메뉴 건너뛰기




Volumn 152, Issue 4, 2011, Pages 1274-1283

Insulin-induced oxidative stress up-regulates heme oxygenase-1 via diverse signaling cascades in the C2 skeletal myoblast cell line

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 AMINO 7 TERT BUTYL 5 (4 CHLOROPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; HEME OXYGENASE 1; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN TYROSINE KINASE; STRESS ACTIVATED PROTEIN KINASE 1; TRANSCRIPTION FACTOR RELA;

EID: 79953202853     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2010-1319     Document Type: Article
Times cited : (14)

References (82)
  • 1
    • 0026021161 scopus 로고
    • Insulin resistance: A multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidemia, and atherosclerotic cardiovascular disease
    • DeFronzo RA, Ferrannini E 1991 Insulin resistance: a multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidemia, and atherosclerotic cardiovascular disease. Diabetes Care 14:173-194
    • (1991) Diabetes Care , vol.14 , pp. 173-194
    • DeFronzo, R.A.1    Ferrannini, E.2
  • 3
    • 63049123598 scopus 로고    scopus 로고
    • Insulin-induced NADPH oxidase activation promotes proliferation and matrix metalloproteinase activation in monocytes/macrophages
    • San José G, Bidegain J, Robador PA, Díez J, Fortuño A, Zalba G 2009 Insulin-induced NADPH oxidase activation promotes proliferation and matrix metalloproteinase activation in monocytes/macrophages. Free Rad Biol Med 46:1058-1067
    • (2009) Free Rad Biol Med , vol.46 , pp. 1058-1067
    • San José, G.1    Bidegain, J.2    Robador, P.A.3    Díez, J.4    Fortuño, A.5    Zalba, G.6
  • 5
    • 77951205104 scopus 로고    scopus 로고
    • Therapeutic targeting of signaling pathways in muscular dystrophy
    • Bhatnagar S, Kumar A 2010 Therapeutic targeting of signaling pathways in muscular dystrophy. J Mol Med 88:155-166
    • (2010) J Mol Med , vol.88 , pp. 155-166
    • Bhatnagar, S.1    Kumar, A.2
  • 6
    • 0034918907 scopus 로고    scopus 로고
    • Myogenic satellite cells: Physiology to molecular biology
    • Hawke TJ, Garry DJ 2001 Myogenic satellite cells: physiology to molecular biology. J Appl Physiol 91:534-551 (Pubitemid 32681081)
    • (2001) Journal of Applied Physiology , vol.91 , Issue.2 , pp. 534-551
    • Hawke, T.J.1    Garry, D.J.2
  • 7
    • 0017759258 scopus 로고
    • Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle
    • Yaffe D, Saxel O 1977 Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature 270:725-727 (Pubitemid 8239246)
    • (1977) Nature , vol.270 , Issue.5639 , pp. 725-727
    • Yaffe, D.1    Saxel, O.2
  • 8
    • 0036470213 scopus 로고    scopus 로고
    • Insulin signaling pathways in time and space
    • DOI 10.1016/S0962-8924(01)02207-3, PII S0962892401022073
    • Saltiel AR, Pessin JE 2002 Insulin signaling pathways in time and space. Trends Cell Biol 12:65-71 (Pubitemid 34146521)
    • (2002) Trends in Cell Biology , vol.12 , Issue.2 , pp. 65-71
    • Saltiel, A.R.1    Pessin, J.E.2
  • 10
    • 77449115115 scopus 로고    scopus 로고
    • Cluster analysis of insulin action in adipocytes reveals a key role for Akt at the plasma membrane
    • Ng G, Ramm JG, Burchfield AC, Coster J, Stockli A, James DE 2010 Cluster analysis of insulin action in adipocytes reveals a key role for Akt at the plasma membrane, J Biol Chem 285:2245-2257
    • (2010) J Biol Chem , vol.285 , pp. 2245-2257
    • Ng, G.1    Ramm, J.G.2    Burchfield, A.C.3    Coster, J.4    Stockli, A.5    James, D.E.6
  • 11
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • DOI 10.1038/414799a
    • Saltiel AR, Kahn CR 2001 Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414:799-806 (Pubitemid 34000783)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 12
    • 33645860825 scopus 로고    scopus 로고
    • Reactive oxygen species have a causal role in multiple forms of insulin resistance
    • Houstis N, Rosen ED, Lander ES 2006 Reactive oxygen species have a causal role in multiple forms of insulin resistance. Nature 440:944-948
