메뉴 건너뛰기




Volumn 4, Issue , 2014, Pages 928-935

High-fat diet-induced changes in liver thioredoxin and thioredoxin reductase as a novel feature of insulin resistance

Author keywords

High fat diet; Insulin resistance; S acylation; Thioredoxin; Thioredoxin reductase

Indexed keywords

THIOREDOXIN; THIOREDOXIN REDUCTASE; 4 HYDROXYNONENAL; INSULIN; LIVER ENZYME;

EID: 84918521580     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2014.10.015     Document Type: Article
Times cited : (21)

References (37)
  • 1
    • 78751582294 scopus 로고    scopus 로고
    • Effects of a high-fat diet on energy metabolism and ROS production in rat liver
    • Vial G., et al. Effects of a high-fat diet on energy metabolism and ROS production in rat liver. J. Hepatol. 2011, 54:348-356.
    • (2011) J. Hepatol. , vol.54 , pp. 348-356
    • Vial, G.1
  • 2
    • 47149115165 scopus 로고    scopus 로고
    • Increased oxidative stress precedes the onset of high-fat diet-induced insulin resistance and obesity
    • Matsuzawa-Nagata N., et al. Increased oxidative stress precedes the onset of high-fat diet-induced insulin resistance and obesity. Metabolism 2008, 57:1071-1077.
    • (2008) Metabolism , vol.57 , pp. 1071-1077
    • Matsuzawa-Nagata, N.1
  • 3
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • Zhong L., Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J. Biol. Chem. 2000, 275:18121-18128.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2
  • 4
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Bjornstedt M., Xue J., Huang W., Akesson B., Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J. Biol. Chem. 1994, 269:29382-29384.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 5
    • 0029591899 scopus 로고
    • Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell
    • Cha M.K., Kim I.H. Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell. Biochem. Biophys. Res. Commun. 1995, 217:900-907.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 900-907
    • Cha, M.K.1    Kim, I.H.2
  • 6
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M., et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 1998, 17:2596-2606.
    • (1998) EMBO J. , vol.17 , pp. 2596-2606
    • Saitoh, M.1
  • 7
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 1979, 254:9627-9632.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 8
    • 84860497776 scopus 로고    scopus 로고
    • The role of thioredoxin in the regulation of cellular processes by S-nitrosylation
    • Sengupta R., Holmgren A. The role of thioredoxin in the regulation of cellular processes by S-nitrosylation. Biochim. Biophys. Acta 2012, 1820:689-700.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 689-700
    • Sengupta, R.1    Holmgren, A.2
  • 9
    • 58049200135 scopus 로고    scopus 로고
    • Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation
    • Chen Y.Y., Chu H.M., Pan K.T., Teng C.H., Wang D.L., Wang A.H., Khoo K.H., Meng T.C. Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation. J. Biol. Chem. 2008, 283:35265-35272.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35265-35272
    • Chen, Y.Y.1    Chu, H.M.2    Pan, K.T.3    Teng, C.H.4    Wang, D.L.5    Wang, A.H.6    Khoo, K.H.7    Meng, T.C.8
  • 10
    • 80052235110 scopus 로고    scopus 로고
    • Increased adipocyte S-nitrosylation targets anti-lipolytic action of insulin: relevance to adipose tissue dysfunction in obesity
    • Ovadia H., Haim Y., Nov O., Almog O., Kovsan J., Bashan N., Benhar M., Rudich A. Increased adipocyte S-nitrosylation targets anti-lipolytic action of insulin: relevance to adipose tissue dysfunction in obesity. J. Biol. Chem. 2011, 286:30433-30443.
    • (2011) J. Biol. Chem. , vol.286 , pp. 30433-30443
