메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages

Redox-sensitivity and site-specificity of S- and N- denitrosation in proteins

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; CYSTEINE; GLUTATHIONE; HUMAN SERUM ALBUMIN; NITRIC OXIDE; NITROSAMINE; OXYGEN; S NITROSOGLUTATHIONE; S NITROSOTHIOL; SUPEROXIDE; SUPEROXIDE DISMUTASE; TRYPTOPHAN; ANTIOXIDANT; N ACETYL N' NITROSOTRYPTOPHAN; N-ACETYL-N'-NITROSOTRYPTOPHAN; NITROGEN; PROTEIN; SERUM ALBUMIN;

EID: 78650988987     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0014400     Document Type: Article
Times cited : (11)

References (45)
  • 1
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC (2001) Nitrosylation: the prototypic redox-based signaling mechanism. Cell 106: 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 3
    • 0031037180 scopus 로고    scopus 로고
    • Suppression of apoptosis by nitric oxide via inhibition of interleukin-1b-converting enzyme (ice)-like and cysteine protease protein (cpp)-32-like proteases
    • Dimmeler S, Haendeler J, Nehls M, Zeiher AM (1997) Suppression of apoptosis by nitric oxide via inhibition of interleukin-1b-converting enzyme (ice)-like and cysteine protease protein (cpp)-32-like proteases. J Exp Med 185: 601-607.
    • (1997) J Exp Med , vol.185 , pp. 601-607
    • Dimmeler, S.1    Haendeler, J.2    Nehls, M.3    Zeiher, A.M.4
  • 4
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • Sun J, Xin C, Eu JP, Stamler JS, Meissner G (2001) Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc Natl Acad Sci USA 98: 11158-11162.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 5
    • 0037443130 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols
    • Li S, Whorton RA (2003) Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols. Arch Biochem Biophys 410: 269-279.
    • (2003) Arch Biochem Biophys , vol.410 , pp. 269-279
    • Li, S.1    Whorton, R.A.2
  • 7
    • 84961004853 scopus 로고
    • The production of malignant primary hepatic tumours in the rat by feeding dimethylnitrosamine
    • Magee PN, Barnes JM (1956) The production of malignant primary hepatic tumours in the rat by feeding dimethylnitrosamine. Br J Cancer.
    • (1956) Br J Cancer
    • Magee, P.N.1    Barnes, J.M.2
  • 8
    • 0029893843 scopus 로고    scopus 로고
    • Nitrosation of tryptophan residue(s) in serum albumin and model dipeptides. Biochemical characterization and bioactivity
    • Zhang YY, Xu AM, Nomen M, Walsh M, Keaney JF, Jr., et al. (1996) Nitrosation of tryptophan residue(s) in serum albumin and model dipeptides. Biochemical characterization and bioactivity. J Biol Chem 271: 14271-14279.
    • (1996) J Biol Chem , vol.271 , pp. 14271-14279
    • Zhang, Y.Y.1    Xu, A.M.2    Nomen, M.3    Walsh, M.4    Keaney Jr., J.F.5
  • 9
    • 0029956121 scopus 로고    scopus 로고
    • Polynitrosylated proteins: Characterization, bioactivity, and functional consequences
    • Simon DI, Mullins ME, Jia L, Gaston B, Singel DJ, et al. (1996) Polynitrosylated proteins: characterization, bioactivity, and functional consequences. Proc Natl Acad Sci U S A 93: 4736-4741.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4736-4741
    • Simon, D.I.1    Mullins, M.E.2    Jia, L.3    Gaston, B.4    Singel, D.J.5
  • 10
    • 1642447134 scopus 로고    scopus 로고
    • Cellular targets and mechanisms of nitros(yl)ation: An insight into their nature and kinetics in vivo
    • Bryan NS, Rassaf T, Maloney RE, Rodriguez CM, Saijo F, et al. (2004) Cellular targets and mechanisms of nitros(yl)ation: An insight into their nature and kinetics in vivo. Proc Natl Acad Sci U S A 101: 4308-4313.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4308-4313
    • Bryan, N.S.1    Rassaf, T.2    Maloney, R.E.3    Rodriguez, C.M.4    Saijo, F.5
  • 11
    • 0036890053 scopus 로고    scopus 로고
    • Concomitant presence of Nnitroso and S-nitroso proteins in human plasma
    • Rassaf T, Bryan NS, Kelm M, Feelisch M (2002) Concomitant presence of Nnitroso and S-nitroso proteins in human plasma. Free Radic Biol Med 33: 1590-1596.
