메뉴 건너뛰기




Volumn 60, Issue 4, 2012, Pages 1059-1066

Suppression of free fatty acid-induced insulin resistance by phytopolyphenols in C2C12 mouse skeletal muscle cells

Author keywords

insulin resistance; phytopolyphenols; skeletal muscle cells; type 2 diabetes

Indexed keywords

ACETYL-COA CARBOXYLASE; AKT PHOSPHORYLATION; AMP-ACTIVATED PROTEIN KINASE; CURCUMIN; ENERGY REGULATION; EPICATECHIN; EPIGALLOCATECHIN GALLATE; FREE FATTY ACID; GALLATE; GLUCOSE UPTAKE; INSULIN RECEPTOR SUBSTRATE-1; INSULIN RESISTANCE; INSULIN-STIMULATED GLUCOSE; MAPK SIGNALING; P38 MAPK; PHYTOPOLYPHENOLS; PLASMA LEVELS; POLYPHENOLS; PROTEIN KINASE C; SKELETAL MUSCLE; SKELETAL MUSCLE CELLS; TYPE 2 DIABETES MELLITUS; TYPE-2 DIABETES;

EID: 84863062486     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf204496f     Document Type: Article
Times cited : (88)

References (33)
  • 1
    • 0030748457 scopus 로고    scopus 로고
    • The insulin signaling system and the IRS proteins
    • White, M. F. The insulin signaling system and the IRS proteins Diabetologia 1997, 40 (2) S2-S17
    • (1997) Diabetologia , vol.40 , Issue.2
    • White, M.F.1
  • 2
    • 0033913213 scopus 로고    scopus 로고
    • Signaling pathways in insulin action: Molecular targets of insulin resistance
    • Pessin, J. E.; Saltiel, A. R. Signaling pathways in insulin action: molecular targets of insulin resistance J. Clin. Invest. 2000, 106 (2) 165-169 (Pubitemid 30483117)
    • (2000) Journal of Clinical Investigation , vol.106 , Issue.2 , pp. 165-169
    • Pessin, J.E.1    Saltiel, A.R.2
  • 3
    • 17044386953 scopus 로고    scopus 로고
    • Type 2 diabetes: Principles of phathogenesis and therapy
    • Stumvoll, M.; Goldstein, B. J.; van Haeften, T. W. Type 2 diabetes: principles of phathogenesis and therapy Lancet 2005, 365 (9467) 1333-1346
    • (2005) Lancet , vol.365 , Issue.9467 , pp. 1333-1346
    • Stumvoll, M.1    Goldstein, B.J.2    Van Haeften, T.W.3
  • 4
    • 0032966682 scopus 로고    scopus 로고
    • Diabetes epidemiology as a tool to trigger diabetes research and care
    • DOI 10.1007/s001250051188
    • Zimmet, P. Z. Diabetes epidemiology as a tool to trigger diabetes research and care Diabetologia 1999, 42 (5) 499-518 (Pubitemid 29195999)
    • (1999) Diabetologia , vol.42 , Issue.5 , pp. 499-518
    • Zimmet, P.Z.1
  • 5
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • DOI 10.1038/414782a
    • Zimmet, P.; Alberti, K. G.; Shaw, J. Global and societal implications of the diabetes epidemic Nature 2001, 414 (6865) 782-787 (Pubitemid 34000780)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.M.M.2    Shaw, J.3
  • 6
    • 0031014830 scopus 로고    scopus 로고
    • Role of fatty acids in the pathogenesis of insulin resistance and NIDDM
    • Boden, G. Role of fatty acids in the pathogenesis of insulin resistance and NIDDM Diabetes 1997, 46 (1) 3-10 (Pubitemid 27009941)
    • (1997) Diabetes , vol.46 , Issue.1 , pp. 3-10
    • Boden, G.1
  • 7
    • 0035082482 scopus 로고    scopus 로고
    • Effects of free fatty acids on gluconeogenesis and autoregulation of glucose production in type 2 diabetes
    • Boden, G.; Chen, X.; Capulong, E.; Mozzoli, M. Effects of free fatty acids on gluconeogenesis and autoregulation of glucose production in type 2 diabetes Diabetes 2001, 50 (4) 810-816 (Pubitemid 32242638)
    • (2001) Diabetes , vol.50 , Issue.4 , pp. 810-816
    • Boden, G.1    Chen, X.2    Capulong, E.3    Mozzoli, M.4
  • 8
    • 33745815985 scopus 로고    scopus 로고
    • AMP-activated protein kinase signaling in metabolic regulation
    • DOI 10.1172/JCI29044
    • Long, Y. C.; Zierath, J. R. AMP-activated protein kinase signaling in metabolic regulation J. Clin. Invest. 2006, 116 (7) 1776-1783 (Pubitemid 44033297)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.7 , pp. 1776-1783
