메뉴 건너뛰기




Volumn 90, Issue 6, 2012, Pages 1218-1229

Cross-linking of serine racemase dimer by reactive oxygen species and reactive nitrogen species

Author keywords

Dimerization; Disulfide; Mass spectrometry; Nitric oxide; Oxidation; Peroxynitrite

Indexed keywords

CYSTEINE DERIVATIVE; DIMER; DODECYL SULFATE SODIUM; HYDROGEN PEROXIDE; HYDROXYL RADICAL; LINSIDOMINE; MERCAPTOETHANOL; NITRIC OXIDE; PEROXYNITRITE; RACEMASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; RECOMBINANT ENZYME; SERINE; SERINE RACEMASE; SMALL INTERFERING RNA; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 84862830340     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.22832     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 0346100520 scopus 로고    scopus 로고
    • Peroxynitrite reactivity with amino acids and proteins
    • Alvarez B, Radi R. 2003. Peroxynitrite reactivity with amino acids and proteins. Amino Acids 25: 295-311.
    • (2003) Amino Acids , vol.25 , pp. 295-311
    • Alvarez, B.1    Radi, R.2
  • 2
    • 0042536473 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity
    • Arundine M, Tymianski M. 2003. Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity. Cell Calcium 34: 325-337.
    • (2003) Cell Calcium , vol.34 , pp. 325-337
    • Arundine, M.1    Tymianski, M.2
  • 3
    • 0032812464 scopus 로고    scopus 로고
    • Peroxynitrite scavenging by different antioxidants. Part I: convenient assay
    • Balavoine GG, Geletii YV. 1999. Peroxynitrite scavenging by different antioxidants. Part I: convenient assay. Nitric Oxide 3: 40-54.
    • (1999) Nitric Oxide , vol.3 , pp. 40-54
    • Balavoine, G.G.1    Geletii, Y.V.2
  • 4
    • 24044501617 scopus 로고    scopus 로고
    • An unconventional hypothesis of oxidation in Alzheimer's disease: intersections with excitotoxicity
    • Barger SW. 2004. An unconventional hypothesis of oxidation in Alzheimer's disease: intersections with excitotoxicity. Front Biosci 9: 3286-3295.
    • (2004) Front Biosci , vol.9 , pp. 3286-3295
    • Barger, S.W.1
  • 5
    • 0035146889 scopus 로고    scopus 로고
    • Activation of microglia by secreted amyloid precursor protein evokes release of glutamate by cystine exchange and attenuates synaptic function
    • Barger SW, Basile AS. 2001. Activation of microglia by secreted amyloid precursor protein evokes release of glutamate by cystine exchange and attenuates synaptic function. J Neurochem 76: 846-854.
    • (2001) J Neurochem , vol.76 , pp. 846-854
    • Barger, S.W.1    Basile, A.S.2
  • 6
    • 34248152778 scopus 로고    scopus 로고
    • Glutamate release from activated microglia requires the oxidative burst and lipid peroxidation
    • Barger SW, Goodwin ME, Porter MM, Beggs ML. 2007. Glutamate release from activated microglia requires the oxidative burst and lipid peroxidation. J Neurochem 101: 1205-1213.
    • (2007) J Neurochem , vol.101 , pp. 1205-1213
    • Barger, S.W.1    Goodwin, M.E.2    Porter, M.M.3    Beggs, M.L.4
  • 7
    • 10044235332 scopus 로고    scopus 로고
    • Secreted beta-amyloid precursor protein activates microglia via JNK and p38-MAPK
    • Bodles AM, Barger SW. 2005. Secreted beta-amyloid precursor protein activates microglia via JNK and p38-MAPK. Neurobiol Aging 26: 9-16.
    • (2005) Neurobiol Aging , vol.26 , pp. 9-16
    • Bodles, A.M.1    Barger, S.W.2
  • 9
    • 0035369112 scopus 로고    scopus 로고
    • NMDA receptor subunits: diversity, development and disease
    • Cull-Candy S, Brickley S, Farrant M. 2001. NMDA receptor subunits: diversity, development and disease. Curr Opin Neurobiol 11: 327-335.
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 327-335
    • Cull-Candy, S.1    Brickley, S.2    Farrant, M.3
  • 10
    • 0034601688 scopus 로고    scopus 로고
    • Human serine racemase: molecular cloning, genomic organization and functional analysis
    • De Miranda J, Santoro A, Engelender S, Wolosker H. 2000. Human serine racemase: molecular cloning, genomic organization and functional analysis. Gene 256: 183-188.
    • (2000) Gene , vol.256 , pp. 183-188
    • De Miranda, J.1    Santoro, A.2    Engelender, S.3    Wolosker, H.4
  • 14
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation. An update
