메뉴 건너뛰기




Volumn 36, Issue 1, 2009, Pages 60-69

Resistin induces insulin resistance by both AMPK-dependent and AMPK-independent mechanisms in HepG2 cells

Author keywords

AMPK; Diabetes; HepG2; Insulin; Resistin; SiRNA

Indexed keywords

ANTIDIABETIC AGENT; GLUCOSE 6 PHOSPHATASE; GLUCOSE TRANSPORTER 2; GLYCOGEN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; INSULIN; INSULIN RECEPTOR SUBSTRATE; IRS2 PROTEIN, HUMAN; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PRKAA2 PROTEIN, HUMAN; PROTEIN KINASE B; RESISTIN; RETN PROTEIN, HUMAN; SACCHARIC ACID; SLC2A2 PROTEIN, HUMAN; SMALL INTERFERING RNA; SOCS3 PROTEIN, HUMAN; SUPPRESSOR OF CYTOKINE SIGNALING;

EID: 70349570571     PISSN: 1355008X     EISSN: 15590100     Source Type: Journal    
DOI: 10.1007/s12020-009-9198-7     Document Type: Article
Times cited : (77)

References (50)
  • 1
    • 0033849777 scopus 로고    scopus 로고
    • Obesity and insulin resistance
    • B.B. Kahn, J.S. Flier, Obesity and insulin resistance. J. Clin. Invest. 106, 473-481 (2000)
    • (2000) J. Clin. Invest. , vol.106 , pp. 473-481
    • Kahn, B.B.1    Flier, J.S.2
  • 2
    • 0842324779 scopus 로고    scopus 로고
    • Obesity wars: Molecular progress confronts an expanding epidemic
    • J.S. Flier, Obesity wars: Molecular progress confronts an expanding epidemic. Cell 116, 337-350 (2004)
    • (2004) Cell , vol.116 , pp. 337-350
    • Flier, J.S.1
  • 4
    • 0034890103 scopus 로고    scopus 로고
    • Physiological role of adipose tissue: White adipose tissue as an endocrine and secretory organ
    • P. Trayhurn, J.H. Beattie, Physiological role of adipose tissue: White adipose tissue as an endocrine and secretory organ. Proc. Nutr. Soc. 60, 329-339 (2001)
    • (2001) Proc. Nutr. Soc. , vol.60 , pp. 329-339
    • Trayhurn, P.1    Beattie, J.H.2
  • 6
    • 0035815608 scopus 로고    scopus 로고
    • A cysteine-rich adipose tissue-specific secretory factor inhibits adipocyte differentiation
    • K.H. Kim, K. Lee, Y.S. Moon, H.S. Sul, A cysteine-rich adipose tissue-specific secretory factor inhibits adipocyte differentiation. J. Biol. Chem. 276, 11252-11256 (2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 11252-11256
    • Kim, K.H.1    Lee, K.2    Moon, Y.S.3    Sul, H.S.4
  • 11
    • 0038692862 scopus 로고    scopus 로고
    • A promoter genotype and oxidative stress potentially link resistin to human insulin resistance
    • S.R. Smith, F. Bai, C. Charbonneau, L. Janderova, G. Argyropoulos, A promoter genotype and oxidative stress potentially link resistin to human insulin resistance. Diabetes 52, 1611-1618 (2003)
    • (2003) Diabetes , vol.52 , pp. 1611-1618
    • Smith, S.R.1    Bai, F.2    Charbonneau, C.3    Janderova, L.4    Argyropoulos, G.5
  • 12
    • 0242320395 scopus 로고    scopus 로고
    • Circulating resistin levels are not associated with obesity or insulin resistance in humans and are not regulated by fasting or leptin administration: Cross-sectional and interventional studies in normal, insulinresistant, and diabetic subjects
    • J.H. Lee, J.L. Chan, N. Yiannakouris, M. Kontogianni, E. Estrada, R. Seip, C. Orlova, C.S. Mantzoros, Circulating resistin levels are not associated with obesity or insulin resistance in humans and are not regulated by fasting or leptin administration: Cross-sectional and interventional studies in normal, insulinresistant, and diabetic subjects. J. Clin. Endocrinol. Metab. 88, 4848-4856 (2003)
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 4848-4856
    • Lee, J.H.1    Chan, J.L.2    Yiannakouris, N.3    Kontogianni, M.4    Estrada, E.5    Seip, R.6    Orlova, C.7    Mantzoros, C.S.8
  • 13
  • 14
    • 0037434632 scopus 로고    scopus 로고