    • (2002) Free Radic Biol Med , vol.33 , pp. 1590-1596
    • Rassaf, T.1    Bryan, N.S.2    Kelm, M.3    Feelisch, M.4
  • 12
    • 0034620508 scopus 로고    scopus 로고
    • An apoptotic model for nitrosative stress
    • Eu JP, Liu L, Zeng M, Stamler JS (2000) An apoptotic model for nitrosative stress. Biochemistry 39: 1040-1047.
    • (2000) Biochemistry , vol.39 , pp. 1040-1047
    • Eu, J.P.1    Liu, L.2    Zeng, M.3    Stamler, J.S.4
  • 13
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • Benhar M, Forrester MT, Stamler JS (2009) Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat Rev Mol Cell Biol 10: 721-732.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 14
    • 0004206788 scopus 로고
    • Cambridge: Press Syndicate of the University of Cambridge
    • Williams DLH (1988) Nitrosation. Cambridge: Press Syndicate of the University of Cambridge.
    • (1988) Nitrosation
    • Williams, D.L.H.1
  • 15
    • 34347256733 scopus 로고    scopus 로고
    • Dependence of N-nitrosodimethylamine photodecomposition on the irradiation wavelength: Excitation to the s(2) state as a doorway to the dimethylamine radical ground-state chemistry
    • Pelaez D, Arenas JF, Otero JC, Soto J (2007) Dependence of N-nitrosodimethylamine photodecomposition on the irradiation wavelength: excitation to the s(2) state as a doorway to the dimethylamine radical ground-state chemistry. J Org Chem 72: 4741-4749.
    • (2007) J Org Chem , vol.72 , pp. 4741-4749
    • Pelaez, D.1    Arenas, J.F.2    Otero, J.C.3    Soto, J.4
  • 16
    • 37049100140 scopus 로고
    • Denitrosation of N-acetyl-N-nitrosotryptophan in acid solution
    • Meyer TA, Williams DLH (1982) Denitrosation of N-acetyl-N-nitrosotryptophan in acid solution. J Chem Soc, Perkin Trans 2: 1383-1387.
    • (1982) J Chem Soc, Perkin Trans , vol.2 , pp. 1383-1387
    • Meyer, T.A.1    Williams, D.L.H.2
  • 17
    • 36749025053 scopus 로고    scopus 로고
    • Generation, basic chemistry, and detection of Nnitrosotryptophan derivatives
    • Kirsch M, Korth HG (2007) Generation, basic chemistry, and detection of Nnitrosotryptophan derivatives. Org Biomol Chem 5: 3889-3894.
    • (2007) Org Biomol Chem , vol.5 , pp. 3889-3894
    • Kirsch, M.1    Korth, H.G.2
  • 18
    • 8544259626 scopus 로고    scopus 로고
    • Formation of S-nitrosothiols from regiospecific reaction of thiols with N-nitrosotryptophan derivatives
    • Sonnenschein K, de GH, Kirsch M (2004) Formation of S-nitrosothiols from regiospecific reaction of thiols with N-nitrosotryptophan derivatives. J Biol Chem 279: 45433-45440.
    • (2004) J Biol Chem , vol.279 , pp. 45433-45440
    • Sonnenschein, K.1    De, G.H.2    Kirsch, M.3
  • 19
    • 22244479276 scopus 로고    scopus 로고
    • Mechanisms of NO release by N1-nitrosomelatonin: Nucleophilic attack versus reducing pathways
    • De Biase PM, Turjanski AG, Estrin DA, Doctorovich F (2005) Mechanisms of NO release by N1-nitrosomelatonin: nucleophilic attack versus reducing pathways. J Org Chem 70: 5790-5798.