    • (2006) Nature , vol.440 , pp. 944-948
    • Houstis, N.1    Rosen, E.D.2    Lander, E.S.3
  • 13
    • 0036796875 scopus 로고    scopus 로고
    • Oxidative stress and stress-activated signaling pathways: A unifying hypothesis of type 2 diabetes
    • DOI 10.1210/er.2001-0039
    • Evans JL, Goldfine ID, Maddux BA, Grodsky GM 2002 Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of type 2 diabetes. Endocr Rev 23:599-622 (Pubitemid 35191625)
    • (2002) Endocrine Reviews , vol.23 , Issue.5 , pp. 599-622
    • Evans, J.L.1    Goldfine, I.D.2    Maddux, B.A.3    Grodsky, G.M.4
  • 15
    • 0033590207 scopus 로고    scopus 로고
    • The role of cyclooxygenases in inflammation, cancer, and development
    • Williams CS, Mann M, DuBois RN 1999 The role of cyclooxygenases in inflammation, cancer, and development. Oncogene 18:7908-7916 (Pubitemid 30066236)
    • (1999) Oncogene , vol.18 , Issue.55 , pp. 7908-7916
    • Williams, C.S.1    Mann, M.2    DuBois, R.N.3
  • 16
    • 0026033907 scopus 로고
    • Induction of heme oxygenase: A general response to oxidant stress in cultured mammalian cells
    • Applegate LA, Luscher P, Tyrrell RM 1991 Induction of heme oxygenase: a general response to oxidant stress in cultured mammalian cells. Cancer Res 51:974-978
    • (1991) Cancer Res , vol.51 , pp. 974-978
    • Applegate, L.A.1    Luscher, P.2    Tyrrell, R.M.3
  • 17
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • DOI 10.1073/pnas.86.1.99
    • Keyse SM, Tyrrell RM 1989 Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci USA 86:99-103 (Pubitemid 19036341)
    • (1989) Proceedings of the National Academy of Sciences of the United States of America , vol.86 , Issue.1 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 19
    • 33646699095 scopus 로고    scopus 로고
    • Insulin induces heme oxygenase-1 through the phosphatidylinositol 3-kinase/Akt pathway and the Nrf2 transcription factor in renal cells
    • DOI 10.1111/j.1742-4658.2006.05224.x
    • Harrison EM, McNally SJ, Devey L, Garden OJ, Ross JA, Wigmore SJ 2006 Insulin induces heme oxygenase-1 through the phosphatidylinositol 3-kinase/Akt pathway and the Nrf2 transcription factor in renal cells. FEBS J 273:2345-2356 (Pubitemid 43736650)
    • (2006) FEBS Journal , vol.273 , Issue.11 , pp. 2345-2356
    • Harrison, E.M.1    McNally, S.J.2    Devey, L.3    Garden, O.J.4    Ross, J.A.5    Wigmore, S.J.6
  • 20
    • 79951654422 scopus 로고    scopus 로고
    • Insulin up-regulates heme oxygenase-1 expression in 3T3-L1 adipocytes via PI3-kinase- And PKC-dependent pathways and heme oxygenase-1-associated microRNA downregulation
    • Chang CL, Au LC, Huang SW, Fai Kwok C, Ho LT, Juan CC 2011 Insulin up-regulates heme oxygenase-1 expression in 3T3-L1 adipocytes via PI3-kinase- and PKC-dependent pathways and heme oxygenase-1-associated microRNA downregulation. Endocrinology 152:384-393
    • (2011) Endocrinology , vol.152 , pp. 384-393
    • Chang, C.L.1    Au, L.C.2    Huang, S.W.3    Fai Kwok, C.4    Ho, L.T.5    Juan, C.C.6
  • 21
    • 0042822096 scopus 로고    scopus 로고
    • Intramuscular heat shock protein 72 and heme oxygenase-1 mRNA are reduced in patients with type 2 diabetes: Evidence that insulin resistance is associated with a disturbed antioxidant defense mechanism
    • DOI 10.2337/diabetes.52.9.2338
    • Bruce CR, Carey AL, Hawley JA, Febbraio MA 2003 Intramuscular heat shock protein 72 and heme oxygenase-1 mRNA are reduced in patients with type 2 diabetes: evidence that insulin resistance is associated with a disturbed antioxidant defense mechanism. Diabetes 52:2338-2345 (Pubitemid 37059505)
    • (2003) Diabetes , vol.52 , Issue.9 , pp. 2338-2345
    • Bruce, C.R.1    Carey, A.L.2    Hawley, J.A.3    Febbraio, M.A.4
  • 22
    • 14244268391 scopus 로고    scopus 로고
    • Defective glucose-stimulated insulin release in the diabetic Goto-Kakizaki (GK) rat coincides with reduced activity of the islet carbon monoxide signaling pathway
    • DOI 10.1210/en.2004-0851
