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Volumn 218, Issue , 2014, Pages 12-19

NADPH oxidase inhibitor, apocynin, improves renal glutathione status in Zucker diabetic fatty rats: A comparison with melatonin

Author keywords

Apocynin; Glutathione; Kidney; Melatonin; NADPH oxidase; ZDF rat

Indexed keywords

APOCYNIN; CREATININE; DRINKING WATER; GLUCOSE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HYDROXYL RADICAL; MELATONIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UREA;

EID: 84900854397     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2014.04.005     Document Type: Article
Times cited : (29)

References (51)
  • 2
    • 84861062943 scopus 로고    scopus 로고
    • Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system
    • B. Lassègue, A. San Martín, and K.K. Griendling Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system Circ. Res. 110 2012 1364 1390
    • (2012) Circ. Res. , vol.110 , pp. 1364-1390
    • Lassègue, B.1    San Martín, A.2    Griendling, K.K.3
  • 3
    • 80051580160 scopus 로고    scopus 로고
    • Oxidative stress and diabetic kidney disease
    • R.C. Stanton Oxidative stress and diabetic kidney disease Curr. Diab. Rep. 11 2011 330 336
    • (2011) Curr. Diab. Rep. , vol.11 , pp. 330-336
    • Stanton, R.C.1
  • 5
    • 34547788748 scopus 로고    scopus 로고
    • Suppressing renal NADPH oxidase to treat diabetic nephropathy
    • A. Tojo, K. Asaba, and M.L. Onozato Suppressing renal NADPH oxidase to treat diabetic nephropathy Expert Opin. Ther. Targets 11 2007 1011 1018
    • (2007) Expert Opin. Ther. Targets , vol.11 , pp. 1011-1018
    • Tojo, A.1    Asaba, K.2    Onozato, M.L.3
  • 7
    • 84875625176 scopus 로고    scopus 로고
    • Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor
    • M.S. Petronio, M.L. Zeraik, L.M. Fonseca, and V.F. Ximenes Apocynin: chemical and biophysical properties of a NADPH oxidase inhibitor Molecules 18 2013 2821 2839
    • (2013) Molecules , vol.18 , pp. 2821-2839
    • Petronio, M.S.1    Zeraik, M.L.2    Fonseca, L.M.3    Ximenes, V.F.4
  • 8
    • 53449087924 scopus 로고    scopus 로고
    • The role of the methoxyphenol apocynin, a vascular NADPH oxidase inhibitor, as a chemopreventative agent in the potential treatment of cardiovascular diseases
    • J. Yu, M. Weïwer, R.J. Linhardt, and J.S. Dordick The role of the methoxyphenol apocynin, a vascular NADPH oxidase inhibitor, as a chemopreventative agent in the potential treatment of cardiovascular diseases Curr. Vasc. Pharmacol. 6 2008 204 217
    • (2008) Curr. Vasc. Pharmacol. , vol.6 , pp. 204-217
    • Yu, J.1    Weïwer, M.2    Linhardt, R.J.3    Dordick, J.S.4
  • 10
    • 33646130154 scopus 로고    scopus 로고
    • The NADPH oxidase inhibitor apocynin (acetovanillone) induces oxidative stress
    • C. Riganti, C. Costamagna, A. Bosia, and D. Gigo The NADPH oxidase inhibitor apocynin (acetovanillone) induces oxidative stress Toxicol. Appl. Pharmacol. 212 2006 179 187
    • (2006) Toxicol. Appl. Pharmacol. , vol.212 , pp. 179-187
    • Riganti, C.1    Costamagna, C.2    Bosia, A.3    Gigo, D.4
  • 12
    • 65049087190 scopus 로고    scopus 로고
    • Glutathione: Overview of its protective roles, measurement, and biosynthesis
    • H.J. Forman, H. Zhang, and A. Rinna Glutathione: overview of its protective roles, measurement, and biosynthesis Mol. Aspects. Med. 30 2009 1 12