    • Yun, C.L.1    Zierath, J.R.2
  • 9
    • 0029978799 scopus 로고    scopus 로고
    • Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise
    • Winder, W. W.; Hardie, D. G. Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise Am. J. Physiol. 1996, 270 (2 Part 1) E299-E304
    • (1996) Am. J. Physiol. , vol.270 , Issue.2 PART 1
    • Winder, W.W.1    Hardie, D.G.2
  • 10
    • 54549088739 scopus 로고    scopus 로고
    • Epigallocatechin gallate (EGCG) attenuates high glucose-induced insulin signaling blockade in human hepG2 hepatoma cells
    • Lin, C. L.; Lin, J. K. Epigallocatechin gallate (EGCG) attenuates high glucose-induced insulin signaling blockade in human hepG2 hepatoma cells Mol. Nutr. Food Res. 2008, 52, 930-939
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 930-939
    • Lin, C.L.1    Lin, J.K.2
  • 11
    • 70649084038 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate (EGCG) protects the insulin sensitivity in rat L6 muscle cells exposed to dexamethasone condition
    • Zhang, Z. F.; Li, Q.; Liang, J.; Dai, X. Q.; Ding, Y.; Wang, J. B.; Li, Y. Epigallocatechin-3-gallate (EGCG) protects the insulin sensitivity in rat L6 muscle cells exposed to dexamethasone condition Phytomedicine 2010, 17, 14-18
    • (2010) Phytomedicine , vol.17 , pp. 14-18
    • Zhang, Z.F.1    Li, Q.2    Liang, J.3    Dai, X.Q.4    Ding, Y.5    Wang, J.B.6    Li, Y.7
  • 12
    • 80051564679 scopus 로고    scopus 로고
    • Epigallocatechin-3-O-gallate (EGCG) attenuates FFAs-induced peripheral insulin resistance through AMPK pathway and insulin signaling pathway in vivo
    • Li, Y.; Zhao, S.; Zhang, W.; Zhao, P.; He, B.; Wu, N.; Han, P. Epigallocatechin-3-O-gallate (EGCG) attenuates FFAs-induced peripheral insulin resistance through AMPK pathway and insulin signaling pathway in vivo Diabetes Res. Clin. Pract. 2011, 93, 205-214
    • (2011) Diabetes Res. Clin. Pract. , vol.93 , pp. 205-214
    • Li, Y.1    Zhao, S.2    Zhang, W.3    Zhao, P.4    He, B.5    Wu, N.6    Han, P.7
  • 13
    • 77951931613 scopus 로고    scopus 로고
    • Epigallocatechin gallate (EGCG) and rutin suppress the glucotoxicity through activating IRS2 and AMPK signaling in rat pancreatic β cells
    • Cai, E. P.; Lin, J. K. Epigallocatechin gallate (EGCG) and rutin suppress the glucotoxicity through activating IRS2 and AMPK signaling in rat pancreatic β cells J. Agric. Food Chem. 2009, 57, 9817-9827
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 9817-9827
    • Cai, E.P.1    Lin, J.K.2
  • 14
    • 0037414811 scopus 로고    scopus 로고
    • Salicylic acid reverses PMA and TNF-alpha-induced IRS1 serine 307 phosphorylation and insulin resistance in HEK 293 cells
    • Jiang, G.; Dallas-Yang, Q.; Liu, F.; Moller, D. E.; Zhang, B. B. Salicylic acid reverses PMA and TNF-alpha-induced IRS1 serine 307 phosphorylation and insulin resistance in HEK 293 cells J. Biol. Chem. 2003, 278 (1) 180-186
    • (2003) J. Biol. Chem. , vol.278 , Issue.1 , pp. 180-186
    • Jiang, G.1    Dallas-Yang, Q.2    Liu, F.3    Moller, D.E.4    Zhang, B.B.5
  • 15
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • DOI 10.1038/414799a
    • Saltiel, A. R.; Kahn, C. R. Insulin signalling and the regulation of glucose and lipid metabolism Nature 2001, 414 (6865) 799-806 (Pubitemid 34000783)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 16
    • 33847080728 scopus 로고    scopus 로고
    • AMP-activated protein kinase in metabolic control and insulin signaling
    • Towler, M. C.; Hardie, D. G. AMP-activated protein kinase in metabolic control and insulin signaling Circ. Res. 2007, 100 (3) 328-341
    • (2007) Circ. Res. , vol.100 , Issue.3 , pp. 328-341
    • Towler, M.C.1    Hardie, D.G.2
  • 17
    • 79953221811 scopus 로고    scopus 로고