    • Halliwell B, Gutteridge JM. 1992. Biologically relevant metal ion-dependent hydroxyl radical generation. An update. FEBS Lett 307: 108-112.
    • (1992) FEBS Lett , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 15
    • 37049135943 scopus 로고
    • The chemistry of pernitrites. Part I. Kinetics of decomposition of pernitrous acid
    • Hughes M, Nicklin H. 1968. The chemistry of pernitrites. Part I. Kinetics of decomposition of pernitrous acid. J Chem Soc A 1968: 450-452.
    • (1968) J Chem Soc A , vol.1968 , pp. 450-452
    • Hughes, M.1    Nicklin, H.2
  • 16
    • 58149373550 scopus 로고    scopus 로고
    • 1-42-induced neurotoxicity is attenuated in serine racemase knock-out mice
    • 1-42-induced neurotoxicity is attenuated in serine racemase knock-out mice. J Neurosci 31: 14486-14491.
    • (2008) J Neurosci , vol.31 , pp. 14486-14491
    • Inoue, R.1    Hashimoto, K.2    Harai, T.3    Mori, H.4
  • 17
    • 33744900653 scopus 로고    scopus 로고
    • Neuron-derived D-serine release provides a novel means to activate N-methyl-D-aspartate receptors
    • Kartvelishvily E, Shleper M, Balan L, Dumin E, Wolosker H. 2006. Neuron-derived D-serine release provides a novel means to activate N-methyl-D-aspartate receptors. J Biol Chem 281: 14151-14162.
    • (2006) J Biol Chem , vol.281 , pp. 14151-14162
    • Kartvelishvily, E.1    Shleper, M.2    Balan, L.3    Dumin, E.4    Wolosker, H.5
  • 19
    • 84859442731 scopus 로고    scopus 로고
    • Contributions of the D-serine pathway to schizophrenia
    • February 2 E-pub ahead of print].
    • Labrie V, Wong AH, Roder JC. 2011. Contributions of the D-serine pathway to schizophrenia. Neuropharmacology [February 2 E-pub ahead of print].
    • (2011) Neuropharmacology
    • Labrie, V.1    Wong, A.H.2    Roder, J.C.3
  • 20
    • 0036179194 scopus 로고    scopus 로고
    • Excitotoxicity: perspectives based on N-methyl-D-aspartate receptor subtypes
    • Lynch DR, Guttmann RP. 2002. Excitotoxicity: perspectives based on N-methyl-D-aspartate receptor subtypes. J Pharmacol Exp Ther 300: 717-723.
    • (2002) J Pharmacol Exp Ther , vol.300 , pp. 717-723
    • Lynch, D.R.1    Guttmann, R.P.2
  • 21
    • 68749102352 scopus 로고    scopus 로고
    • Modification of surfactant protein D by reactive oxygen-nitrogen intermediates is accompanied by loss of aggregating activity, in vitro and in vivo
    • Matalon S, Shrestha K, Kirk M, Waldheuser S, McDonald B, Smith K, Gao Z, Belaaouaj A, Crouch EC. 2009. Modification of surfactant protein D by reactive oxygen-nitrogen intermediates is accompanied by loss of aggregating activity, in vitro and in vivo. FASEB J 23: 1415-1430.
    • (2009) FASEB J , vol.23 , pp. 1415-1430
    • Matalon, S.1    Shrestha, K.2    Kirk, M.3    Waldheuser, S.4    McDonald, B.5    Smith, K.6    Gao, Z.7    Belaaouaj, A.8    Crouch, E.C.9
  • 23
    • 46749118458 scopus 로고    scopus 로고
    • Role of the peroxynitrite-poly(ADP-ribose) polymerase pathway in human disease
    • Pacher P, Szabo C. 2008. Role of the peroxynitrite-poly(ADP-ribose) polymerase pathway in human disease. Am J Pathol 173: 2-13.
    • (2008) Am J Pathol , vol.173 , pp. 2-13
    • Pacher, P.1    Szabo, C.2
  • 24
    • 0000071430 scopus 로고
    • Chemical syntheses with quenched flow reactor. Hydroxy-trihydroborate and peroxynitrite
    • Reed J, Ho H, Jolly W. 1974. Chemical syntheses with quenched flow reactor. Hydroxy-trihydroborate and peroxynitrite. J Am Chem Soc 96: 1248-1249.
    • (1974) J Am Chem Soc , vol.96 , pp. 1248-1249
    • Reed, J.1    Ho, H.2    Jolly, W.3
  • 25
    • 34648825386 scopus 로고    scopus 로고
    • D-serine is a key determinant of glutamate toxicity in amyotrophic lateral sclerosis
    • Sasabe J, Chiba T, Yamada M, Okamoto K, Nishimoto I, Matsuoka M, Aiso S. 2007. D-serine is a key determinant of glutamate toxicity in amyotrophic lateral sclerosis. EMBO J 26: 4149-4159.
    • (2007) EMBO J , vol.26 , pp. 4149-4159
    • Sasabe, J.1    Chiba, T.2    Yamada, M.3    Okamoto, K.4    Nishimoto, I.5    Matsuoka, M.6    Aiso, S.7
  • 26
    • 0028988978 scopus 로고
    • D-serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release