    • (2009) Mol. Aspects. Med. , vol.30 , pp. 1-12
    • Forman, H.J.1    Zhang, H.2    Rinna, A.3
  • 14
  • 15
    • 4344625264 scopus 로고    scopus 로고
    • Nephropathy in Zucker diabetic fat rat is associated with oxidative and nitrosative stress: Prevention by chronic therapy with a peroxynitrite scavenger ebselen
    • P.N. Chander, O. Gealekman, S.V. Brodsky, S. Elitok, A. Tojo, M. Crabtree, S.S. Gross, and M.S. Goligorsky Nephropathy in Zucker diabetic fat rat is associated with oxidative and nitrosative stress: prevention by chronic therapy with a peroxynitrite scavenger ebselen J. Am. Soc. Nephrol. 15 2004 2391 2403
    • (2004) J. Am. Soc. Nephrol. , vol.15 , pp. 2391-2403
    • Chander, P.N.1    Gealekman, O.2    Brodsky, S.V.3    Elitok, S.4    Tojo, A.5    Crabtree, M.6    Gross, S.S.7    Goligorsky, M.S.8
  • 16
    • 64549104842 scopus 로고    scopus 로고
    • The use of animal models in the study of diabetes mellitus
    • A. Chatzigeorgiou, A. Halapas, K. Kalafatakis, and E. Kamper The use of animal models in the study of diabetes mellitus In Vivo 23 2009 245 258
    • (2009) Vivo , vol.23 , pp. 245-258
    • Chatzigeorgiou, A.1    Halapas, A.2    Kalafatakis, K.3    Kamper, E.4
  • 17
    • 79960566642 scopus 로고    scopus 로고
    • Long-term treatment with nebivolol attenuates renal damage in Zucker diabetic fatty rats
    • J.E. Toblli, G. Cao, J.F. Giani, M.C. Muñoz, M. Angerosa, and F.P. Dominici Long-term treatment with nebivolol attenuates renal damage in Zucker diabetic fatty rats J. Hypertens. 29 2011 1613 1623
    • (2011) J. Hypertens. , vol.29 , pp. 1613-1623
    • Toblli, J.E.1    Cao, G.2    Giani, J.F.3    Muñoz, M.C.4    Angerosa, M.5    Dominici, F.P.6
  • 19
    • 33846940538 scopus 로고    scopus 로고
    • Melatonin is more effective than taurine and 5-hydroxytryptophan against hyperglycemia-induced kidney-cortex tubules injury
    • R.A. Derlacz, M. Sliwinska, A. Piekutowska, K. Winiarska, J. Drozak, and J. Bryla Melatonin is more effective than taurine and 5-hydroxytryptophan against hyperglycemia-induced kidney-cortex tubules injury J. Pineal Res. 42 2007 203 209
    • (2007) J. Pineal Res. , vol.42 , pp. 203-209
    • Derlacz, R.A.1    Sliwinska, M.2    Piekutowska, A.3    Winiarska, K.4    Drozak, J.5    Bryla, J.6
  • 21
    • 84862588786 scopus 로고    scopus 로고
    • Glucose: A vital toxin and potential utility of melatonin in protecting against the diabetic state
    • A. Korkmaz, S. Ma, T. Topal, S. Rosales-Corral, D.X. Tan, and R.J. Reiter Glucose: a vital toxin and potential utility of melatonin in protecting against the diabetic state Mol. Cell. Endocrinol. 349 2012 128 137
    • (2012) Mol. Cell. Endocrinol. , vol.349 , pp. 128-137
    • Korkmaz, A.1    Ma, S.2    Topal, T.3    Rosales-Corral, S.4    Tan, D.X.5    Reiter, R.J.6
  • 24
    • 0032923362 scopus 로고    scopus 로고
    • Melatonin and taurine reduce early glomerulopathy in diabetic rats
    • H. Ha, M.R. Yu, and K.H. Kim Melatonin and taurine reduce early glomerulopathy in diabetic rats Free Radic. Biol. Med. 26 1999 944 950
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 944-950
    • Ha, H.1    Yu, M.R.2    Kim, K.H.3
  • 25
    • 0035850674 scopus 로고    scopus 로고
    • The inhibition of gluconeogenesis by chloroquine contributes to its hypoglycaemic action