    • The genomic organization of mouse resistin reveals major differences from the human resistin: Functional implications
    • S. Ghosh, A.K. Singh, B. Aruna, S. Mukhopadhyay, N.Z. Ehtesham, The genomic organization of mouse resistin reveals major differences from the human resistin: Functional implications. Gene. 305, 27-34 (2003)
    • (2003) Gene. , vol.305 , pp. 27-34
    • Ghosh, S.1    Singh, A.K.2    Aruna, B.3    Mukhopadhyay, S.4    Ehtesham, N.Z.5
  • 15
    • 0034806403 scopus 로고    scopus 로고
    • Insulin resistance and type 2 diabetes are not related to resistin expression in human fat cells or skeletal muscle
    • I. Nagaev, U. Smith, Insulin resistance and type 2 diabetes are not related to resistin expression in human fat cells or skeletal muscle. Biochem. Biophys. Res. Commun. 285, 561-564 (2001)
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 561-564
    • Nagaev, I.1    Smith, U.2
  • 17
    • 10944247187 scopus 로고    scopus 로고
    • The AMP-activated protein kinase pathway-new players upstream and downstream
    • D.G. Hardie, The AMP-activated protein kinase pathway-new players upstream and downstream. J. Cell Sci. 117, 5479-5487 (2004)
    • (2004) J. Cell Sci. , vol.117 , pp. 5479-5487
    • Hardie, D.G.1
  • 18
    • 0347318052 scopus 로고    scopus 로고
    • The AMP-activated protein kinase cascade-A unifying system for energy control
    • D. Carling, The AMP-activated protein kinase cascade-a unifying system for energy control. Trends Biochem. Sci. 29, 18-24 (2004)
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 18-24
    • Carling, D.1
  • 23
    • 33745815985 scopus 로고    scopus 로고
    • AMP-activated protein kinase signaling in metabolic regulation
    • Y.C. Long, J.R. Zierath, AMP-activated protein kinase signaling in metabolic regulation. J. Clin. Invest. 116, 1776-1783 (2006)
    • (2006) J. Clin. Invest. , vol.116 , pp. 1776-1783
    • Long, Y.C.1    Zierath, J.R.2
  • 24
    • 33646142778 scopus 로고    scopus 로고
    • Glucose-induced repression of PPARalpha gene expression in pancreatic beta-cells involves PP2A activation and AMPK inactivation
    • K. Ravnskjaer, M. Boergesen, L.T. Dalgaard, S. Mandrup, Glucose-induced repression of PPARalpha gene expression in pancreatic beta-cells involves PP2A activation and AMPK inactivation. J. Mol. Endocrinol. 36, 289-299 (2006)
    • (2006) J. Mol. Endocrinol. , vol.36 , pp. 289-299
    • Ravnskjaer, K.1    Boergesen, M.2    Dalgaard, L.T.3    Mandrup, S.4
  • 25
    • 0032497842 scopus 로고    scopus 로고
    • The role of PI 3-kinase in insulin action
    • D.R. Alessi, C.P. Downes, The role of PI 3-kinase in insulin action. Biochim. Biophys. Acta 1436, 151-164 (1998)
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 151-164
    • Alessi, D.R.1    Downes, C.P.2
  • 26
    • 0032189381 scopus 로고    scopus 로고
    • Protein kinase B (c-Akt): A multifunctional mediator of phosphatidylinositol 3-kinase activation
    • P.J. Coffer, J. Jin, J.R. Woodgett, Protein kinase B (c-Akt): A multifunctional mediator of phosphatidylinositol 3-kinase activation. Biochem. J. 335(Pt 1), 1-13 (1998)
    • (1998) Biochem. J. , vol.335 , Issue.PART 1 , pp. 1-13
    • Coffer, P.J.1    Jin, J.2    Woodgett, J.R.3
  • 27
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • L.C. Cantley, The phosphoinositide 3-kinase pathway. Science 296, 1655-1657 (2002)
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 28
    • 0030841793 scopus 로고    scopus 로고
    • PDK1, one of the missing links in insulin signal transduction?
    • P. Cohen, D.R. Alessi, D.A. Cross, PDK1, one of the missing links in insulin signal transduction? FEBS Lett. 410, 3-10 (1997)
    • (1997) FEBS Lett. , vol.410 , pp. 3-10
    • Cohen, P.1    Alessi, D.R.2    Cross, D.A.3