    • Ovadia, H.1    Haim, Y.2    Nov, O.3    Almog, O.4    Kovsan, J.5    Bashan, N.6    Benhar, M.7    Rudich, A.8
  • 11
    • 57349188998 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B by manipulation of dietary selenium affects the triglyceride concentration in rat liver
    • Mueller A.S., et al. Redox regulation of protein tyrosine phosphatase 1B by manipulation of dietary selenium affects the triglyceride concentration in rat liver. J. Nutr. 2008, 138:2328-2336.
    • (2008) J. Nutr. , vol.138 , pp. 2328-2336
    • Mueller, A.S.1
  • 14
    • 77953587983 scopus 로고    scopus 로고
    • Oxidative stress signaling underlying liver disease and hepatoprotective mechanisms
    • Videla L.A. Oxidative stress signaling underlying liver disease and hepatoprotective mechanisms. World J. Hepatol. 2009, 1:72-78.
    • (2009) World J. Hepatol. , vol.1 , pp. 72-78
    • Videla, L.A.1
  • 16
    • 77956226935 scopus 로고    scopus 로고
    • Decreased serum levels of thioredoxin in patients with coronary artery disease plus hyperhomocysteinemia is strongly associated with the disease severity
    • Wu Y., Yang L., Zhong L. Decreased serum levels of thioredoxin in patients with coronary artery disease plus hyperhomocysteinemia is strongly associated with the disease severity. Atherosclerosis 2010, 212:351-355.
    • (2010) Atherosclerosis , vol.212 , pp. 351-355
    • Wu, Y.1    Yang, L.2    Zhong, L.3
  • 17
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel R.C., Green W.N. Labeling and quantifying sites of protein palmitoylation. Biotechniques 2004, 36:276-285.
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 18
    • 84876011856 scopus 로고    scopus 로고
    • The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity
    • Cebula M., Moolla N., Capovilla A., Arner E.S. The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity. J. Biol. Chem. 2013, 288:10002-10011.
    • (2013) J. Biol. Chem. , vol.288 , pp. 10002-10011
    • Cebula, M.1    Moolla, N.2    Capovilla, A.3    Arner, E.S.4
  • 19
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: policing protein stability and traffic
    • Linder M.E., Deschenes R.J. Palmitoylation: policing protein stability and traffic. Nat. Rev. Mol. Cell Biol. 2007, 8:74-84.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 20
    • 84862571570 scopus 로고    scopus 로고
    • Redox cycling of 1,2-naphthoquinone by thioredoxin1 through Cys32 and Cys35 causes inhibition of its catalytic activity and activation of ASK1/p38 signaling
    • Shinkai Y., Iwamoto N., Miura T., Ishii T., Cho A.K., Kumagai Y. Redox cycling of 1,2-naphthoquinone by thioredoxin1 through Cys32 and Cys35 causes inhibition of its catalytic activity and activation of ASK1/p38 signaling. Chem. Res. Toxicol. 2012, 25:1222-1230.
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 1222-1230
    • Shinkai, Y.1    Iwamoto, N.2    Miura, T.3    Ishii, T.4    Cho, A.K.5    Kumagai, Y.6
  • 21
    • 33745828301 scopus 로고    scopus 로고
    • Saturated fatty acids induce endoplasmic reticulum stress and apoptosis independently of ceramide in liver cells
    • Wei Y., Wang D., Topczewski F., Pagliassotti M.J. Saturated fatty acids induce endoplasmic reticulum stress and apoptosis independently of ceramide in liver cells. Am. J. Physiol. Endocrinol. Metab. 2006, 291:275-281.
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.291 , pp. 275-281
    • Wei, Y.1    Wang, D.2    Topczewski, F.3    Pagliassotti, M.J.4
  • 22
    • 84889637971 scopus 로고    scopus 로고
    • In vivo multi-tissue efficacy of peroxisome proliferator-activated receptor-gamma therapy on glucose and fatty acid metabolism in obese type 2 diabetic rats