    • (2005) J Org Chem , vol.70 , pp. 5790-5798
    • de Biase, P.M.1    Turjanski, A.G.2    Estrin, D.A.3    Doctorovich, F.4
  • 20
    • 0038823593 scopus 로고    scopus 로고
    • Regiospecific Nitrosation of N-terminalblocked Tryptophan Derivatives by N2O3 at Physiological pH
    • Kirsch M, Fuchs A, de Groot H (2003) Regiospecific Nitrosation of N-terminalblocked Tryptophan Derivatives by N2O3 at Physiological pH. J Biol Chem 278: 11931-11936.
    • (2003) J Biol Chem , vol.278 , pp. 11931-11936
    • Kirsch, M.1    Fuchs, A.2    de Groot, H.3
  • 22
    • 0345306295 scopus 로고    scopus 로고
    • Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein
    • Romeo AA, Capobianco JA, English AM (2003) Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein. J Am Chem Soc 125: 14370-14378.
    • (2003) J Am Chem Soc , vol.125 , pp. 14370-14378
    • Romeo, A.A.1    Capobianco, J.A.2    English, A.M.3
  • 23
    • 0036846736 scopus 로고    scopus 로고
    • Concomitant S-, N-, and heme-nitros(yl)ation in biological tissues and fluids: Implications for the fate of NO in vivo
    • Feelisch M, Rassaf T, Mnaimneh S, Singh N, Bryan NS, et al. (2002) Concomitant S-, N-, and heme-nitros(yl)ation in biological tissues and fluids: implications for the fate of NO in vivo. FASEB J 16: 1775-1785.
    • (2002) FASEB J , vol.16 , pp. 1775-1785
    • Feelisch, M.1    Rassaf, T.2    Mnaimneh, S.3    Singh, N.4    Bryan, N.S.5
  • 24
    • 0036162361 scopus 로고    scopus 로고
    • Site-directed mutagenesis studies of human serum albumin define tryptophan at amino acid position 214 as the principal site for nitrosation
    • Harohalli K, Petersen CE, Ha CE, Feix JB, Bhagavan NV (2002) Site-directed mutagenesis studies of human serum albumin define tryptophan at amino acid position 214 as the principal site for nitrosation. J Biomed Sci 9: 47-58.
    • (2002) J Biomed Sci , vol.9 , pp. 47-58
    • Harohalli, K.1    Petersen, C.E.2    Ha, C.E.3    Feix, J.B.4    Bhagavan, N.V.5
  • 25
    • 2542516981 scopus 로고    scopus 로고
    • The mechanism of transmembrane S-nitrosothiol transport
    • Zhang Y, Hogg N (2004) The mechanism of transmembrane S-nitrosothiol transport. Proc Natl Acad Sci USA 101: 7891-7896.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7891-7896
    • Zhang, Y.1    Hogg, N.2
  • 26
    • 0029927487 scopus 로고    scopus 로고
    • The role of glutathione in the transport and catabolism of nitric oxide
    • Hogg N, Singh RJ, Kalyanaraman B (1996) The role of glutathione in the transport and catabolism of nitric oxide. FEBS Lett 382: 223-228.
    • (1996) FEBS Lett , vol.382 , pp. 223-228
    • Hogg, N.1    Singh, R.J.2    Kalyanaraman, B.3
  • 28
    • 0029002385 scopus 로고
    • Kinetic factors that control the fate of thiyl radicals in cells
    • Wardman P, von Sonntag C (1995) Kinetic factors that control the fate of thiyl radicals in cells. Methods Enzymol 251: 31-45.
    • (1995) Methods Enzymol , vol.251 , pp. 31-45
    • Wardman, P.1    von Sonntag, C.2
  • 29
    • 43849090222 scopus 로고    scopus 로고
    • Thiyl radicals react with nitric oxide to form S-nitrosothiols with rate constants near the diffusion-controlled limit
    • Madej E, Folkes LK, Wardman P, Czapski G, Goldstein S (2008) Thiyl radicals react with nitric oxide to form S-nitrosothiols with rate constants near the diffusion-controlled limit. Free Radic Biol Med 44: 2013-2018.
