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Volumn 410, Issue 3, 2011, Pages 555-562

SUMO1 attenuates stress-induced ROS generation by inhibiting NADPH oxidase 2

Author keywords

Heat shock; NADPH oxidase complex (NOX); Reactive oxygen species (ROS); SUMO1

Indexed keywords

REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SUMO 1 PROTEIN;

EID: 79960042724     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.06.025     Document Type: Article
Times cited : (27)

References (24)
  • 1
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R., Delphin C., Guan T., Gerace L., Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 1997, 88:97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 2
    • 0030588674 scopus 로고    scopus 로고
    • Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin
    • Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F., Chang H.M., Yeh E.T. Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin. J. Immunol. 1996, 157:4277-4281.
    • (1996) J. Immunol. , vol.157 , pp. 4277-4281
    • Okura, T.1    Gong, L.2    Kamitani, T.3    Wada, T.4    Okura, I.5    Wei, C.F.6    Chang, H.M.7    Yeh, E.T.8
  • 3
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy M.N., Howe K., Etkin L.D., Solomon E., Freemont P.S. PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 1996, 13:971-982.
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 4
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis M.J., Coutavas E., Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 1996, 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 7
    • 0033826520 scopus 로고    scopus 로고
    • Role for mitochondrial oxidants as regulators of cellular metabolism
    • Nemoto S., Takeda K., Yu Z.X., Ferrans V.J., Finkel T. Role for mitochondrial oxidants as regulators of cellular metabolism. Mol. Cell. Biol. 2000, 20:7311-7318.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7311-7318
    • Nemoto, S.1    Takeda, K.2    Yu, Z.X.3    Ferrans, V.J.4    Finkel, T.5
  • 8
    • 0038757584 scopus 로고    scopus 로고
    • Protein kinase B activation by reactive oxygen species is independent of tyrosine kinase receptor phosphorylation and requires SRC activity
    • Esposito F., Chirico G., Montesano Gesualdi N., Posadas I., Ammendola R., Russo T., Cirino G., Cimino F. Protein kinase B activation by reactive oxygen species is independent of tyrosine kinase receptor phosphorylation and requires SRC activity. J. Biol. Chem. 2003, 278:20828-20834.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20828-20834
    • Esposito, F.1    Chirico, G.2    Montesano Gesualdi, N.3    Posadas, I.4    Ammendola, R.5    Russo, T.6    Cirino, G.7    Cimino, F.8
  • 9
    • 33745728157 scopus 로고    scopus 로고
    • Hydrogen peroxide produced by angiopoietin-1 mediates angiogenesis
    • Kim Y.M., Kim K.E., Koh G.Y., Ho Y.S., Lee K.J. Hydrogen peroxide produced by angiopoietin-1 mediates angiogenesis. Cancer Res. 2006, 66:6167-6174.
    • (2006) Cancer Res. , vol.66 , pp. 6167-6174
    • Kim, Y.M.1    Kim, K.E.2    Koh, G.Y.3    Ho, Y.S.4    Lee, K.J.5
  • 10
    • 0037189477 scopus 로고    scopus 로고
    • Proteomic analysis of protein phosphorylations in heat shock response and thermotolerance
    • Kim H.J., Song E.J., Lee K.J. Proteomic analysis of protein phosphorylations in heat shock response and thermotolerance. J. Biol. Chem. 2002, 277:23193-23207.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23193-23207
    • Kim, H.J.1    Song, E.J.2    Lee, K.J.3
  • 12
    • 1942474634 scopus 로고    scopus 로고
    • Glucuronic acid is a novel inducer of heat shock response
    • Kim Y.M., Kim H.J., Song E.J., Lee K.J. Glucuronic acid is a novel inducer of heat shock response. Mol. Cell. Biochem. 2004, 259:23-33.
    • (2004) Mol. Cell. Biochem. , vol.259 , pp. 23-33
    • Kim, Y.M.1    Kim, H.J.2    Song, E.J.3    Lee, K.J.4
  • 13
    • 17044394700 scopus 로고    scopus 로고
    • NADPH oxidase mediates interleukin-6 expression in cerulein-stimulated pancreatic acinar cells
    • Yu J.H., Lim J.W., Kim H., Kim K.H. NADPH oxidase mediates interleukin-6 expression in cerulein-stimulated pancreatic acinar cells. Int. J. Biochem. Cell Biol. 2005, 37:1458-1469.
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 1458-1469
    • Yu, J.H.1    Lim, J.W.2    Kim, H.3    Kim, K.H.4
  • 14
