메뉴 건너뛰기




Volumn 162, Issue 3, 2006, Pages 228-236

Further evidence that rat liver microsomal glutathione transferase 1 is not a cellular protein target for S-nitrosylation

Author keywords

Biotin switch method; Hepatocyte; Microsomal glutathione S transferase 1; Reactive nitrogen species; S Nitrosoglutathione; S Nitrosylation

Indexed keywords

2,3 NAPHTHALENEDIAMINE; BIOTIN; ENZYME ANTIBODY; GLUTATHIONE TRANSFERASE; MICROSOMAL GLUTATHIONE TRANSFERASE 1; MICROSOME ENZYME; MITOCHONDRIAL PROTEIN; MONOCLONAL ANTIBODY; NAPHTHALENE DERIVATIVE; NITRIC OXIDE; PROTEIN; S NITROSOCYSTEINE; S NITROSOGLUTATHIONE; S NITROSOTHIOL; UNCLASSIFIED DRUG;

EID: 33748752041     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2006.06.010     Document Type: Article
Times cited : (2)

References (35)
  • 1
    • 0020209472 scopus 로고
    • Microsomal glutathione S-transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione S-transferases A, B and C
    • Morgenstern R., Guthenberg C., and Depierre J.W. Microsomal glutathione S-transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione S-transferases A, B and C. Eur. J. Biochem. 128 (1982) 243-248
    • (1982) Eur. J. Biochem. , vol.128 , pp. 243-248
    • Morgenstern, R.1    Guthenberg, C.2    Depierre, J.W.3
  • 2
    • 0027276544 scopus 로고
    • Evidence that rat liver microsomal glutathione transferase is responsible for glutathione-dependent protection against lipid peroxidation
    • Mosialou E., Ekstrom G., Adang A.E., and Morgenstern R. Evidence that rat liver microsomal glutathione transferase is responsible for glutathione-dependent protection against lipid peroxidation. Biochem. Pharmacol. 45 (1993) 1645-1651
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 1645-1651
    • Mosialou, E.1    Ekstrom, G.2    Adang, A.E.3    Morgenstern, R.4
  • 3
    • 4444316044 scopus 로고    scopus 로고
    • Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1
    • Busenlehner L.S., Codreanu S.G., Holm P.J., Bhakat P., Hebert H., Morgenstern R., and Armstrong R.N. Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1. Biochemistry 43 (2004) 11145-11152
    • (2004) Biochemistry , vol.43 , pp. 11145-11152
    • Busenlehner, L.S.1    Codreanu, S.G.2    Holm, P.J.3    Bhakat, P.4    Hebert, H.5    Morgenstern, R.6    Armstrong, R.N.7
  • 4
    • 0037222168 scopus 로고    scopus 로고
    • Activation of microsomal glutathione S-transferase by peroxynitrite
    • Ji Y., and Bennett B.M. Activation of microsomal glutathione S-transferase by peroxynitrite. Mol. Pharmacol. 63 (2003) 136-146
    • (2003) Mol. Pharmacol. , vol.63 , pp. 136-146
    • Ji, Y.1    Bennett, B.M.2
  • 5
    • 33644850478 scopus 로고    scopus 로고
    • Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione S-transferase by peroxynitrite
    • Ji Y., Neverova I., Van Eyk J.E., and Bennett B.M. Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione S-transferase by peroxynitrite. J. Biol. Chem. 281 (2006) 1986-1991
    • (2006) J. Biol. Chem. , vol.281 , pp. 1986-1991
    • Ji, Y.1    Neverova, I.2    Van Eyk, J.E.3    Bennett, B.M.4
  • 6
    • 0037090937 scopus 로고    scopus 로고
    • Regulation of microsomal and cytosolic glutathione S-transferase activities by S-nitrosylation
    • Ji Y., Toader V., and Bennett B.M. Regulation of microsomal and cytosolic glutathione S-transferase activities by S-nitrosylation. Biochem. Pharmacol. 63 (2002) 1397-1404
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 1397-1404
    • Ji, Y.1    Toader, V.2    Bennett, B.M.3
  • 7
    • 0006674617 scopus 로고    scopus 로고
    • Protein S-thiolation and redox regulation of membrane-bound glutathione transferase
    • Sies H., Dafre A.L., Ji Y., and Akerboom T.P. Protein S-thiolation and redox regulation of membrane-bound glutathione transferase. Chem. Biol. Interact. 111-112 (1998) 177-185
    • (1998) Chem. Biol. Interact. , vol.111-112 , pp. 177-185
    • Sies, H.1    Dafre, A.L.2    Ji, Y.3    Akerboom, T.P.4
  • 9
    • 0024321876 scopus 로고
    • Activation of rat liver microsomal glutathione transferase by limited proteolysis
    • Morgenstern R., Lundquist G., Jornvall H., and DePierre J.W. Activation of rat liver microsomal glutathione transferase by limited proteolysis. Biochem. J. 260 (1989) 577-582
    • (1989) Biochem. J. , vol.260 , pp. 577-582
    • Morgenstern, R.1    Lundquist, G.2    Jornvall, H.3    DePierre, J.W.4
  • 10
    • 15944380094 scopus 로고    scopus 로고
    • Microsomal glutathione transferase 1 is not S-nitrosylated in rat liver microsomes or in endotoxin challenged rats
    • Shi Q., and Lou Y.J. Microsomal glutathione transferase 1 is not S-nitrosylated in rat liver microsomes or in endotoxin challenged rats. Pharmacol. Res. 51 (2005) 303-310
    • (2005) Pharmacol. Res. , vol.51 , pp. 303-310
    • Shi, Q.1    Lou, Y.J.2
  • 12
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey S.R., and Snyder S.H. The biotin switch method for the detection of S-nitrosylated proteins. Sci. STKE. PL1. (2001)
    • (2001) Sci. STKE. PL1.
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 13
    • 20444429884 scopus 로고    scopus 로고