    • Nemanich S., Rani S., Shoghi K. In vivo multi-tissue efficacy of peroxisome proliferator-activated receptor-gamma therapy on glucose and fatty acid metabolism in obese type 2 diabetic rats. Obesity (Silver Spring) 2013, 21:2522-2529.
    • (2013) Obesity (Silver Spring) , vol.21 , pp. 2522-2529
    • Nemanich, S.1    Rani, S.2    Shoghi, K.3
  • 23
    • 0842263981 scopus 로고    scopus 로고
    • The biology of peroxisome proliferator-activated receptors: relationship with lipid metabolism and insulin sensitivity
    • Ferre P. The biology of peroxisome proliferator-activated receptors: relationship with lipid metabolism and insulin sensitivity. Diabetes 2004, 53(Suppl 1):43-50.
    • (2004) Diabetes , vol.53 , pp. 43-50
    • Ferre, P.1
  • 24
    • 64249139719 scopus 로고    scopus 로고
    • PI-3 K/AKT and ERK signaling pathways mediate leptin-induced inhibition of PPARgamma gene expression in primary rat hepatic stellate cells
    • Zhou Y., Jia X., Wang G., Wang X., Liu J. PI-3 K/AKT and ERK signaling pathways mediate leptin-induced inhibition of PPARgamma gene expression in primary rat hepatic stellate cells. Mol. Cell. Biochem. 2009, 325:131-139.
    • (2009) Mol. Cell. Biochem. , vol.325 , pp. 131-139
    • Zhou, Y.1    Jia, X.2    Wang, G.3    Wang, X.4    Liu, J.5
  • 25
    • 63849189635 scopus 로고    scopus 로고
    • Inhibition of protein tyrosine phosphatase-1B with antisense oligonucleotides improves insulin sensitivity and increases adiponectin concentrations in monkeys
    • Swarbrick M.M., et al. Inhibition of protein tyrosine phosphatase-1B with antisense oligonucleotides improves insulin sensitivity and increases adiponectin concentrations in monkeys. Endocrinology 2009, 150:1670-1679.
    • (2009) Endocrinology , vol.150 , pp. 1670-1679
    • Swarbrick, M.M.1
  • 26
    • 78650262266 scopus 로고    scopus 로고
    • Insulin signaling and insulin sensitizing in muscle and liver of obese monkeys: peroxisome proliferator-activated receptor gamma agonist improves defective activation of atypical protein kinase C
    • Ortmeyer H.K., et al. Insulin signaling and insulin sensitizing in muscle and liver of obese monkeys: peroxisome proliferator-activated receptor gamma agonist improves defective activation of atypical protein kinase C. Antioxid. Redox Signal. 2011, 14:207-219.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 207-219
    • Ortmeyer, H.K.1
  • 27
    • 84857934301 scopus 로고    scopus 로고
    • Insulin regulates liver metabolism in vivo in the absence of hepatic Akt and Foxo1
    • Lu M., et al. Insulin regulates liver metabolism in vivo in the absence of hepatic Akt and Foxo1. Nat. Med. 2012, 18:388-395.
    • (2012) Nat. Med. , vol.18 , pp. 388-395
    • Lu, M.1
  • 28
    • 0034791125 scopus 로고    scopus 로고
    • Inhibition of protein kinase B (PKB) and PKCzeta mediates keratin K10-induced cell cycle arrest
    • Paramio J.M., Segrelles C., Ruiz S., Jorcano J.L. Inhibition of protein kinase B (PKB) and PKCzeta mediates keratin K10-induced cell cycle arrest. Mol. Cell. Biol. 2001, 21:7449-7459.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7449-7459
    • Paramio, J.M.1    Segrelles, C.2    Ruiz, S.3    Jorcano, J.L.4
  • 29
    • 29144492209 scopus 로고    scopus 로고
    • Involvement of the small protein tyrosine phosphatases TC-PTP and PTP1B in signal transduction and diseases: from diabetes, obesity to cell cycle, and cancer
    • Dube N., Tremblay M.L. Involvement of the small protein tyrosine phosphatases TC-PTP and PTP1B in signal transduction and diseases: from diabetes, obesity to cell cycle, and cancer. Biochim. Biophys. Acta 2005, 1754:108-117.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 108-117