    • Counter-modulation of fatty acid-induced pro-inflammatory nuclear factor κb signalling in rat skeletal muscle cells by AMP-activated protein kinase
    • Green, C. J.; Macrae, K.; Fogarty, S.; Hardie, D. G.; Sakamoto, K.; Hundal, H. S. Counter-modulation of fatty acid-induced pro-inflammatory nuclear factor κB signalling in rat skeletal muscle cells by AMP-activated protein kinase Biochem. J. 2011, 435 (2) 463-474
    • (2011) Biochem. J. , vol.435 , Issue.2 , pp. 463-474
    • Green, C.J.1    MacRae, K.2    Fogarty, S.3    Hardie, D.G.4    Sakamoto, K.5    Hundal, H.S.6
  • 18
    • 0041413142 scopus 로고    scopus 로고
    • The AMP-activated protein kinase activator AICAR does not induce GLUT4 translocation to transverse tubules but stimulates glucose uptake and p38 mitogen-activated protein kinases α and β in skeletal muscle
    • DOI 10.1096/fj.02-1125com
    • Lemieux, K.; Konrad, D.; Klip, A.; Marette, A. The AMP-activatied protein kinase activator AICAR does not induce GLUT4 translocation to transverse tubules but stimulates glucose uptake and p38 mitogen-activated protein kinases alpha and beta in skeletal muscle FASEB J. 2003, 17 (12) 1658-1665 (Pubitemid 37100067)
    • (2003) FASEB Journal , vol.17 , Issue.12 , pp. 1658-1665
    • Lemieux, K.1    Konrad, D.2    Klip, A.3    Marette, A.4
  • 19
    • 0347721775 scopus 로고    scopus 로고
    • A dominant-negative p38 MAPK mutant and novel selective inhibitors of p38 MAPK reduce insulin-stimulated glucose uptake in 3T3-L1 adipocytes without affecting GLUT4 translocation
    • DOI 10.1074/jbc.M205277200
    • Somwar, R.; Koterski, S.; Sweeney, G.; Sciotti, R.; Djuric, S.; Berg, C.; Trevillyan, J.; Scherer, P. E.; Rondinone, C. M.; Klip, A. A dominant-negative p38 MAPK mutant and novel selective inhibitors of p38 MAPK reduce insulin-stimulated glucose uptake in 3T3L1 adipocytes without affecting GLUT4 translocation J. Biol. Chem. 2002, 277 (52) 50386-50395 (Pubitemid 36042189)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.52 , pp. 50386-50395
    • Somwar, R.1    Koterski, S.2    Sweeney, G.3    Sciotti, R.4    Djuric, S.5    Berg, C.6    Trevillyan, J.7    Scherer, P.E.8    Rondinone, C.M.9    Klip, A.10
  • 20
    • 17444434110 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase a and b by insulin and contraction in rat skeletal muscle: Potential role in the stimulation of glucose transport
    • Somwar, R.; Perreault, M.; Kapur, S.; Taha, C.; Sweeney, G.; Ramlal, T.; Kim, D. Y.; Keen, J.; Cote, C. H.; Klip, A.; Marette, A. Activation of p38 mitogen-activated protein kinase a and b by insulin and contraction in rat skeletal muscle: Potential role in the stimulation of glucose transport Diabetes 2000, 49 (11) 1794-1800
    • (2000) Diabetes , vol.49 , Issue.11 , pp. 1794-1800
    • Somwar, R.1    Perreault, M.2    Kapur, S.3    Taha, C.4    Sweeney, G.5    Ramlal, T.6    Kim, D.Y.7    Keen, J.8    Cote, C.H.9    Klip, A.10    Marette, A.11
  • 21
    • 0142056241 scopus 로고    scopus 로고
    • IRS-1 Regulation in Health and Disease
    • DOI 10.1080/1521654031000138569
    • Schmitz-Peiffer, C.; Whitehead, J. P. IRS-1 Regulation in Health and Disease IUBMB Life 2003, 55 (7) 367-374 (Pubitemid 37271094)
    • (2003) IUBMB Life , vol.55 , Issue.7 , pp. 367-374
    • Schmitz-Peiffer, C.1    Whitehead, J.P.2
  • 22
    • 33845401821 scopus 로고    scopus 로고
    • Apoptosis in skeletal muscle myotubes is induced by ceramides and is positively related to insulin resistance
    • Turpin, S. M.; Lancaster, G. I.; Darby, I.; Febbraio, M. A.; Watt, M. J. Apoptosis in skeletal muscle myotubes is induced by ceramides and is positively related to insulin resistance Am. J. Physiol. Endocrinol. Metab. 2006, 291 (6) E1341-E1350
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.291 , Issue.6