    • Detection and identification of S-nitrosylated proteins in endothelial cells
    • Martinez-Ruiz A., and Lamas S. Detection and identification of S-nitrosylated proteins in endothelial cells. Methods Enzymol. 396 (2005) 131-139
    • (2005) Methods Enzymol. , vol.396 , pp. 131-139
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 14
    • 14644423288 scopus 로고    scopus 로고
    • Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins
    • Zhang Y., Keszler A., Broniowska K.A., and Hogg N. Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins. Free. Radical Biol. Med. 38 (2005) 874-881
    • (2005) Free. Radical Biol. Med. , vol.38 , pp. 874-881
    • Zhang, Y.1    Keszler, A.2    Broniowska, K.A.3    Hogg, N.4
  • 15
    • 29644434588 scopus 로고    scopus 로고
    • Ascorbic acid reduction of microtubule protein disulfides and its relevance to protein S-nitrosylation assays
    • Landino L.M., Koumas M.T., Mason C.E., and Alston J.A. Ascorbic acid reduction of microtubule protein disulfides and its relevance to protein S-nitrosylation assays. Biochem. Biophys. Res. Commun. 340 (2006) 347-352
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 347-352
    • Landino, L.M.1    Koumas, M.T.2    Mason, C.E.3    Alston, J.A.4
  • 16
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • Lindermayr C., Saalbach G., and Durner J. Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant. Physiol. 137 (2005) 921-930
    • (2005) Plant. Physiol. , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 19
    • 0037155791 scopus 로고    scopus 로고
    • Basal and stimulated protein S-nitrosylation in multiple cell types and tissues
    • Gow A.J., Chen Q., Hess D.T., Day B.J., Ischiropoulos H., and Stamler J.S. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J. Biol. Chem. 277 (2002) 9637-9640
    • (2002) J. Biol. Chem. , vol.277 , pp. 9637-9640
    • Gow, A.J.1    Chen, Q.2    Hess, D.T.3    Day, B.J.4    Ischiropoulos, H.5    Stamler, J.S.6
  • 21
    • 0021677474 scopus 로고
    • The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms
    • Morgenstern R., Lundqvist G., Andersson G., Balk L., and DePierre J.W. The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms. Biochem. Pharmacol. 33 (1984) 3609-3614
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3609-3614
    • Morgenstern, R.1    Lundqvist, G.2    Andersson, G.3    Balk, L.4    DePierre, J.W.5
  • 23
    • 0037899293 scopus 로고    scopus 로고
    • Compartmentalized nitrosation and nitration in mitochondria
    • Ghafourifar P., and Colton C.A. Compartmentalized nitrosation and nitration in mitochondria. Antioxid. Redox. Signal. 5 (2003) 349-354
    • (2003) Antioxid. Redox. Signal. , vol.5 , pp. 349-354
    • Ghafourifar, P.1    Colton, C.A.2
  • 24
    • 0021104760 scopus 로고
    • Microsomal glutathione transferase. Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition
    • Morgenstern R., and DePierre J.W. Microsomal glutathione transferase. Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition. Eur. J. Biochem. 134 (1983) 591-597
    • (1983) Eur. J. Biochem. , vol.134 , pp. 591-597
    • Morgenstern, R.1    DePierre, J.W.2
  • 26
    • 0020333948 scopus 로고
    • Fractionation of isolated liver cells after disruption with a nitrogen bomb and sonication
    • Autuori F., Brunk U., Peterson E., and Dallner G. Fractionation of isolated liver cells after disruption with a nitrogen bomb and sonication. J. Cell. Sci. 57 (1982) 1-13
    • (1982) J. Cell. Sci. , vol.57 , pp. 1-13
    • Autuori, F.1    Brunk, U.2    Peterson, E.3    Dallner, G.4
  • 27
    • 0035849714 scopus 로고    scopus 로고
    • S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation
    • Lane P., Hao G., and Gross S.S. S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation. Sci. STKE. RE1. (2001)
    • (2001) Sci. STKE. RE1.
    • Lane, P.1    Hao, G.2    Gross, S.S.3
  • 29
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation the prototypic redox-based signaling mechanism
    • Stamler J.S., Lamas S., and Fang F.C. Nitrosylation the prototypic redox-based signaling mechanism. Cell 106 (2001) 675-683
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 30
  • 31
    • 1542373633 scopus 로고    scopus 로고
    • S-nitrosothiols in the blood: roles, amounts, and methods of analysis
    • Stamler J.S. S-nitrosothiols in the blood: roles, amounts, and methods of analysis. Circ. Res. 94 (2004) 414-417
    • (2004) Circ. Res. , vol.94 , pp. 414-417
    • Stamler, J.S.1
  • 32
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • Liu L., Hausladen A., Zeng M., Que L., Heitman J., and Stamler J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490-494
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 35
    • 33646187917 scopus 로고    scopus 로고
    • Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase
    • Imaizumi N., Miyagi S., and Aniya Y. Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase. Life Sci. 78 (2006) 2998-3006
    • (2006) Life Sci. , vol.78 , pp. 2998-3006
    • Imaizumi, N.1    Miyagi, S.2    Aniya, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.