    • Mosén H, Salehi A, Alm P, Henningsson R, Jimenez-Feltström J, Ostenson CG, Efendic S, Lundquist I 2005 Defective glucose-stimulated insulin release in the diabetic Goto-Kakizaki (GK) rat coincides with reduced activity of the islet carbon monoxide signaling pathway. Endocrinology 146:1553-1558 (Pubitemid 40289346)
    • (2005) Endocrinology , vol.146 , Issue.3 , pp. 1553-1558
    • Mosen, H.1    Salehi, A.2    Alm, P.3    Henningsson, R.4    Jimenez-Feltstrom, J.5    Ostenson, C.-G.6    Efendic, S.7    Lundquist, I.8
  • 24
    • 41149155892 scopus 로고    scopus 로고
    • Treatment of obese diabetic mice with a heme oxygenase inducer reduces visceral and subcutaneous adiposity, increases adiponectin levels and improves insulin sensitivity and glucose tolerance
    • Li M, Kim DH, Tsenovoy PL, Peterson SJ, Rezzani R, Rodella LF, Aronow WS, Ikehara S, Abraham NG 2008 Treatment of obese diabetic mice with a heme oxygenase inducer reduces visceral and subcutaneous adiposity, increases adiponectin levels and improves insulin sensitivity and glucose tolerance. Diabetes 57:1526-1535
    • (2008) Diabetes , vol.57 , pp. 1526-1535
    • Li, M.1    Kim, D.H.2    Tsenovoy, P.L.3    Peterson, S.J.4    Rezzani, R.5    Rodella, L.F.6    Aronow, W.S.7    Ikehara, S.8    Abraham, N.G.9
  • 25
    • 65649110522 scopus 로고    scopus 로고
    • Heme oxygenase system enhances insulin sensitivity and glucose metabolism in streptozotocin-induced diabetes
    • Ndisang JF, Jadhav A 2009 Heme oxygenase system enhances insulin sensitivity and glucose metabolism in streptozotocin-induced diabetes. Am J Physiol Endocrinol Metab 296:E829-E841
    • (2009) Am J Physiol Endocrinol Metab , vol.296
    • Ndisang, J.F.1    Jadhav, A.2
  • 26
    • 66649132533 scopus 로고    scopus 로고
    • Upregulating the heme oxygenase systems enhances insulin sensitivity and improves glucose metabolism in insulin-resistant diabetes in Goto-Kakizaki rats
    • Ndisang JF, Jadhav A 2009 Upregulating the heme oxygenase systems enhances insulin sensitivity and improves glucose metabolism in insulin-resistant diabetes in Goto-Kakizaki rats. Endocrinology 150:2627-2636
    • (2009) Endocrinology , vol.150 , pp. 2627-2636
    • Ndisang, J.F.1    Jadhav, A.2
  • 27
    • 66449100734 scopus 로고    scopus 로고
    • The heme oxygenase system abates hyperglycemia in Zucker diabetic fatty rats by potentiating insulin-sensitizing pathways
    • Ndisang JF, Lane N, Jadhav A 2009 The heme oxygenase system abates hyperglycemia in Zucker diabetic fatty rats by potentiating insulin-sensitizing pathways. Endocrinology 150:2098-2108
    • (2009) Endocrinology , vol.150 , pp. 2098-2108
    • Ndisang, J.F.1    Lane, N.2    Jadhav, A.3
  • 28
    • 33747080587 scopus 로고    scopus 로고
    • 2-induced upregulation of heme oxygenase-1 mRNA in H9c2 cells
    • DOI 10.1016/j.cellsig.2006.02.001, PII S0898656806000350
    • Aggeli IK, Gaitanaki C, Beis I 2006 Involvement of JNK1/2 and p38-MAPK/MSK1 pathways in H2O2-induced upregulation of heme oxygenase-1 mRNA in H9c2 cells. Cell Signal 18:1801-1812 (Pubitemid 44216133)
    • (2006) Cellular Signalling , vol.18 , Issue.10 , pp. 1801-1812
    • Aggeli, I.-K.S.1    Gaitanaki, C.2    Beis, I.3
  • 30
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • DOI 10.1074/jbc.271.40.24313
    • Kyriakis JM, Avruch J 1996 Sounding the alarm: protein kinase cascades activated by stress and inflammation. J Biol Chem 271:24313-24316 (Pubitemid 26333156)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.40 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 32
    • 0034701113 scopus 로고    scopus 로고
    • Age-dependent increase of heme oxygenase-1 gene expression in the liver mediated by NFκB
    • DOI 10.1016/S0047-6374(00)00087-7, PII S0047637400000877
    • Lavrovsky Y, Song CS, Chatterjee B, Roy AK 2000 Age-dependent increase of heme oxygenase 1 gene expression in the liver mediated by NF-κB. Mech Age Dev 114:49-60 (Pubitemid 30154167)
    • (2000) Mechanisms of Ageing and Development , vol.114 , Issue.1 , pp. 49-60