    • R. Jarzyna, A. Kiersztan, O. Lisowa, and J. Bryla The inhibition of gluconeogenesis by chloroquine contributes to its hypoglycaemic action Eur. J. Pharmacol. 428 2001 381 388
    • (2001) Eur. J. Pharmacol. , vol.428 , pp. 381-388
    • Jarzyna, R.1    Kiersztan, A.2    Lisowa, O.3    Bryla, J.4
  • 26
    • 79251538947 scopus 로고    scopus 로고
    • Inhibition of renal gluconeogenesis contributes to hypoglycaemic action of NADPH oxidase inhibitor, apocynin
    • K. Winiarska, M. Grabowski, and M.K. Rogacki Inhibition of renal gluconeogenesis contributes to hypoglycaemic action of NADPH oxidase inhibitor, apocynin Chem. Biol. Interact. 189 2011 119 126
    • (2011) Chem. Biol. Interact. , vol.189 , pp. 119-126
    • Winiarska, K.1    Grabowski, M.2    Rogacki, M.K.3
  • 27
    • 0025737103 scopus 로고
    • Regulation of mouse glutathione S-transferases by chemoprotectors. Molecular evidence for the existence of three distinct alpha-class glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver
    • L.I. McLellan, L.A. Kerr, A.D. Cronshaw, and J.D. Hayes Regulation of mouse glutathione S-transferases by chemoprotectors. Molecular evidence for the existence of three distinct alpha-class glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver Biochem. J. 276 1991 461 469
    • (1991) Biochem. J. , vol.276 , pp. 461-469
    • McLellan, L.I.1    Kerr, L.A.2    Cronshaw, A.D.3    Hayes, J.D.4
  • 28
    • 24944480708 scopus 로고    scopus 로고
    • Oxygen availability limits renal NADPH-dependent superoxide production
    • Y. Chen, P.S. Gill, and W.J. Welch Oxygen availability limits renal NADPH-dependent superoxide production Am. J. Physiol. Ren. Physiol. 289 2005 749 753
    • (2005) Am. J. Physiol. Ren. Physiol. , vol.289 , pp. 749-753
    • Chen, Y.1    Gill, P.S.2    Welch, W.J.3
  • 30
  • 32
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • D.E. Paglia, and W.N. Valentine Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase J. Lab. Clin. Med. 70 1967 158 169
    • (1967) J. Lab. Clin. Med. , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 33
    • 0037818355 scopus 로고    scopus 로고
    • A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production
    • D. Hamilton, J.H. Wu, M. Alaoui-Jamali, and G. Batist A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production Blood 102 2003 725 730
    • (2003) Blood , vol.102 , pp. 725-730
    • Hamilton, D.1    Wu, J.H.2    Alaoui-Jamali, M.3    Batist, G.4
  • 36
    • 0025857309 scopus 로고
    • Recovery of impaired gluconeogenesis in kidney cortex tubules of gentamicin-treated rabbits
    • M. Michalik, I. Biedermann, T. Lietz, and J. Bryla Recovery of impaired gluconeogenesis in kidney cortex tubules of gentamicin-treated rabbits Pharmacol. Res. 23 1991 259 269
    • (1991) Pharmacol. Res. , vol.23 , pp. 259-269
    • Michalik, M.1    Biedermann, I.2    Lietz, T.3    Bryla, J.4
  • 37
    • 0037084991 scopus 로고    scopus 로고
    • Determination of intracellular glutathione and thiols by high performance liquid chromatography with a gold electrode at the femtomole level: Comparison with a spectroscopic assay
    • Y. Hiraku, M. Murata, and S. Kawanishi Determination of intracellular glutathione and thiols by high performance liquid chromatography with a gold electrode at the femtomole level: comparison with a spectroscopic assay Biochim. Biophys. Acta 1570 2002 47 52
    • (2002) Biochim. Biophys. Acta , vol.1570 , pp. 47-52