    • (2008) Free Radic Biol Med , vol.44 , pp. 2013-2018
    • Madej, E.1    Folkes, L.K.2    Wardman, P.3    Czapski, G.4    Goldstein, S.5
  • 30
    • 33845201164 scopus 로고    scopus 로고
    • On the mechanism of the ascorbic acid-induced release of nitric oxide from N-nitrosated tryptophan derivatives: Scavenging of NO by ascorbyl radicals
    • Kytzia A, Korth HG, Sustmann R, de Groot H, Kirsch M (2006) On the mechanism of the ascorbic acid-induced release of nitric oxide from N-nitrosated tryptophan derivatives: scavenging of NO by ascorbyl radicals. Chemistry 12: 8786-8797.
    • (2006) Chemistry , vol.12 , pp. 8786-8797
    • Kytzia, A.1    Korth, H.G.2    Sustmann, R.3    de Groot, H.4    Kirsch, M.5
  • 31
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter DC, Ho JX (1994) Structure of serum albumin. Adv Protein Chem 45: 153-203.
    • (1994) Adv Protein Chem , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 32
    • 0034610268 scopus 로고    scopus 로고
    • An autocatalytic mechanism of protein nitrosylation
    • Nedospasov A, Rafikov R, Nudler E (2000) An autocatalytic mechanism of protein nitrosylation. Proc Natl Acad Sci USA 97: 13543-13548.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13543-13548
    • Nedospasov, A.1    Rafikov, R.2    Nudler, E.3
  • 33
    • 40949098241 scopus 로고    scopus 로고
    • Copper dependence of the biotin switch assay: Modified assay for measuring cellular and blood nitrosated proteins
    • Wang X, Kettenhofen NJ, Shiva S, Hogg N, Gladwin MT (2008) Copper dependence of the biotin switch assay: Modified assay for measuring cellular and blood nitrosated proteins. Free Radic Biol Med.
    • (2008) Free Radic Biol Med
    • Wang, X.1    Kettenhofen, N.J.2    Shiva, S.3    Hogg, N.4    Gladwin, M.T.5
  • 34
    • 36048931836 scopus 로고    scopus 로고
    • Effects of endogenous ligands on the biological role of human serum albumin in S-nitrosylation
    • Ishima Y, Akaike T, Kragh-Hansen U, Hiroyama S, Sawa T, et al. (2007) Effects of endogenous ligands on the biological role of human serum albumin in S-nitrosylation. Biochem Biophys Res Commun 364: 790-795.
    • (2007) Biochem Biophys Res Commun , vol.364 , pp. 790-795
    • Ishima, Y.1    Akaike, T.2    Kragh-Hansen, U.3    Hiroyama, S.4    Sawa, T.5
  • 35
    • 58049213353 scopus 로고    scopus 로고
    • S-nitrosylated human serum albumin-mediated cytoprotective activity is enhanced by fatty acid binding
    • Ishima Y, Akaike T, Kragh-Hansen U, Hiroyama S, Sawa T, Suenaga A, et al. (2008) S-nitrosylated human serum albumin-mediated cytoprotective activity is enhanced by fatty acid binding. J Biol Chem 283: 34966-34975.
    • (2008) J Biol Chem , vol.283 , pp. 34966-34975
    • Ishima, Y.1    Akaike, T.2    Kragh-Hansen, U.3    Hiroyama, S.4    Sawa, T.5    Suenaga, A.6
  • 36
    • 14044275170 scopus 로고    scopus 로고
    • Nitrolinoleic acid: An endogenous peroxisome proliferator-activated receptor c ligand
    • Schopfer FJ, Lin Y, Baker PRS, Cui T, Garcia-Barrio M, et al. (2005) Nitrolinoleic acid: An endogenous peroxisome proliferator-activated receptor c ligand. Proc Natl Acad Sci USA 102: 2340-2345.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2340-2345
    • Schopfer, F.J.1    Lin, Y.2    Baker, P.R.S.3    Cui, T.4    Garcia-Barrio, M.5
  • 37
    • 0036877403 scopus 로고    scopus 로고
    • Structural features of proteins responsible for resistance of tryptophan residues to nitrosylation
    • Suntsova TP, Beda NV, Nedospasov AA (2002) Structural features of proteins responsible for resistance of tryptophan residues to nitrosylation. IUBMB Life 54: 281-292.
