-3208
    • Moskovitz, J.1    Jenkins, N.2    Gilbert, D.J.3    Copeland, N.G.4    Jursky, F.5    Weissbach, H.6    Brot, N.7
  • 46
    • 0037063326 scopus 로고    scopus 로고
    • Activity, tissue, distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: HCBS1
    • Jung S., Hansel A., Kasperczyk H., Hoshi T., Heinemann S.H. Activity, tissue, distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1. FEBS Lett. 527:2002;91-94.
    • (2002) FEBS Lett. , vol.527 , pp. 91-94
    • Jung, S.1    Hansel, A.2    Kasperczyk, H.3    Hoshi, T.4    Heinemann, S.H.5
  • 47
    • 0032783980 scopus 로고    scopus 로고
    • Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases
    • Huang W., Escribano J., Sarfarazi M., Coca-Prados M. Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases. Gene. 233:1999;233-240.
    • (1999) Gene , vol.233 , pp. 233-240
    • Huang, W.1    Escribano, J.2    Sarfarazi, M.3    Coca-Prados, M.4


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