메뉴 건너뛰기




Volumn 81, Issue , 2015, Pages 13-21

ERK1/2 pathway is involved in renal gluconeogenesis inhibition under conditions of lowered NADPH oxidase activity

Author keywords

Diabetes; ERK1 2 pathway; Gluconeogenesis; NADPH oxidase; Phosphoenolpyruvate carboxykinase; Renal proximal tubules; ZDF rat

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2,4 THIAZOLIDINEDIONE; 3 (2 AMINOETHYL) 5 [(4 ETHOXYPHENYL)METHYLENE] 2,4 THIAZOLIDINEDIONE; APOCYNIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TEMPOL; UNCLASSIFIED DRUG; 1,3 BUTADIENE DERIVATIVE; 2,4 THIAZOLIDINEDIONE DERIVATIVE; ACETOPHENONE DERIVATIVE; AMINE OXIDE; ANTIDIABETIC AGENT; ANTIOXIDANT; MITOGEN ACTIVATED PROTEIN KINASE 3; NITRILE; PHOSPHOENOLPYRUVATE CARBOXYKINASE 1 (SOLUBLE) PROTEIN, RAT; PROTEIN KINASE INHIBITOR; REACTIVE OXYGEN METABOLITE; SIGNAL PEPTIDE; SPIN LABELING;