    • (2002) IUBMB Life , vol.54 , pp. 281-292
    • Suntsova, T.P.1    Beda, N.V.2    Nedospasov, A.A.3
  • 38
    • 0029783551 scopus 로고    scopus 로고
    • Mutations in a specific human serum albumin thyroxine binding site define the structural basis of familial dysalbuminemic hyperthyroxinemia
    • Petersen CE, Ha CE, Jameson DM, Bhagavan NV (1996) Mutations in a specific human serum albumin thyroxine binding site define the structural basis of familial dysalbuminemic hyperthyroxinemia. J Biol Chem 271: 19110-19117.
    • (1996) J Biol Chem , vol.271 , pp. 19110-19117
    • Petersen, C.E.1    Ha, C.E.2    Jameson, D.M.3    Bhagavan, N.V.4
  • 39
    • 0030945733 scopus 로고    scopus 로고
    • Mutagenesis studies of thyroxine binding to human serum albumin define an important structural characteristic of subdomain 2A
    • Petersen CE, Ha CE, Harohalli K, Park D, Bhagavan NV (1997) Mutagenesis studies of thyroxine binding to human serum albumin define an important structural characteristic of subdomain 2A. Biochemistry 36: 7012-7017.
    • (1997) Biochemistry , vol.36 , pp. 7012-7017
    • Petersen, C.E.1    Ha, C.E.2    Harohalli, K.3    Park, D.4    Bhagavan, N.V.5
  • 40
    • 0032878898 scopus 로고    scopus 로고
    • Structural investigations of a new familial dysalbuminemic hyperthyroxinemia genotype
    • Petersen CE, Ha CE, Harohalli K, Park DS, Feix JB, et al. (1999) Structural investigations of a new familial dysalbuminemic hyperthyroxinemia genotype. Clin Chem 45: 1248-1254.
    • (1999) Clin Chem , vol.45 , pp. 1248-1254
    • Petersen, C.E.1    Ha, C.E.2    Harohalli, K.3    Park, D.S.4    Feix, J.B.5
  • 42
    • 0035957839 scopus 로고    scopus 로고
    • Artifactual-free analysis of Snitrosoglutathione and S-nitrosglutathione by neutral-pH, anion-pairing, highperformance liquid chromatography
    • Tsikas D, Denker K, Frölich JC (2001) Artifactual-free analysis of Snitrosoglutathione and S-nitrosglutathione by neutral-pH, anion-pairing, highperformance liquid chromatography. J Chromatogr A 915: 107-116.
    • (2001) J Chromatogr A , vol.915 , pp. 107-116
    • Tsikas, D.1    Denker, K.2    Frölich, J.C.3
  • 44
    • 0038182543 scopus 로고    scopus 로고
    • Oxidation and Nitrosation of Thiols at Low Micromolar Exposure to Nitric Oxide. EVIDENCE FOR A FREE RADICAL MECHANISM
    • Jourd'heuil D, Jourd'heuil FL, Feelisch M (2003) Oxidation and Nitrosation of Thiols at Low Micromolar Exposure to Nitric Oxide. EVIDENCE FOR A FREE RADICAL MECHANISM. J Biol Chem 278: 15720-15726.
    • (2003) J Biol Chem , vol.278 , pp. 15720-15726
    • Jourd'heuil, D.1    Jourd'heuil, F.L.2    Feelisch, M.3
  • 45
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures
    • Bhattacharya AA, Curry S, Franks NP (2000) Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem 275: 38731-38738.
    • (2000) J Biol Chem , vol.275 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.