    • Hiraku, Y.1    Murata, M.2    Kawanishi, S.3
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 80052000670 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 in health and disease: From molecular mechanisms to therapeutic opportunities
    • E. Lubos, J. Loscalzo, and D.E. Handy Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities Antioxid. Redox. Signal. 15 2011 1957 1997
    • (2011) Antioxid. Redox. Signal. , vol.15 , pp. 1957-1997
    • Lubos, E.1    Loscalzo, J.2    Handy, D.E.3
  • 44
    • 2942590474 scopus 로고    scopus 로고
    • Apocynin prevents cyclooxygenase 2 expression in human monocytes through NADPH oxidase and glutathione redox-dependent mechanisms
    • S.S. Barbieri, V. Cavalca, S. Eligini, M. Brambilla, A. Caiani, E. Tremoli, and S. Colli Apocynin prevents cyclooxygenase 2 expression in human monocytes through NADPH oxidase and glutathione redox-dependent mechanisms Free Radic. Biol. Med. 37 2004 156 165
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 156-165
    • Barbieri, S.S.1    Cavalca, V.2    Eligini, S.3    Brambilla, M.4    Caiani, A.5    Tremoli, E.6    Colli, S.7
  • 46
    • 84855398654 scopus 로고    scopus 로고
    • Anti-oxidative effect of apocynin on insulin resistance in high-fat diet mice
    • R. Meng, D.L. Zhu, Y. Bi, D.H. Yang, and Y.P. Wang Anti-oxidative effect of apocynin on insulin resistance in high-fat diet mice Ann. Clin. Lab. Sci. 41 2011 236 243
    • (2011) Ann. Clin. Lab. Sci. , vol.41 , pp. 236-243
    • Meng, R.1    Zhu, D.L.2    Bi, Y.3    Yang, D.H.4    Wang, Y.P.5
  • 48
    • 58249119832 scopus 로고    scopus 로고
    • Effects of NADPH oxidase inhibitor on diabetic nephropathy in OLETF rats: The role of reducing oxidative stress in its protective property
    • S.M. Nam, M.Y. Lee, J.H. Koh, J.H. Park, J.Y. Shin, Y.G. Shin, S.B. Koh, E.Y. Lee, and C.H. Chung Effects of NADPH oxidase inhibitor on diabetic nephropathy in OLETF rats: the role of reducing oxidative stress in its protective property Diab. Res. Clin. Pract. 83 2009 176 182
    • (2009) Diab. Res. Clin. Pract. , vol.83 , pp. 176-182
    • Nam, S.M.1    Lee, M.Y.2    Koh, J.H.3    Park, J.H.4    Shin, J.Y.5    Shin, Y.G.6    Koh, S.B.7    Lee, E.Y.8    Chung, C.H.9
  • 49
    • 77953328985 scopus 로고    scopus 로고
    • Preservation of kidney function with combined inhibition of NADPH oxidase and angiotensin-converting enzyme in diabetic nephropathy
    • V. Thallas-Bonke, M.T. Coughlan, L.A. Bach, M.E. Cooper, and J.M. Forbes Preservation of kidney function with combined inhibition of NADPH oxidase and angiotensin-converting enzyme in diabetic nephropathy Am. J. Nephrol. 32 2010 73 82
    • (2010) Am. J. Nephrol. , vol.32 , pp. 73-82
    • Thallas-Bonke, V.1    Coughlan, M.T.2    Bach, L.A.3    Cooper, M.E.4    Forbes, J.M.5
  • 50
    • 84890129569 scopus 로고    scopus 로고
    • Influence of melatonin receptor signalling on parameters involved in blood glucose regulation
    • 10.1111/jpi.12100 [Epub ahead of print]
    • I. Bazwinsky-Wutschke, L. Bieseke, E. Mühlbauer, and E. Peschke Influence of melatonin receptor signalling on parameters involved in blood glucose regulation J. Pineal Res. 2013 10.1111/jpi.12100 [Epub ahead of print]
    • (2013) J. Pineal Res.
    • Bazwinsky-Wutschke, I.1    Bieseke, L.2    Mühlbauer, E.3    Peschke, E.4


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