  • 29
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • S.R. Datta, A. Brunet, M.E. Greenberg, Cellular survival: A play in three Akts. Genes Dev. 13, 2905-2927 (1999)
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 31
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • B.D. Manning, L.C. Cantley, AKT/PKB signaling: Navigating downstream. Cell 129, 1261-1274 (2007)
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 32
    • 9144244927 scopus 로고    scopus 로고
    • Resistin and type 2 diabetes: Regulation of resistin expression by insulin and rosiglitazone and the effects of recombinant resistin on lipid and glucose metabolism in human differentiated adipocytes
    • P.G. McTernan, F.M. Fisher, G. Valsamakis, R. Chetty, A. Harte, C.L. McTernan, P.M. Clark, S.A. Smith, A.H. Barnett, S. Kumar, Resistin and type 2 diabetes: Regulation of resistin expression by insulin and rosiglitazone and the effects of recombinant resistin on lipid and glucose metabolism in human differentiated adipocytes. J. Clin. Endocrinol. Metab. 88, 6098-6106 (2003)
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 6098-6106
    • McTernan, P.G.1    Fisher, F.M.2    Valsamakis, G.3    Chetty, R.4    Harte, A.5    McTernan, C.L.6    Clark, P.M.7    Smith, S.A.8    Barnett, A.H.9    Kumar, S.10
  • 34
    • 34548124842 scopus 로고    scopus 로고
    • Conditioned medium obtained from in vitro differentiated adipocytes and resistin induce insulin resistance in human hepatocytes
    • L. Zhou, H. Sell, K. Eckardt, Z. Yang, J. Eckel, Conditioned medium obtained from in vitro differentiated adipocytes and resistin induce insulin resistance in human hepatocytes. FEBS Lett. 581, 4303-4308 (2007)
    • (2007) FEBS Lett. , vol.581 , pp. 4303-4308
    • Zhou, L.1    Sell, H.2    Eckardt, K.3    Yang, Z.4    Eckel, J.5
  • 35
    • 14644426519 scopus 로고    scopus 로고
    • Complementary roles of IRS-1 and IRS-2 in the hepatic regulation of metabolism
    • C.M. Taniguchi, K. Ueki, R. Kahn, Complementary roles of IRS-1 and IRS-2 in the hepatic regulation of metabolism. J. Clin. Invest. 115, 718-727 (2005)
    • (2005) J. Clin. Invest. , vol.115 , pp. 718-727
    • Taniguchi, C.M.1    Ueki, K.2    Kahn, R.3
  • 37
    • 0033815967 scopus 로고    scopus 로고
    • Characterization of the role of AMP-activated protein kinase in the regulation of glucoseactivated gene expression using constitutively active and dominant negative forms of the kinase
    • A. Woods, D. Zzout-Marniche, M. Foretz, S.C. Stein, P. Lemarchand, P. Ferre, F. Foufelle, D. Carling, Characterization of the role of AMP-activated protein kinase in the regulation of glucoseactivated gene expression using constitutively active and dominant negative forms of the kinase. Mol. Cell. Biol. 20, 6704-6711 (2000)
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6704-6711
    • Woods, A.1    Zzout-Marniche, D.2    Foretz, M.3    Stein, S.C.4    Lemarchand, P.5    Ferre, P.6    Foufelle, F.7    Carling, D.8
  • 38
    • 9144271181 scopus 로고    scopus 로고
    • AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulin-resistant human HepG2 cells
    • M. Zang, A. Zuccollo, X. Hou, D. Nagata, K. Walsh, H. Herscovitz, P. Brecher, N.B. Ruderman, R.A. Cohen, AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulin-resistant human HepG2 cells. J. Biol. Chem. 279, 47898-47905 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 47898-47905
    • Zang, M.1    Zuccollo, A.2    Hou, X.3    Nagata, D.4    Walsh, K.5    Herscovitz, H.6    Brecher, P.7    Ruderman, N.B.8    Cohen, R.A.9
  • 42
    • 23044439100 scopus 로고    scopus 로고
    • Human resistin stimulates the pro-inflammatory cytokines TNF-alpha and IL-12 in macrophages by NF-kappaBdependent pathway
