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Volumn 18, Issue 8, 2007, Pages 291-299

Adipose stress-sensing kinases: linking obesity to malfunction

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE;

EID: 34948911181     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tem.2007.08.006     Document Type: Review
Times cited : (64)

References (72)
  • 1
    • 0002210727 scopus 로고
    • A syndrome produced by diverse nocuous agents
    • Selye H. A syndrome produced by diverse nocuous agents. Nature 138 (1936) 230-231
    • (1936) Nature , vol.138 , pp. 230-231
    • Selye, H.1
  • 2
    • 32644479922 scopus 로고    scopus 로고
    • Cellular redox state and insulin sensitivity: potential role of lipoic acid
    • Zierath J.R., and Wallberg-Henriksen H. (Eds), Taylor and Francis
    • Rudich A., and Bashan N. Cellular redox state and insulin sensitivity: potential role of lipoic acid. In: Zierath J.R., and Wallberg-Henriksen H. (Eds). Muscle Metabolism (2002), Taylor and Francis 329-348
    • (2002) Muscle Metabolism , pp. 329-348
    • Rudich, A.1    Bashan, N.2
  • 3
    • 33645745733 scopus 로고    scopus 로고
    • Activation of oxidative stress by acute glucose fluctuations compared with sustained chronic hyperglycemia in patients with Type 2 diabetes
    • Monnier L., et al. Activation of oxidative stress by acute glucose fluctuations compared with sustained chronic hyperglycemia in patients with Type 2 diabetes. J. Am. Med. Assoc. 295 (2006) 1681-1687
    • (2006) J. Am. Med. Assoc. , vol.295 , pp. 1681-1687
    • Monnier, L.1
  • 4
    • 85030434746 scopus 로고    scopus 로고
    • Increased oxidative stress in obesity and its impact on metabolic syndrome
    • Furukawa S., et al. Increased oxidative stress in obesity and its impact on metabolic syndrome. J. Clin. Invest. 114 (2004) 1752-1761
    • (2004) J. Clin. Invest. , vol.114 , pp. 1752-1761
    • Furukawa, S.1
  • 5
    • 12144273607 scopus 로고    scopus 로고
    • PKC-δ-dependent activation of oxidative stress in adipocytes of obese and insulin-resistant mice: role for NADPH oxidase
    • Talior I., et al. PKC-δ-dependent activation of oxidative stress in adipocytes of obese and insulin-resistant mice: role for NADPH oxidase. Am. J. Physiol. Endocrinol. Metab. 288 (2005) E405-E411
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.288
    • Talior, I.1
  • 6
    • 20344373410 scopus 로고    scopus 로고
    • Overexpression of glucose-6-phosphate dehydrogenase is associated with lipid dysregulation and insulin resistance in obesity
    • Park J., et al. Overexpression of glucose-6-phosphate dehydrogenase is associated with lipid dysregulation and insulin resistance in obesity. Mol. Cell. Biol. 25 (2005) 5146-5157
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5146-5157
    • Park, J.1
  • 7
    • 33744950569 scopus 로고    scopus 로고
    • Adipose tissue proadipogenic redox changes in obesity
    • Galinier A., et al. Adipose tissue proadipogenic redox changes in obesity. J. Biol. Chem. 281 (2006) 12682-12687
    • (2006) J. Biol. Chem. , vol.281 , pp. 12682-12687
    • Galinier, A.1
  • 8
    • 34247361278 scopus 로고    scopus 로고
    • Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal
    • Grimsrud P.A., et al. Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol. Cell. Proteomics 6 (2007) 624-637
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 624-637
    • Grimsrud, P.A.1
  • 9
    • 33748314535 scopus 로고    scopus 로고
    • Increased infiltration of macrophages in omental adipose tissue is associated with marked hepatic lesions in morbid human obesity
    • Cancello R., et al. Increased infiltration of macrophages in omental adipose tissue is associated with marked hepatic lesions in morbid human obesity. Diabetes 55 (2006) 1554-1561
    • (2006) Diabetes , vol.55 , pp. 1554-1561
    • Cancello, R.1
  • 10
    • 34347249246 scopus 로고    scopus 로고
    • Macrophage infiltration into omental versus subcutaneous fat across different populations: effect of regional adiposity and the co-morbidities of obesity
    • Harman-Boehm I., et al. Macrophage infiltration into omental versus subcutaneous fat across different populations: effect of regional adiposity and the co-morbidities of obesity. J. Clin. Endocrinol. Metab. 92 (2007) 2240-2247