    • Lavrovsky, Y.1    Song, C.S.2    Chatterjee, B.3    Roy, A.K.4
  • 33
    • 0028039868 scopus 로고
    • Isolation and characterization of the mouse heme oxygenase-1 gene. Distal 5′ sequences are required for induction by heme or heavy metals
    • Alam J, Cai J, Smith A 1994 Isolation and characterization of the mouse heme oxygenase-1 gene. Distal 5′ sequences are required for induction by heme or heavy metals. J Biol Chem 269:1001-1009
    • (1994) J Biol Chem , vol.269 , pp. 1001-1009
    • Alam, J.1    Cai, J.2    Smith, A.3
  • 35
    • 77953565932 scopus 로고    scopus 로고
    • HOX-1 and COX-2: Two differentially regulated key mediators of skeletal myoblast tolerance under oxidative stress
    • Aggeli IK, Kefaloyianni E, Beis I, Gaitanaki C 2010 HOX-1 and COX-2: two differentially regulated key mediators of skeletal myoblast tolerance under oxidative stress. Free Radic Res 44:679-693
    • (2010) Free Radic Res , vol.44 , pp. 679-693
    • Aggeli, I.K.1    Kefaloyianni, E.2    Beis, I.3    Gaitanaki, C.4
  • 36
    • 2942562273 scopus 로고    scopus 로고
    • Evidence for contribution of vascular NAD(P)H oxidase to increased oxidative stress in animal models of diabetes and obesity
    • DOI 10.1016/j.freeradbiomed.2004.04.001, PII S0891584904003041
    • Sonta T, Inoguchi T, Tsubouchi H, Sekiguchi N, Kobayashi K, Matsumoto S, Utsumi H, Nawata H 2004 Evidence for contribution of vascular NAD(P)H oxidase to increased oxidative stress in animal models of diabetes and obesity. Free Radic Biol Med 37:115-123 (Pubitemid 38746655)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.1 , pp. 115-123
    • Sonta, T.1    Inoguchi, T.2    Tsubouchi, H.3    Sekiguchi, N.4    Kobayashi, K.5    Matsumoto, S.6    Utsumi, H.7    Nawata, H.8
  • 37
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • Griendling KK, Sorescu D, Ushio-Fukai M 2000 NAD(P)H oxidase: role in cardiovascular biology and disease. Circ Res 86:494-501 (Pubitemid 30165039)
    • (2000) Circulation Research , vol.86 , Issue.5 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 38
    • 0030894971 scopus 로고    scopus 로고
    • 2 generation in human adipocyte plasma membranes is mediated by Gαi2
    • 2 generation in human adipocyte plasma membranes is mediated by Gαi2. J Biol Chem 272:10135-10143
    • (1997) J Biol Chem , vol.272 , pp. 10135-10143
    • Krieger-Brauer, H.I.1    Medda, P.K.2    Kather, H.3
  • 40
    • 33751002989 scopus 로고    scopus 로고
    • ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-κB transactivation during oxidative stress in skeletal myoblasts
    • DOI 10.1016/j.cellsig.2006.05.004, PII S0898656806001100
    • Kefaloyianni E, Gaitanaki C, Beis I 2006 ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-κB transactivation during oxidative stress in skeletal myoblasts. Cell Signal 18:2238-2251 (Pubitemid 44740489)
    • (2006) Cellular Signalling , vol.18 , Issue.12 , pp. 2238-2251
    • Kefaloyianni, E.1    Gaitanaki, C.2    Beis, I.3
  • 41
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T 1983 Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65:55-63 (Pubitemid 14203433)
    • (1983) Journal of Immunological Methods , vol.65 , Issue.1-2 , pp. 55-63
    • Mosmann, T.1
  • 42
    • 0842308157 scopus 로고    scopus 로고
    • Enhancement of chemotherapeutic response of tumor cells by a heme oxygenase inhibitor, pegylated zinc protoporphyrin
    • DOI 10.1002/ijc.11644
    • Fang J, Sawa T, Akaike T, Greish K, Maeda H 2004 Enhancement of chemotherapeutic response of tumor cells by a heme oxygenase inhibitor, pegylated zinc protoporphyrin. Int J Cancer 109:1-8 (Pubitemid 38165358)
    • (2004) International Journal of Cancer , vol.109 , Issue.1 , pp. 1-8
    • Fang, J.1    Sawa, T.2    Akaike, T.3    Greish, K.4    Maeda, H.5
  • 43
    • 0021108041 scopus 로고
    • Hormone-responsive myofibrillar protease activity in cultured rat myoblasts