    • N. Silswal, A.K. Singh, B. Aruna, S. Mukhopadhyay, S. Ghosh, N.Z. Ehtesham, Human resistin stimulates the pro-inflammatory cytokines TNF-alpha and IL-12 in macrophages by NF-kappaBdependent pathway. Biochem. Biophys. Res. Commun. 334, 1092-1101 (2005)
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1092-1101
    • Silswal, N.1    Singh, A.K.2    Aruna, B.3    Mukhopadhyay, S.4    Ghosh, S.5    Ehtesham, N.Z.6
  • 44
    • 33745196745 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase in the liver: A new strategy for the management of metabolic hepatic disorders
    • B. Viollet, M. Foretz, B. Guigas, S. Horman, R. Dentin, L. Bertrand, L. Hue, F. Andreelli, Activation of AMP-activated protein kinase in the liver: A new strategy for the management of metabolic hepatic disorders. J. Physiol. 574, 41-53 (2006)
    • (2006) J. Physiol. , vol.574 , pp. 41-53
    • Viollet, B.1    Foretz, M.2    Guigas, B.3    Horman, S.4    Dentin, R.5    Bertrand, L.6    Hue, L.7    Andreelli, F.8
  • 45
    • 33847080728 scopus 로고    scopus 로고
    • AMP-activated protein kinase in metabolic control and insulin signaling
    • M.C. Towler, D.G. Hardie, AMP-activated protein kinase in metabolic control and insulin signaling. Circ. Res. 100, 328-341 (2007)
    • (2007) Circ. Res. , vol.100 , pp. 328-341
    • Towler, M.C.1    Hardie, D.G.2
  • 47
    • 0034074153 scopus 로고    scopus 로고
    • 5-aminoimidazole-4-carboxamide riboside mimics the effects of insulin on the expression of the 2 key gluconeogenic genes PEPCK and glucose-6-phosphatase
    • P.A. Lochhead, I.P. Salt, K.S. Walker, D.G. Hardie, C. Sutherland, 5-aminoimidazole-4-carboxamide riboside mimics the effects of insulin on the expression of the 2 key gluconeogenic genes PEPCK and glucose-6-phosphatase. Diabetes 49, 896-903 (2000)
    • (2000) Diabetes , vol.49 , pp. 896-903
    • Lochhead, P.A.1    Salt, I.P.2    Walker, K.S.3    Hardie, D.G.4    Sutherland, C.5
  • 48
    • 0037853260 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling-3 (SOCS-3), a potential mediator of interleukin-6-dependent insulin resistance in hepatocytes
    • J.J. Senn, P.J. Klover, I.A. Nowak, T.A. Zimmers, L.G. Koniaris, R.W. Furlanetto, R.A. Mooney, Suppressor of cytokine signaling-3 (SOCS-3), a potential mediator of interleukin-6-dependent insulin resistance in hepatocytes. J. Biol. Chem. 278, 13740-13746 (2003)
    • (2003) J. Biol. Chem. , vol.278 , pp. 13740-13746
    • Senn, J.J.1    Klover, P.J.2    Nowak, I.A.3    Zimmers, T.A.4    Koniaris, L.G.5    Furlanetto, R.W.6    Mooney, R.A.7
  • 49
    • 0035930605 scopus 로고    scopus 로고
    • SOCS-3 inhibits insulin signaling and is up-regulated in response to tumor necrosis factoralpha in the adipose tissue of obese mice
    • B. Emanuelli, P. Peraldi, C. Filloux, C. Chavey, K. Freidinger, D.J. Hilton, G.S. Hotamisligil, O.E. Van, SOCS-3 inhibits insulin signaling and is up-regulated in response to tumor necrosis factoralpha in the adipose tissue of obese mice. J. Biol. Chem. 276, 47944-47949 (2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 47944-47949
    • Emanuelli, B.1    Peraldi, P.2    Filloux, C.3    Chavey, C.4    Freidinger, K.5    Hilton, D.J.6    Hotamisligil, G.S.7    Van, O.E.8
  • 50
    • 0036830636 scopus 로고    scopus 로고
    • SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2
    • L. Rui, M. Yuan, D. Frantz, S. Shoelson, M.F. White, SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2. J. Biol. Chem. 277, 42394-42398 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 42394-42398
    • Rui, L.1    Yuan, M.2    Frantz, D.3    Shoelson, S.4    White, M.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.