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson G.L., Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 2002, 298:1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 15
    • 33845996199 scopus 로고    scopus 로고
    • Link between mitochondria and NADPH oxidase 1 isozyme for the sustained production of reactive oxygen species and cell death
    • Lee S.B., Bae I.H., Bae Y.S., Um H.D. Link between mitochondria and NADPH oxidase 1 isozyme for the sustained production of reactive oxygen species and cell death. J. Biol. Chem. 2006, 281:36228-36235.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36228-36235
    • Lee, S.B.1    Bae, I.H.2    Bae, Y.S.3    Um, H.D.4
  • 16
    • 38049173243 scopus 로고    scopus 로고
    • Mechanism of angiotensin II-induced superoxide production in cells reconstituted with angiotensin type 1 receptor and the components of NADPH oxidase
    • Choi H., Leto T.L., Hunyady L., Catt K.J., Bae Y.S., Rhee S.G. Mechanism of angiotensin II-induced superoxide production in cells reconstituted with angiotensin type 1 receptor and the components of NADPH oxidase. J. Biol. Chem. 2008, 283:255-267.
    • (2008) J. Biol. Chem. , vol.283 , pp. 255-267
    • Choi, H.1    Leto, T.L.2    Hunyady, L.3    Catt, K.J.4    Bae, Y.S.5    Rhee, S.G.6
  • 17
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • Chen K., Kirber M.T., Xiao H., Yang Y., Keaney J.F. Regulation of ROS signal transduction by NADPH oxidase 4 localization. J. Cell Biol. 2008, 181:1129-1139.
    • (2008) J. Cell Biol. , vol.181 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney, J.F.5
  • 18
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5
    • Cheng G., Cao Z., Xu X., van Meir E.G., Lambeth J.D. Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 2001, 269:131-140.
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    van Meir, E.G.4    Lambeth, J.D.5
  • 19
    • 0031941373 scopus 로고    scopus 로고
    • Validation of lucigenin (bis-N-methylacridinium) as a chemilumigenic probe for detecting superoxide anion radical production by enzymatic and cellular systems
    • Li Y., Zhu H., Kuppusamy P., Roubaud V., Zweier J.L., Trush M.A. Validation of lucigenin (bis-N-methylacridinium) as a chemilumigenic probe for detecting superoxide anion radical production by enzymatic and cellular systems. J. Biol. Chem. 1998, 273:2015-2023.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2015-2023
    • Li, Y.1    Zhu, H.2    Kuppusamy, P.3    Roubaud, V.4    Zweier, J.L.5    Trush, M.A.6
  • 20
    • 0028365310 scopus 로고
    • Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells
    • Griendling K.K., Minieri C.A., Ollerenshaw J.D., Alexander R.W. Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ. Res. 1994, 74:1141-1148.
    • (1994) Circ. Res. , vol.74 , pp. 1141-1148
    • Griendling, K.K.1    Minieri, C.A.2    Ollerenshaw, J.D.3    Alexander, R.W.4
  • 21
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection
    • Morimoto R.I., Santoro M.G. Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nat. Biotechnol. 1998, 16:833-838.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 22
    • 36349022018 scopus 로고    scopus 로고
    • Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction
    • Martin S., Wilkinson K.A., Nishimune A., Henley J.M. Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction. Nat. Rev. Neurosci. 2007, 8:948-959.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 948-959
    • Martin, S.1    Wilkinson, K.A.2    Nishimune, A.3    Henley, J.M.4
  • 23
    • 17044428567 scopus 로고    scopus 로고
    • Sumoylation silences the plasma membrane leak K+ channel K2P1
    • Rajan S., Plant L.D., Rabin M.L., Butler M.H., Goldstein S.A. Sumoylation silences the plasma membrane leak K+ channel K2P1. Cell 2005, 121:37-47.
    • (2005) Cell , vol.121 , pp. 37-47
    • Rajan, S.1    Plant, L.D.2    Rabin, M.L.3    Butler, M.H.4    Goldstein, S.A.5
  • 24
    • 34249046463 scopus 로고    scopus 로고
    • SUMOylation regulates kainate-receptor-mediated synaptic transmission
    • Martin S., Nishimune A., Mellor J.R., Henley J.M. SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature 2007, 447:321-325.
    • (2007) Nature , vol.447 , pp. 321-325
    • Martin, S.1    Nishimune, A.2    Mellor, J.R.3    Henley, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.