    • Mayer M, Chaouat M, Lernau OZ, Nissan S 1983 Hormone-responsive myofibrillar protease activity in cultured rat myoblasts. FEBS Lett 161:239-242
    • (1983) FEBS Lett , vol.161 , pp. 239-242
    • Mayer, M.1    Chaouat, M.2    Lernau, O.Z.3    Nissan, S.4
  • 44
    • 0028867742 scopus 로고
    • Activation of transcription factor NF-κB is suppressed by curcumin (diferuloymethane)
    • Singh S, Aggarwal BB 1995 Activation of transcription factor NF-κB is suppressed by curcumin (diferuloymethane). J Biol Chem 270:24995-25000
    • (1995) J Biol Chem , vol.270 , pp. 24995-25000
    • Singh, S.1    Aggarwal, B.B.2
  • 45
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • DOI 10.1146/annurev.immunol.18.1.621
    • Karin M, Ben-Neriah Y 2000 Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu Rev Immunol 18:621-663 (Pubitemid 30365393)
    • (2000) Annual Review of Immunology , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 46
    • 77953527349 scopus 로고    scopus 로고
    • Role of heme oxygenase in inflammation, insulin-signalling, diabetes and obesity
    • Ndisang JF 2010 Role of heme oxygenase in inflammation, insulin-signalling, diabetes and obesity. Mediators Inflamm 2010:359732
    • (2010) Mediators Inflamm , vol.2010 , pp. 359732
    • Ndisang, J.F.1
  • 47
    • 18744368158 scopus 로고    scopus 로고
    • Heme oxygenase overexpression attenuates glucose-mediated oxidative stress in quiescent cell phase: Linking heme to hyperglycemia complications
    • DOI 10.2174/1567202053586802
    • Sacerdoti D, Olszanecki R, Li Volti G, Colombrita C, Scapagnini G, Abraham NG 2005 Hemeoxygenase overexpression attenuates glucose- mediated oxidative stress in quiescent cell phase: linking heme to hyperglycemia complications. Curr Neurovasc Res 2:103-111 (Pubitemid 40676618)
    • (2005) Current Neurovascular Research , vol.2 , Issue.2 , pp. 103-111
    • Sacerdoti, D.1    Olszanecki, R.2    Li, V.G.3    Colombrita, C.4    Scapagnini, G.5    Abraham, N.G.6
  • 50
    • 79551470306 scopus 로고    scopus 로고
    • Oxidative stress, insulin signaling, and diabetes
    • Rains JL, Jain SK 2011 Oxidative stress, insulin signaling, and diabetes. Free Radic Biol Med 50:567-575
    • (2011) Free Radic Biol Med , vol.50 , pp. 567-575
    • Rains, J.L.1    Jain, S.K.2
  • 51
    • 17644399404 scopus 로고    scopus 로고
    • Role of insulin-induced reactive oxygen species in the insulin signaling pathway
    • DOI 10.1089/ars.2005.7.1021
    • Goldstein BJ, Mahadev K, Wu X, Zhu L, Motoshima H 2005 Role of insulin-induced reactive oxygen species in the insulin signaling pathway. Antioxid Redox Signal 7:1021-1031 (Pubitemid 40973798)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.7-8 , pp. 1021-1031
    • Goldstein, B.J.1    Mahadev, K.2    Wu, X.3    Zhu, L.4    Motoshima, H.5
  • 53
    • 0026572097 scopus 로고
    • 2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase
    • 2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase. J Clin Invest 89:1006-1013
    • (1992) J Clin Invest , vol.89 , pp. 1006-1013
    • Krieger-Brauer, H.I.1    Kather, H.2
  • 54
    • 2342625311 scopus 로고    scopus 로고
    • Insulin Generates Free Radicals by an NAD(P)H, Phosphatidylinositol 3′-Kinase-Dependent Mechanism in Human Skin Fibroblasts Ex Vivo
    • DOI 10.2337/diabetes.53.5.1344
    • Ceolotto G, Bevilacqua M, Papparella I, Baritono E, Franco L, Corvaja C, Mazzoni M, Semplicini A, Avogaro A 2004 Insulin generates free radicals by an NAD(P)H, phosphatidylinositol 3′-kinase-dependent mechanism in human skin fibroblasts ex vivo. Diabetes 53:1344-1351 (Pubitemid 38569022)
    • (2004) Diabetes , vol.53 , Issue.5 , pp. 1344-1351
    • Ceolotto, G.1    Bevilacqua, M.2    Papparella, I.3    Baritono, E.4    Franco, L.5    Corvaja, C.6    Mazzoni, M.7    Semplicini, A.8    Avogaro, A.9
  • 55
    • 0032867462 scopus 로고    scopus 로고
    • Phosphorylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide: The structural basis of redox priming