    • Dube, N.1    Tremblay, M.L.2
  • 30
    • 0034054497 scopus 로고    scopus 로고
    • Dynamics of protein-tyrosine phosphatases in rat adipocytes
    • Calera M.R., Vallega G., Pilch P.F. Dynamics of protein-tyrosine phosphatases in rat adipocytes. J. Biol. Chem. 2000, 275:6308-6312.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6308-6312
    • Calera, M.R.1    Vallega, G.2    Pilch, P.F.3
  • 31
    • 2642683510 scopus 로고    scopus 로고
    • Differential regulation of insulin receptor substrates-1 and -2 (IRS-1 and IRS-2) and phosphatidylinositol 3-kinase isoforms in liver and muscle of the obese diabetic (ob/ob) mouse
    • Kerouz N.J., Horsch D., Pons S., Kahn C.R. Differential regulation of insulin receptor substrates-1 and -2 (IRS-1 and IRS-2) and phosphatidylinositol 3-kinase isoforms in liver and muscle of the obese diabetic (ob/ob) mouse. J. Clin. Invest. 1997, 100:3164-3172.
    • (1997) J. Clin. Invest. , vol.100 , pp. 3164-3172
    • Kerouz, N.J.1    Horsch, D.2    Pons, S.3    Kahn, C.R.4
  • 32
    • 0036260017 scopus 로고    scopus 로고
    • Role of the insulin receptor substrate 1 and phosphatidylinositol 3-kinase signaling pathway in insulin-induced expression of sterol regulatory element binding protein 1c and glucokinase genes in rat hepatocytes
    • Matsumoto M., Ogawa W., Teshigawara K., Inoue H., Miyake K., Sakaue H., Kasuga M. Role of the insulin receptor substrate 1 and phosphatidylinositol 3-kinase signaling pathway in insulin-induced expression of sterol regulatory element binding protein 1c and glucokinase genes in rat hepatocytes. Diabetes 2002, 51:1672-1680.
    • (2002) Diabetes , vol.51 , pp. 1672-1680
    • Matsumoto, M.1    Ogawa, W.2    Teshigawara, K.3    Inoue, H.4    Miyake, K.5    Sakaue, H.6    Kasuga, M.7
  • 33
    • 33748312093 scopus 로고    scopus 로고
    • Dual role of transcription factor FoxO1 in controlling hepatic insulin sensitivity and lipid metabolism
    • Matsumoto M., Han S., Kitamura T., Accili D. Dual role of transcription factor FoxO1 in controlling hepatic insulin sensitivity and lipid metabolism. J. Clin. Invest. 2006, 116:2464-2472.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2464-2472
    • Matsumoto, M.1    Han, S.2    Kitamura, T.3    Accili, D.4
  • 34
    • 33244472848 scopus 로고    scopus 로고
    • Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo
    • Fang J., Holmgren A. Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo. J. Am. Chem. Soc. 2006, 128:1879-1885.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1879-1885
    • Fang, J.1    Holmgren, A.2
  • 35
    • 0033531970 scopus 로고    scopus 로고
    • Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products
    • Bruns C.M., Hubatsch I., Ridderstrom M., Mannervik B., Tainer J.A. Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. J. Mol. Biol. 1999, 288:427-439.
    • (1999) J. Mol. Biol. , vol.288 , pp. 427-439
    • Bruns, C.M.1    Hubatsch, I.2    Ridderstrom, M.3    Mannervik, B.4    Tainer, J.A.5
  • 36
    • 0030052887 scopus 로고    scopus 로고
    • Lipid peroxidation contributes to hydrogen peroxide induced cytotoxicity in renal epithelial cells
    • Sheridan A.M., Fitzpatrick S., Wang C., Wheeler D.C., Lieberthal W. Lipid peroxidation contributes to hydrogen peroxide induced cytotoxicity in renal epithelial cells. Kidney Int. 1996, 49:88-93.
    • (1996) Kidney Int. , vol.49 , pp. 88-93
    • Sheridan, A.M.1    Fitzpatrick, S.2    Wang, C.3    Wheeler, D.C.4    Lieberthal, W.5
  • 37
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner E.S., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 2000, 267:6102-6109.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.