EID: 84923233384     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.12.024     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 76249133903 scopus 로고    scopus 로고
    • Role of the kidney in normal glucose homeostasis and in the hyperglycaemia of diabetes mellitus: Therapeutic implications
    • J.E. Gerich Role of the kidney in normal glucose homeostasis and in the hyperglycaemia of diabetes mellitus: therapeutic implications Diabet. Med. 27 2010 136 142
    • (2010) Diabet. Med. , vol.27 , pp. 136-142
    • Gerich, J.E.1
  • 2
    • 79952209559 scopus 로고    scopus 로고
    • Glucose handling by the kidney
    • A. Mather, and C. Pollock Glucose handling by the kidney Kidney Int. Suppl. 120 2011 S1 S6
    • (2011) Kidney Int. Suppl. , vol.120 , pp. S1-S6
    • Mather, A.1    Pollock, C.2
  • 3
    • 84860391886 scopus 로고    scopus 로고
    • Kidney: Its impact on glucose homeostasis and hormonal regulation
    • A. Mitrakou Kidney: its impact on glucose homeostasis and hormonal regulation Diabetes Res. Clin. Pract. 93 Suppl. 1 2011 S66 S72
    • (2011) Diabetes Res. Clin. Pract. , vol.93 , pp. S66-S72
    • Mitrakou, A.1
  • 4
    • 83555166240 scopus 로고    scopus 로고
    • Transcription factors and coactivators controlling nutrient and hormonal regulation of hepatic gluconeogenesis
    • S. Jitrapakdee Transcription factors and coactivators controlling nutrient and hormonal regulation of hepatic gluconeogenesis Int. J. Biochem. Cell. Biol. 44 2012 33 45
    • (2012) Int. J. Biochem. Cell. Biol. , vol.44 , pp. 33-45
    • Jitrapakdee, S.1
  • 6
    • 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
  • 7
    • 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
  • 9
    • 84880176927 scopus 로고    scopus 로고
    • Nox as a target for diabetic complications
    • Y. Gorin, and K. Block Nox as a target for diabetic complications Clin. Sci. 125 2013 361 382
    • (2013) Clin. Sci. , vol.125 , pp. 361-382
    • Gorin, Y.1    Block, K.2
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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) In Vivo , vol.23 , pp. 245-258
    • Chatzigeorgiou, A.1    Halapas, A.2    Kalafatakis, K.3    Kamper, E.4
  • 14
    • 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
  • 15
    • 84900854397 scopus 로고    scopus 로고
    • NADPH oxidase inhibitor, apocynin, improves renal glutathione status in Zucker diabetic fatty rats: A comparison with melatonin
    • K. Winiarska, D. Focht, B. Sierakowski, K. Lewandowski, M. Orlowska, and M. Usarek NADPH oxidase inhibitor, apocynin, improves renal glutathione status in Zucker diabetic fatty rats: a comparison with melatonin Chem. Biol. Interact. 218 2014 12 19
    • (2014) Chem. Biol. Interact. , vol.218 , pp. 12-19
    • Winiarska, K.1    Focht, D.2    Sierakowski, B.3    Lewandowski, K.4    Orlowska, M.5    Usarek, M.6
  • 16
    • 24944480708 scopus 로고    scopus 로고
    • Oxygen availability limits renal NADPH-dependent superoxide production
    • Y. ChenS. Gill, and W.L. Welch Oxygen availability limits renal NADPH-dependent superoxide production Am. J. Physiol. Renal Physiol 289 2005 749 753
    • (2005) Am. J. Physiol. Renal Physiol , vol.289 , pp. 749-753
    • Chen, Y.1    Gill, P.S.2    Welch, W.L.3
  • 17
  • 18
    • 0018264555 scopus 로고
    • P-enolpyruvate carboxykinase ferroactivator. Distribution and the influence of diabetes and starvation
    • M.J. MacDonald, L.A. Bentle, and H.A. Lardy P-enolpyruvate carboxykinase ferroactivator. Distribution and the influence of diabetes and starvation J. Biol. Chem. 253 1978 116 124
    • (1978) J. Biol. Chem. , vol.253 , pp. 116-124
    • Macdonald, M.J.1    Bentle, L.A.2    Lardy, H.A.3
  • 19
    • 0018348829 scopus 로고
    • Determination of phosphoenolpyruvate carboxykinase activity with deoxyguanosine 5′-diphosphate asnucleotide substrate
    • Petrescu, I.; Bojan, O.; Saied, M.; Barzu, O.; Schmidt, F.; Kuhnle, H.F. Determination of phosphoenolpyruvate carboxykinase activity with deoxyguanosine 5′-diphosphate asnucleotide substrate. Anal. Biochem. 96: 279-281; 1979.
    • (1979) Anal. Biochem , vol.96 , pp. 279-281
    • Petrescu, I.1    Bojan, O.2    Saied, M.3    Barzu, O.4    Schmidt, F.5    Kuhnle H. ., F.6
  • 22
    • 37549064772 scopus 로고    scopus 로고
    • Simultaneous extraction of several metabolites of energy metabolism and related substances in mammalian cells: Optimization using experimental design
    • J.B. Ritter, Y. Genzel, and U. Reichl Simultaneous extraction of several metabolites of energy metabolism and related substances in mammalian cells: optimization using experimental design Anal. Biochem. 373 2008 349 369
    • (2008) Anal. Biochem. , vol.373 , pp. 349-369
    • Ritter, J.B.1    Genzel, Y.2    Reichl, U.3
  • 23
    • 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
  • 24
    • 77951090729 scopus 로고    scopus 로고
    • Effects of tempol and redox-cycling nitroxides in models of oxidative stress
    • S.C. Wilcox Effects of tempol and redox-cycling nitroxides in models of oxidative stress Pharmacol. Ther. 126 2010 119 145
    • (2010) Pharmacol. Ther. , vol.126 , pp. 119-145
    • Wilcox, S.C.1
  • 26
    • 84880267827 scopus 로고    scopus 로고
    • Reactive oxygen species in the activation of MAP kinases
    • Y. Son, S. Kim, H.T. Chung, and H.O. Pae Reactive oxygen species in the activation of MAP kinases Methods Enzymol. 528 2013 27 48
    • (2013) Methods Enzymol. , vol.528 , pp. 27-48
    • Son, Y.1    Kim, S.2    Chung, H.T.3    Pae, H.O.4
  • 28
    • 34249816776 scopus 로고    scopus 로고
    • Multisite phosphorylation of the cAMP response element-binding protein (CREB) by a diversity of protein kinases
    • M. Johannessen, and U. Moens Multisite phosphorylation of the cAMP response element-binding protein (CREB) by a diversity of protein kinases Front. Biosci. 12 2007 1814 1832
    • (2007) Front. Biosci. , vol.12 , pp. 1814-1832
    • Johannessen, M.1    Moens, U.2
  • 30
    • 84862294189 scopus 로고    scopus 로고
    • Jr. ERK1/2 MAP kinases: Structure, function, and regulation
    • R. Roskoski Jr. ERK1/2 MAP kinases: structure, function, and regulation Pharmacol. Res. 66 2012 105 143
    • (2012) Pharmacol. Res. , vol.66 , pp. 105-143
    • Roskoski, R.1
  • 31
    • 52449095361 scopus 로고    scopus 로고
    • The RSK family of kinases: Emerging roles in cellular signalling
    • R. Anjum, and J. Blenis The RSK family of kinases: emerging roles in cellular signalling Nat. Rev. Mol. Cell. Biol. 9 2008 747 758
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 747-758
    • Anjum, R.1    Blenis, J.2
  • 35
    • 0014731259 scopus 로고
    • Hormonal regulation of phosphoenolpyruvate carboxykinase activity in liver and kidney of adult animals and formation of this enzyme in developing rabbit liver
    • Usatenko, M.S.Hormonalregulationofphosphoenolpyruvatecarboxykinase activity inliverandkidneyofadultanimalsandformationofthisenzymein developing rabbitliver. Biochem. Med. 3:298310;1970.
    • (1970) Biochem. Med. , vol.3 , pp. 298-310
    • Usatenko, M.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.