    • Schmid E, Hotz-Wagenblatt A, Hacj V, Dröge W 1999 Phosphorylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide: the structural basis of redox priming. FASEB J 13:1491-1500 (Pubitemid 29411781)
    • (1999) FASEB Journal , vol.13 , Issue.12 , pp. 1491-1500
    • Schmid, E.1    Hotz-Wagenblatt, A.2    Hack, V.3    Droge, W.4
  • 56
    • 77957657096 scopus 로고    scopus 로고
    • In vivo differential effects of fasting, re-feeding, insulin and insulin stimulation time course on insulin signaling pathway components in peripheral tissues
    • Agouni A, Owen C, Czopek A, Mody N, Delibegovic M 2010 In vivo differential effects of fasting, re-feeding, insulin and insulin stimulation time course on insulin signaling pathway components in peripheral tissues. Biochem Biophys Res Commun 401:104-111
    • (2010) Biochem Biophys Res Commun , vol.401 , pp. 104-111
    • Agouni, A.1    Owen, C.2    Czopek, A.3    Mody, N.4    Delibegovic, M.5
  • 57
    • 0034705239 scopus 로고    scopus 로고
    • Regulation of protien kinase B and 4E-BP1 by oxidative stress in cardiac myocytes
    • Pham FH, Sugden PH, Clerk A 2000 Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes. Circ Res 86:1252-1258 (Pubitemid 30436666)
    • (2000) Circulation Research , vol.86 , Issue.12 , pp. 1252-1258
    • Pham, F.H.1    Sugden, P.H.2    Clerk, A.3
  • 58
    • 27344448911 scopus 로고    scopus 로고
    • Peptide growth factors signal differentially through protein kinase C to extracellular signal-regulated kinases in neonatal cardiomyocytes
    • DOI 10.1016/j.cellsig.2005.04.005, PII S0898656805000860
    • Clerk A, Aggeli IK, Stathopoulou K, Sugden PH 2006 Peptide growth factors signal differentially through protein kinase C to extracellular signal-regulated kinases in neonatal cardiomyocytes. Cell Signal 18:225-235 (Pubitemid 41527166)
    • (2006) Cellular Signalling , vol.18 , Issue.2 , pp. 225-235
    • Clerk, A.1    Aggeli, I.-K.S.2    Stathopoulou, K.3    Sugden, P.H.4
  • 60
    • 41149177025 scopus 로고    scopus 로고
    • Pharmacological and clinical aspects of heme oxygenase
    • DOI 10.1124/pr.107.07104
    • Abraham NG, Kappas A 2008 Pharmacological and clinical aspects of heme oxygenase. Pharmacol Rev 60:79-127 (Pubitemid 351439218)
    • (2008) Pharmacological Reviews , vol.60 , Issue.1 , pp. 79-127
    • Abraham, N.G.1    Kappas, A.2
  • 61
    • 44249095590 scopus 로고    scopus 로고
    • Heme oxygenase-mediated increases in adiponectin decrease fat content and inflammatory cytokines tumor necrosis factor-α and interleukin-6 in Zucker rats and reduce adipogenesis in human mesenchymal stem cells
    • DOI 10.1124/jpet.107.135285
    • Kim DH, Burgess AP, Li M, Tsenovoy PL, Addabbo F, McClung JA, Puri N, Abraham NG 2008 Heme oxygenase-mediated increases in adiponectin decrease fat content and inflammatory cytokines tumor necrosis factor-α and interleukin-6 in Zucker rats and reduce adipogenesis in human mesenchymal stem cells. J Pharmacol Exp Ther 325:833-840 (Pubitemid 351724315)
    • (2008) Journal of Pharmacology and Experimental Therapeutics , vol.325 , Issue.3 , pp. 833-840
    • Dong, H.K.1    Burgess, A.P.2    Li, M.3    Tsenovoy, P.L.4    Addabbo, F.5    McClung, J.A.6    Puri, N.7    Abraham, N.G.8
  • 63
    • 74949102157 scopus 로고    scopus 로고
    • Up-regulating the heme oxygenase system with hemin improves insulin sensitivity and glucose metabolism in adult spontaneously hypertensive rats
    • Ndisang JF, Lane N, Syed N, Jadhav A 2010 Up-regulating the heme oxygenase system with hemin improves insulin sensitivity and glucose metabolism in adult spontaneously hypertensive rats. Endocrinology 151:549-560
    • (2010) Endocrinology , vol.151 , pp. 549-560
    • Ndisang, J.F.1    Lane, N.2    Syed, N.3    Jadhav, A.4
  • 65
    • 33746629383 scopus 로고    scopus 로고
    • The role of c-Jun N-terminal kinase, p38, and extracellular signal-regulated kinase in insulin-induced Thr69 and Thr71 phosphorylation of activating transcription factor 2
    • DOI 10.1210/me.2005-0289
