메뉴 건너뛰기




Volumn 24, Issue 4, 2016, Pages 582-592

Suppressors of Superoxide-H2O2 Production at Site IQ of Mitochondrial Complex I Protect against Stem Cell Hyperplasia and Ischemia-Reperfusion Injury

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; ANTIOXIDANT; CASPASE; HYDROGEN PEROXIDE; PROTECTIVE AGENT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE; SUPEROXIDE DISMUTASE; SUPPRESSORS OF SITE IQ ELECTRON LEAK; UNCLASSIFIED DRUG; CASPASE 3; CASPASE 7; SUPEROXIDE; TUNICAMYCIN;

EID: 84992390935     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2016.08.012     Document Type: Article
Times cited : (168)

References (35)
  • 1
    • 82355183887 scopus 로고    scopus 로고
    • Measurement of proton leak and electron leak in isolated mitochondria
    • Affourtit, C., Quinlan, C.L., Brand, M.D., Measurement of proton leak and electron leak in isolated mitochondria. Methods Mol. Biol. 810 (2012), 165–182.
    • (2012) Methods Mol. Biol. , vol.810 , pp. 165-182
    • Affourtit, C.1    Quinlan, C.L.2    Brand, M.D.3
  • 2
    • 79955133184 scopus 로고    scopus 로고
    • EGF signaling regulates the proliferation of intestinal stem cells in Drosophila
    • Biteau, B., Jasper, H., EGF signaling regulates the proliferation of intestinal stem cells in Drosophila. Development 138 (2011), 1045–1055.
    • (2011) Development , vol.138 , pp. 1045-1055
    • Biteau, B.1    Jasper, H.2
  • 3
    • 52949093944 scopus 로고    scopus 로고
    • JNK activity in somatic stem cells causes loss of tissue homeostasis in the aging Drosophila gut
    • Biteau, B., Hochmuth, C.E., Jasper, H., JNK activity in somatic stem cells causes loss of tissue homeostasis in the aging Drosophila gut. Cell Stem Cell 3 (2008), 442–455.
    • (2008) Cell Stem Cell , vol.3 , pp. 442-455
    • Biteau, B.1    Hochmuth, C.E.2    Jasper, H.3
  • 4
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • Brand, M.D., The sites and topology of mitochondrial superoxide production. Exp. Gerontol. 45 (2010), 466–472.
    • (2010) Exp. Gerontol. , vol.45 , pp. 466-472
    • Brand, M.D.1
  • 5
    • 84964890374 scopus 로고    scopus 로고
    • Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling
    • Published online April 13, 2016
    • Brand, M.D., Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling. Free Radic. Biol. Med., 2016, 10.1016/j.freeradbiomed.2016.04.001 Published online April 13, 2016.
    • (2016) Free Radic. Biol. Med.
    • Brand, M.D.1
  • 6
    • 79955544880 scopus 로고    scopus 로고
    • Mitochondrial c-Jun N-terminal kinase (JNK) signaling initiates physiological changes resulting in amplification of reactive oxygen species generation
    • Chambers, J.W., LoGrasso, P.V., Mitochondrial c-Jun N-terminal kinase (JNK) signaling initiates physiological changes resulting in amplification of reactive oxygen species generation. J. Biol. Chem. 286 (2011), 16052–16062.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16052-16062
    • Chambers, J.W.1    LoGrasso, P.V.2
  • 11
    • 84920520304 scopus 로고    scopus 로고
    • Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise
    • Goncalves, R.L.S., Quinlan, C.L., Perevoshchikova, I.V., Hey-Mogensen, M., Brand, M.D., Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise. J. Biol. Chem. 290 (2015), 209–227.
    • (2015) J. Biol. Chem. , vol.290 , pp. 209-227
    • Goncalves, R.L.S.1    Quinlan, C.L.2    Perevoshchikova, I.V.3    Hey-Mogensen, M.4    Brand, M.D.5
  • 12
    • 84952342515 scopus 로고    scopus 로고
    • Production of superoxide/hydrogen peroxide by the mitochondrial 2-oxoadipate dehydrogenase complex
    • Goncalves, R.L.S., Bunik, V.I., Brand, M.D., Production of superoxide/hydrogen peroxide by the mitochondrial 2-oxoadipate dehydrogenase complex. Free Radic. Biol. Med. 91 (2016), 247–255.
    • (2016) Free Radic. Biol. Med. , vol.91 , pp. 247-255
    • Goncalves, R.L.S.1    Bunik, V.I.2    Brand, M.D.3
  • 14
    • 0942298545 scopus 로고    scopus 로고
    • Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice
    • Hinerfeld, D., Traini, M.D., Weinberger, R.P., Cochran, B., Doctrow, S.R., Harry, J., Melov, S., Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice. J. Neurochem. 88 (2004), 657–667.
    • (2004) J. Neurochem. , vol.88 , pp. 657-667
    • Hinerfeld, D.1    Traini, M.D.2    Weinberger, R.P.3    Cochran, B.4    Doctrow, S.R.5    Harry, J.6    Melov, S.7
  • 15
    • 79551610653 scopus 로고    scopus 로고
    • Redox regulation by Keap1 and Nrf2 controls intestinal stem cell proliferation in Drosophila
    • Hochmuth, C.E., Biteau, B., Bohmann, D., Jasper, H., Redox regulation by Keap1 and Nrf2 controls intestinal stem cell proliferation in Drosophila. Cell Stem Cell 8 (2011), 188–199.
    • (2011) Cell Stem Cell , vol.8 , pp. 188-199
    • Hochmuth, C.E.1    Biteau, B.2    Bohmann, D.3    Jasper, H.4
  • 16
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • Lambert, A.J., Brand, M.D., Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 382 (2004), 511–517.
    • (2004) Biochem. J. , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 17
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Lambert, A.J., Brand, M.D., Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 279 (2004), 39414–39420.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 18
    • 34548617735 scopus 로고    scopus 로고
    • Low rates of hydrogen peroxide production by isolated heart mitochondria associate with long maximum lifespan in vertebrate homeotherms
    • Lambert, A.J., Boysen, H.M., Buckingham, J.A., Yang, T., Podlutsky, A., Austad, S.N., Kunz, T.H., Buffenstein, R., Brand, M.D., Low rates of hydrogen peroxide production by isolated heart mitochondria associate with long maximum lifespan in vertebrate homeotherms. Aging Cell 6 (2007), 607–618.
    • (2007) Aging Cell , vol.6 , pp. 607-618
    • Lambert, A.J.1    Boysen, H.M.2    Buckingham, J.A.3    Yang, T.4    Podlutsky, A.5    Austad, S.N.6    Kunz, T.H.7    Buffenstein, R.8    Brand, M.D.9
  • 19
    • 0035341376 scopus 로고    scopus 로고
    • Mosaic analysis with a repressible cell marker (MARCM) for Drosophila neural development
    • Lee, T., Luo, L., Mosaic analysis with a repressible cell marker (MARCM) for Drosophila neural development. Trends Neurosci. 24 (2001), 251–254.
    • (2001) Trends Neurosci. , vol.24 , pp. 251-254
    • Lee, T.1    Luo, L.2
  • 20
    • 84873838480 scopus 로고    scopus 로고
    • Trachea-derived dpp controls adult midgut homeostasis in Drosophila
    • Li, Z., Zhang, Y., Han, L., Shi, L., Lin, X., Trachea-derived dpp controls adult midgut homeostasis in Drosophila. Dev. Cell 24 (2013), 133–143.
    • (2013) Dev. Cell , vol.24 , pp. 133-143
    • Li, Z.1    Zhang, Y.2    Han, L.3    Shi, L.4    Lin, X.5
  • 22
    • 84867853849 scopus 로고    scopus 로고
    • Mitochondrial defect drives non-autonomous tumour progression through Hippo signalling in Drosophila
    • Ohsawa, S., Sato, Y., Enomoto, M., Nakamura, M., Betsumiya, A., Igaki, T., Mitochondrial defect drives non-autonomous tumour progression through Hippo signalling in Drosophila. Nature 490 (2012), 547–551.
    • (2012) Nature , vol.490 , pp. 547-551
    • Ohsawa, S.1    Sato, Y.2    Enomoto, M.3    Nakamura, M.4    Betsumiya, A.5    Igaki, T.6
  • 23
    • 84884519058 scopus 로고    scopus 로고
    • Inhibitors of ROS production by the ubiquinone-binding site of mitochondrial complex I identified by chemical screening
    • Orr, A.L., Ashok, D., Sarantos, M.R., Shi, T., Hughes, R.E., Brand, M.D., Inhibitors of ROS production by the ubiquinone-binding site of mitochondrial complex I identified by chemical screening. Free Radic. Biol. Med. 65 (2013), 1047–1059.
    • (2013) Free Radic. Biol. Med. , vol.65 , pp. 1047-1059
    • Orr, A.L.1    Ashok, D.2    Sarantos, M.R.3    Shi, T.4    Hughes, R.E.5    Brand, M.D.6
  • 25
    • 0037974679 scopus 로고    scopus 로고
    • Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD
    • Powell, C.S., Jackson, R.M., Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD. Am. J. Physiol. Lung Cell. Mol. Physiol. 285 (2003), L189–L198.
    • (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.285 , pp. L189-L198
    • Powell, C.S.1    Jackson, R.M.2
  • 26
    • 84879774696 scopus 로고    scopus 로고
    • The determination and analysis of site-specific rates of mitochondrial reactive oxygen species production
    • Quinlan, C.L., Perevoschikova, I.V., Goncalves, R.L.S., Hey-Mogensen, M., Brand, M.D., The determination and analysis of site-specific rates of mitochondrial reactive oxygen species production. Methods Enzymol. 526 (2013), 189–217.
    • (2013) Methods Enzymol. , vol.526 , pp. 189-217
    • Quinlan, C.L.1    Perevoschikova, I.V.2    Goncalves, R.L.S.3    Hey-Mogensen, M.4    Brand, M.D.5
  • 27
    • 84879430920 scopus 로고    scopus 로고
    • Sites of reactive oxygen species generation by mitochondria oxidizing different substrates
    • Quinlan, C.L., Perevoshchikova, I.V., Hey-Mogensen, M., Orr, A.L., Brand, M.D., Sites of reactive oxygen species generation by mitochondria oxidizing different substrates. Redox Biol. 1 (2013), 304–312.
    • (2013) Redox Biol. , vol.1 , pp. 304-312
    • Quinlan, C.L.1    Perevoshchikova, I.V.2    Hey-Mogensen, M.3    Orr, A.L.4    Brand, M.D.5
  • 28
    • 84896935583 scopus 로고    scopus 로고
    • The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I
    • Quinlan, C.L., Goncalves, R.L.S., Hey-Mogensen, M., Yadava, N., Bunik, V.I., Brand, M.D., The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I. J. Biol. Chem. 289 (2014), 8312–8325.
    • (2014) J. Biol. Chem. , vol.289 , pp. 8312-8325
    • Quinlan, C.L.1    Goncalves, R.L.S.2    Hey-Mogensen, M.3    Yadava, N.4    Bunik, V.I.5    Brand, M.D.6
  • 30
    • 84975755192 scopus 로고    scopus 로고
    • Mitochondrial ROS signaling in organismal homeostasis
    • Shadel, G.S., Horvath, T.L., Mitochondrial ROS signaling in organismal homeostasis. Cell 163 (2015), 560–569.
    • (2015) Cell , vol.163 , pp. 560-569
    • Shadel, G.S.1    Horvath, T.L.2
  • 31
    • 84897444272 scopus 로고    scopus 로고
    • 2 generation: redox signaling and oxidative stress
    • 2 generation: redox signaling and oxidative stress. J. Biol. Chem. 289 (2014), 8735–8741.
    • (2014) J. Biol. Chem. , vol.289 , pp. 8735-8741
    • Sies, H.1
  • 32
    • 84918835614 scopus 로고    scopus 로고
    • Integration of UPRER and oxidative stress signaling in the control of intestinal stem cell proliferation
    • Wang, L., Zeng, X., Ryoo, H.D., Jasper, H., Integration of UPRER and oxidative stress signaling in the control of intestinal stem cell proliferation. PLoS Genet., 10, 2014, e1004568.
    • (2014) PLoS Genet. , vol.10 , pp. e1004568
    • Wang, L.1    Zeng, X.2    Ryoo, H.D.3    Jasper, H.4
  • 33
    • 84891794636 scopus 로고    scopus 로고
    • JNK interaction with Sab mediates ER stress induced inhibition of mitochondrial respiration and cell death
    • Win, S., Than, T.A., Fernandez-Checa, J.C., Kaplowitz, N., JNK interaction with Sab mediates ER stress induced inhibition of mitochondrial respiration and cell death. Cell Death Dis., 5, 2014, e989.
    • (2014) Cell Death Dis. , vol.5 , pp. e989
    • Win, S.1    Than, T.A.2    Fernandez-Checa, J.C.3    Kaplowitz, N.4
  • 34
    • 84978287529 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase mediates mouse liver injury through a novel Sab (SH3BP5)-dependent pathway leading to inactivation of intramitochondrial Src
    • Win, S., Than, T.A., Min, R.W.M., Aghajan, M., Kaplowitz, N., c-Jun N-terminal kinase mediates mouse liver injury through a novel Sab (SH3BP5)-dependent pathway leading to inactivation of intramitochondrial Src. Hepatology 63 (2016), 1987–2003.
    • (2016) Hepatology , vol.63 , pp. 1987-2003
    • Win, S.1    Than, T.A.2    Min, R.W.M.3    Aghajan, M.4    Kaplowitz, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.