    • Schell MJ, Molliver ME, Snyder SH. 1995. D-serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release. Proc Natl Acad Sci U S A 92: 3948-3952.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3948-3952
    • Schell, M.J.1    Molliver, M.E.2    Snyder, S.H.3
  • 27
    • 0031046980 scopus 로고    scopus 로고
    • D-serine as a neuromodulator: regional and developmental localizations in rat brain glia resemble NMDA receptors
    • Schell MJ, Brady ROJr, Molliver ME, Snyder SH. 1997. D-serine as a neuromodulator: regional and developmental localizations in rat brain glia resemble NMDA receptors. J Neurosci 17: 1604-1615.
    • (1997) J Neurosci , vol.17 , pp. 1604-1615
    • Schell, M.J.1    Brady Jr, R.O.2    Molliver, M.E.3    Snyder, S.H.4
  • 29
    • 0035039021 scopus 로고    scopus 로고
    • Protein oxidation in aging and age-related diseases
    • Stadtman ER. 2001. Protein oxidation in aging and age-related diseases. Ann N Y Acad Sci 928: 22-38.
    • (2001) Ann N Y Acad Sci , vol.928 , pp. 22-38
    • Stadtman, E.R.1
  • 30
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. 2006. Protein oxidation and aging. Free Radic Res 40: 1250-1258.
    • (2006) Free Radic Res , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 32
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF. 2003. Mitochondrial formation of reactive oxygen species. J Physiol 15: 335-344.
    • (2003) J Physiol , vol.15 , pp. 335-344
    • Turrens, J.F.1
  • 33
    • 84862790295 scopus 로고    scopus 로고
    • Roles of quaternary structure and cysteine residues in the activity of human serine racemase. Submitted for publication.
    • Wang W, Barger SW. 2011. Roles of quaternary structure and cysteine residues in the activity of human serine racemase. Submitted for publication.
    • (2011)
    • Wang, W.1    Barger, S.W.2
  • 34
    • 33644560634 scopus 로고    scopus 로고
    • Immunocytochemical analysis of D-serine distribution in the mammalian brain reveals novel anatomical compartmentalizations in glia and neurons
    • Williams SM, Diaz CM, Macnab LT, Sullivan RK, Pow DV. 2006. Immunocytochemical analysis of D-serine distribution in the mammalian brain reveals novel anatomical compartmentalizations in glia and neurons. Glia 53: 401-411.
    • (2006) Glia , vol.53 , pp. 401-411
    • Williams, S.M.1    Diaz, C.M.2    Macnab, L.T.3    Sullivan, R.K.4    Pow, D.V.5
  • 35
    • 0033539510 scopus 로고    scopus 로고
    • Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission
    • Wolosker H, Blackshaw S, Snyder SH. 1999a. Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission. Proc Natl Acad Sci U S A 96: 13409-13414.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13409-13414
    • Wolosker, H.1    Blackshaw, S.2    Snyder, S.H.3
  • 37
    • 14944354601 scopus 로고    scopus 로고
    • Serine racemase induction by inflammatory stimuli is dependent on AP-1
    • Wu S-Z, Barger SW. 2004. Serine racemase induction by inflammatory stimuli is dependent on AP-1. Ann N Y Acad Sci 1035: 133-146.
    • (2004) Ann N Y Acad Sci , vol.1035 , pp. 133-146
    • Wu, S.-Z.1    Barger, S.W.2
  • 39
    • 34347372591 scopus 로고    scopus 로고
    • Induction of serine racemase expression and D-serine release from microglia by secreted amyloid precursor protein (sAPP)
    • Wu S, Basile AS, Barger SW. 2007. Induction of serine racemase expression and D-serine release from microglia by secreted amyloid precursor protein (sAPP). Curr Alzheimer Res 4: 243-251.
    • (2007) Curr Alzheimer Res , vol.4 , pp. 243-251
    • Wu, S.1    Basile, A.S.2    Barger, S.W.3
  • 41
    • 0037929802 scopus 로고    scopus 로고
    • Bicarbonate-dependent peroxidase activity of human Cu,Zn-superoxide dismutase induces covalent aggregation of protein: intermediacy of tryptophan-derived oxidation products
    • Zhang H, Andrekopoulos C, Joseph J, Chandran K, Karoui H, Crow JP, Kalyanaraman B. 2003. Bicarbonate-dependent peroxidase activity of human Cu, Zn-superoxide dismutase induces covalent aggregation of protein: intermediacy of tryptophan-derived oxidation products. J Biol Chem 278: 24078-24089.
    • (2003) J Biol Chem , vol.278 , pp. 24078-24089
    • Zhang, H.1    Andrekopoulos, C.2    Joseph, J.3    Chandran, K.4    Karoui, H.5    Crow, J.P.6    Kalyanaraman, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.