    • Baan B, van Dam H, van der Zon GC, Maassen JA, Ouwens DM 2006 The role of c-Jun N-terminal kinase, p38, and extracellular signal-regulated kinase in insulin-induced Thr69 and Thr71 phosphorylation of activating transcription factor 2. Mol Endocrinol 20:1786-1795 (Pubitemid 44148084)
    • (2006) Molecular Endocrinology , vol.20 , Issue.8 , pp. 1786-1795
    • Baan, B.1    Van Dam, H.2    Van Der, Z.G.C.M.3    Maassen, J.A.4    Ouwens, D.M.5
  • 67
    • 0034465475 scopus 로고    scopus 로고
    • Insulin-mediated cell proliferation and survival involve inhibition of c-Jun N-terminal kinases through a phosphatidylinositol 3-kinase- And mitogen-activated protein kinase phosphatase-1-dependent pathway
    • DOI 10.1210/en.141.3.922
    • Desbois-Mouthon C, Cadoret A, Blivet-Van Eggelpoël MJ, Bertrand F, Caron M, Atfi A, Cherqui G, Capeau J 2000 Insulin-mediated cell proliferation and survival involve inhibition of c-Jun Nterminal kinases through a phosphatidylinositol 3-kinase- and mitogen-activated protein kinase phosphatase-1-dependent pathway. Endocrinology 141:922-931 (Pubitemid 32260434)
    • (2000) Endocrinology , vol.141 , Issue.3 , pp. 922-931
    • Desbois-Mouthon, C.1    Cadoret, A.2    Blivet-Van, E.M.-J.3    Bertrand, F.4    Caron, M.5    Atfi, A.6    Cherqui, G.7    Capeau, J.8
  • 68
    • 65249157982 scopus 로고    scopus 로고
    • Eupatilin with heme oxygenase-1-inducing ability protects cultured feline esophageal epithelial cells from cell damage caused by indomethacin
    • Song HJ, Shin CY, Oh TY, Min YS, Park ES, Sohn UD 2009 Eupatilin with heme oxygenase-1-inducing ability protects cultured feline esophageal epithelial cells from cell damage caused by indomethacin. Biol Pharm Bull 32:589-596
    • (2009) Biol Pharm Bull , vol.32 , pp. 589-596
    • Song, H.J.1    Shin, C.Y.2    Oh, T.Y.3    Min, Y.S.4    Park, E.S.5    Sohn, U.D.6
  • 69
    • 39749124150 scopus 로고    scopus 로고
    • Cytotoxic effects of metal protoporphyrins in glioblastoma cells: Roles of albumin, reactive oxygen species, and heme oxygenase-1
    • Chow JM, Huang GC, Lin HY, Shen SC, Yang LY, Chen YC 2008 Cytotoxic effects of metal protoporphyrins in glioblastoma cells: roles of albumin, reactive oxygen species, and heme oxygenase-1. Toxicol Lett 177:97-107
    • (2008) Toxicol Lett , vol.177 , pp. 97-107
    • Chow, J.M.1    Huang, G.C.2    Lin, H.Y.3    Shen, S.C.4    Yang, L.Y.5    Chen, Y.C.6
  • 70
    • 77951938000 scopus 로고    scopus 로고
    • Cigarette smoke particle-phase extract induces HO-1 expression in human tracheal smooth muscle cells: Role of c-Src/NADPH oxidase/MAPK/Nrf2 signaling pathway
    • Cheng SE, Lee IT, Lin CC, Kou YR, Yang CM 2010 Cigarette smoke particle-phase extract induces HO-1 expression in human tracheal smooth muscle cells: role of c-Src/NADPH oxidase/MAPK/Nrf2 signaling pathway. Free Radic Biol Med 48:1410-1422
    • (2010) Free Radic Biol Med , vol.48 , pp. 1410-1422
    • Cheng, S.E.1    Lee, I.T.2    Lin, C.C.3    Kou, Y.R.4    Yang, C.M.5
  • 71
    • 20444459893 scopus 로고    scopus 로고
    • Heme oxygenase-1 gene activation by the NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride via a protein kinase B, p38-dependent signaling pathway in monocytes
    • DOI 10.1074/jbc.M502943200
    • Wijayanti N, Kietzmann T, Immenschuh S 2005 Heme oxygenase-1 gene activation by the NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride via a protein kinase B, p38-dependent signaling pathway in monocytes. J Biol Chem 280:21820-21829 (Pubitemid 40827832)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 21820-21829
    • Wijayanti, N.1    Kietzmann, T.2    Immenschuh, S.3
  • 72
    • 58149279843 scopus 로고    scopus 로고
    • Lipoteichoic acid induces HO-1 expression via the TLR2/ MyD88/c-Src/NADPH oxidase pathway and Nrf2 in human tracheal smooth muscle cells
    • Lee IT, Wang SW, Lee CW, Chang CC, Lin CC, Luo SF, Yang CM 2008 Lipoteichoic acid induces HO-1 expression via the TLR2/ MyD88/c-Src/NADPH oxidase pathway and Nrf2 in human tracheal smooth muscle cells. J Immunol 181:5098-5110