    • Turpin, S.M.1    Lancaster, G.I.2    Darby, I.3    Febbraio, M.A.4    Watt, M.J.5
  • 23
    • 33845895308 scopus 로고    scopus 로고
    • Palmitate induced mitochondrial deoxyribonucleic acid damage and apoptosis in L6 rat skeletal muscle cells
    • DOI 10.1210/en.2006-0998
    • Rachek, L. I.; Musiyenko, S. I.; LeDoux, S. P.; Wilson, G. L. Palmitate induced mitochondrial deoxyribonucleic acid damage and apoptosis in l6 rat skeletal muscle cells Endocrinology 2007, 148 (1) 293-299 (Pubitemid 46021461)
    • (2007) Endocrinology , vol.148 , Issue.1 , pp. 293-299
    • Rachek, L.I.1    Musiyenko, S.I.2    LeDoux, S.P.3    Wilson, G.L.4
  • 24
    • 0034493687 scopus 로고    scopus 로고
    • Effects of food factors on signal transduction pathways
    • Dong, Z. Effects of food factors on signal transduction pathways Biofactors 2000, 12 (1-4) 17-28 (Pubitemid 32107380)
    • (2000) BioFactors , vol.12 , Issue.1-4 , pp. 17-28
    • Dong, Z.1
  • 25
    • 0030669094 scopus 로고    scopus 로고
    • Protein kinase C modulation of insulin receptor substrate-1 tyrosine phosphorylation requires serine 612
    • DOI 10.1021/bi971157f
    • De Fea, K.; Roth, R. A. Protein kinase C modulation of insulin receptor substrate-1 tyrosine phosphorylation requires serine 612 Biochemistry 1997, 36 (42) 12939-12947 (Pubitemid 27465406)
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 12939-12947
    • De Fea, K.1    Roth, R.A.2
  • 26
    • 0036241769 scopus 로고    scopus 로고
    • Fat targets for insulin signaling
    • DOI 10.1016/S1097-2765(02)00509-9
    • Czech, M. P. Fat targets for insulin signaling Mol. Cell 2002, 9 (4) 695-696 (Pubitemid 34454879)
    • (2002) Molecular Cell , vol.9 , Issue.4 , pp. 695-696
    • Czech, M.P.1
  • 27
    • 0029049346 scopus 로고
    • High concentration of fasting plasma non-esterified fatty acids is a risk factor for the development of NIDDM
    • Paolisso, G.; Tataranni, P. A.; Foley, J. E.; Bogardus, C.; Howard, B. V.; Ravussin, E. High concentration of fasting plasma non-esterified fatty acids is a risk factor for the development of NIDDM Diabetologia 1995, 38 (10) 1213-1217
    • (1995) Diabetologia , vol.38 , Issue.10 , pp. 1213-1217
    • Paolisso, G.1    Tataranni, P.A.2    Foley, J.E.3    Bogardus, C.4    Howard, B.V.5    Ravussin, E.6
  • 28
    • 0035123649 scopus 로고    scopus 로고
    • Insulin signaling leading to proliferation, survival, and membrane ruffling in C2C12 myoblasts
    • DOI 10.1002/1097-4652(200 1)9999:9999<::AID-JCP10 58>3.0.CO;2-V
    • Conejo, R.; Lorenzo, M. Insulin signaling leading to proliferation, survival, and membrane ruffling in C2C12 myoblasts J. Cell. Physiol. 2001, 187 (1) 96-108 (Pubitemid 32195250)
    • (2001) Journal of Cellular Physiology , vol.187 , Issue.1 , pp. 96-108
    • Conejo, R.1    Lorenzo, M.2
  • 29
    • 0141434860 scopus 로고
    • Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity
    • DOI 10.1073/pnas.83.16.5822
    • Bollag, G. E.; Roth, R. A.; Beaudoin, J.; Mochly-Rosen, D.; Koshland, D. E., Jr. Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity Proc. Natl. Acad. Sci. U.S.A. 1986, 83 (16) 5822-5824 (Pubitemid 16000604)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.16 , pp. 5822-5824
    • Bollag, G.E.1    Roth, R.A.2    Beaudoin, J.3
  • 33
    • 59049095317 scopus 로고    scopus 로고
    • The potential role of green tea catechins in the prevention of the metabolic syndrome-A review
    • Thielecke, F.; Boschmann, M. The potential role of green tea catechins in the prevention of the metabolic syndrome-A review Phytochemistry 2009, 70 (1) 11-24
    • (2009) Phytochemistry , vol.70 , Issue.1 , pp. 11-24
    • Thielecke, F.1    Boschmann, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.