    • (2008) J Immunol , vol.181 , pp. 5098-5110
    • Lee, I.T.1    Wang, S.W.2    Lee, C.W.3    Chang, C.C.4    Lin, C.C.5    Luo, S.F.6    Yang, C.M.7
  • 73
    • 77957850108 scopus 로고    scopus 로고
    • Cigarette smoke extract induces HO-1 expression in mouse cerebral vascular endothelial cells: Involvement of c-Src/ NADPH oxidase/PDGFR/ JAK2/STAT3 pathway
    • Shih RH, Lee IT, Hsieh HL, Kou YR, Yang CM 2010 Cigarette smoke extract induces HO-1 expression in mouse cerebral vascular endothelial cells: involvement of c-Src/ NADPH oxidase/PDGFR/ JAK2/STAT3 pathway. J Cell Physiol 225:741-750
    • (2010) J Cell Physiol , vol.225 , pp. 741-750
    • Shih, R.H.1    Lee, I.T.2    Hsieh, H.L.3    Kou, Y.R.4    Yang, C.M.5
  • 76
    • 33646730760 scopus 로고    scopus 로고
    • Antitumor action of curcumin in human papillomavirus associated cells involves downregulation of viral oncogenes, prevention of NFκB and AP-1 translocation, and modulation of apoptosis
    • Divya CS, Pillai MR 2006 Antitumor action of curcumin in human papillomavirus associated cells involves downregulation of viral oncogenes, prevention of NFκB and AP-1 translocation, and modulation of apoptosis. Mol Carcinog 45:320-332
    • (2006) Mol Carcinog , vol.45 , pp. 320-332
    • Divya, C.S.1    Pillai, M.R.2
  • 77
    • 79251555694 scopus 로고    scopus 로고
    • Decreased exercise-induced expression of NF-κB regulated genes in muscle of COPD patients
    • Mercken EM, Hageman GJ, Langen RC, Wouters EF, Schols AM 2010 Decreased exercise-induced expression of NF-κB regulated genes in muscle of COPD patients. Chest [http:// www.ncbi.nlm.nih.gov/pubmed/20688919]
    • (2010) Chest
    • Mercken, E.M.1    Hageman, G.J.2    Langen, R.C.3    Wouters, E.F.4    Schols, A.M.5
  • 79
    • 0035282213 scopus 로고    scopus 로고
    • IκB-independent control of NF-κB activity by modulatory phosphorylations
    • DOI 10.1016/S0968-0004(00)01753-9, PII S0968000400017539
    • Schmitz ML, Bacher S, Kracht M 2001 IκB-independent control of NF-κB activity by modulatory phosphorylations. Trends Biochem Sci 26:186-190 (Pubitemid 32197579)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.3 , pp. 186-190
    • Schmitz, M.L.1    Bacher, S.2    Kracht, M.3
  • 80
    • 0036710479 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of the nuclear factor-κB p65 subunit
    • DOI 10.1016/S0006-2952(02)01161-9, PII S0006295202011619
    • Vermeulen L, De Wilde G, Notebaert S, Vanden Berghe W, Haegeman G 2002 Regulation of the transcriptional activity of the nuclear factor-κB p65 subunit. Biochem Pharmacol 64:963-970 (Pubitemid 35232270)
    • (2002) Biochemical Pharmacology , vol.64 , Issue.5-6 , pp. 963-970
    • Vermeulen, L.1    De Wilde, G.2    Notebaert, S.3    Vanden, B.W.4    Haegeman, G.5
  • 81
    • 34249941912 scopus 로고    scopus 로고
    • A transmembrane osteoclastic protein-tyrosine phosphatase regulates osteoclast activity in part by promoting osteoclast survival through c-Src-dependent activation of NFκB and JNK2
    • DOI 10.1016/j.abb.2007.02.025, PII S0003986107000999
    • Amoui M, Sheng MH, Chen ST, Baylink DJ, Lau KH 2007 A transmembrane osteoclastic protein-tyrosine phosphatase regulates osteoclast activity in part by promoting osteoclast survival through c-Src-dependent activation of NFκB and JNK2. Arch Biochem Biophys 463:47-59 (Pubitemid 46879704)
    • (2007) Archives of Biochemistry and Biophysics , vol.463 , Issue.1 , pp. 47-59
    • Amoui, M.1    Sheng, M.H.-C.2    Chen, S.-T.3    Baylink, D.J.4    Lau, K.-H.W.5
  • 82
    • 11144230328 scopus 로고    scopus 로고
    • 1 receptor involves c-Src, protein kinase C, and ERK signaling
    • DOI 10.1074/jbc.M410196200
    • Liu AM, Wong YH 2004 G16-mediated activation of nuclear factor κB by the adenosine A1 receptor involves c-Src, protein kinase C, and ERK signaling. J Biol Chem 279:53196-53204 (Pubitemid 40051822)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53196-53204
    • Liu, A.M.F.1    Wong, Y.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.