    • (2007) J. Clin. Endocrinol. Metab. , vol.92 , pp. 2240-2247
    • Harman-Boehm, I.1
  • 11
    • 0348230958 scopus 로고    scopus 로고
    • Obesity is associated with macrophage accumulation in adipose tissue
    • Weisberg S.P., et al. Obesity is associated with macrophage accumulation in adipose tissue. J. Clin. Invest. 112 (2003) 1796-1808
    • (2003) J. Clin. Invest. , vol.112 , pp. 1796-1808
    • Weisberg, S.P.1
  • 12
    • 9144223683 scopus 로고    scopus 로고
    • Chronic inflammation in fat plays a crucial role in the development of obesity-related insulin resistance
    • Xu H., et al. Chronic inflammation in fat plays a crucial role in the development of obesity-related insulin resistance. J. Clin. Invest. 112 (2003) 1821-1830
    • (2003) J. Clin. Invest. , vol.112 , pp. 1821-1830
    • Xu, H.1
  • 13
    • 33846026712 scopus 로고    scopus 로고
    • Obesity induces a phenotypic switch in adipose tissue macrophage polarization
    • Lumeng C.N., et al. Obesity induces a phenotypic switch in adipose tissue macrophage polarization. J. Clin. Invest. 117 (2007) 175-184
    • (2007) J. Clin. Invest. , vol.117 , pp. 175-184
    • Lumeng, C.N.1
  • 14
    • 31644443192 scopus 로고    scopus 로고
    • Ceramides in insulin resistance and lipotoxicity
    • Summers S.A. Ceramides in insulin resistance and lipotoxicity. Prog. Lipid Res. 45 (2006) 42-72
    • (2006) Prog. Lipid Res. , vol.45 , pp. 42-72
    • Summers, S.A.1
  • 16
    • 2042540707 scopus 로고    scopus 로고
    • Activation of the hexosamine signaling pathway in adipose tissue results in decreased serum adiponectin and skeletal muscle insulin resistance
    • Hazel M., et al. Activation of the hexosamine signaling pathway in adipose tissue results in decreased serum adiponectin and skeletal muscle insulin resistance. Endocrinology 145 (2004) 2118-2128
    • (2004) Endocrinology , vol.145 , pp. 2118-2128
    • Hazel, M.1
  • 17
    • 6344261703 scopus 로고    scopus 로고
    • Role of hexosamines in insulin resistance and nutrient sensing in human adipose and muscle tissue
    • Pouwels M.J., et al. Role of hexosamines in insulin resistance and nutrient sensing in human adipose and muscle tissue. J. Clin. Endocrinol. Metab. 89 (2004) 5132-5137
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 5132-5137
    • Pouwels, M.J.1
  • 18
    • 20044363264 scopus 로고    scopus 로고
    • The hyperglycemia-induced inflammatory response in adipocytes: the role of reactive oxygen species
    • Lin Y., et al. The hyperglycemia-induced inflammatory response in adipocytes: the role of reactive oxygen species. J. Biol. Chem. 280 (2005) 4617-4626
    • (2005) J. Biol. Chem. , vol.280 , pp. 4617-4626
    • Lin, Y.1
  • 19
    • 33750590489 scopus 로고    scopus 로고
    • Altered adipose and plasma sphingolipid metabolism in obesity: a potential mechanism for cardiovascular and metabolic risk
    • Samad F., et al. Altered adipose and plasma sphingolipid metabolism in obesity: a potential mechanism for cardiovascular and metabolic risk. Diabetes 55 (2006) 2579-2587
    • (2006) Diabetes , vol.55 , pp. 2579-2587
    • Samad, F.1
  • 20
    • 0142164965 scopus 로고    scopus 로고
    • Characterizing the effects of saturated fatty acids on insulin signaling and ceramide and diacylglycerol accumulation in 3T3-L1 adipocytes and C2C12 myotubes
    • Chavez J.A., and Summers S.A. Characterizing the effects of saturated fatty acids on insulin signaling and ceramide and diacylglycerol accumulation in 3T3-L1 adipocytes and C2C12 myotubes. Arch. Biochem. Biophys. 419 (2003) 101-109
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 101-109
    • Chavez, J.A.1    Summers, S.A.2
  • 21
    • 2442539128 scopus 로고    scopus 로고
    • No in vitro effects of fatty acids on glucose uptake, lipolysis or insulin signaling in rat adipocytes
    • Lundgren M., and Eriksson J.W. No in vitro effects of fatty acids on glucose uptake, lipolysis or insulin signaling in rat adipocytes. Horm. Metab. Res. 36 (2004) 203-209
    • (2004) Horm. Metab. Res. , vol.36 , pp. 203-209
    • Lundgren, M.1    Eriksson, J.W.2
  • 22
    • 27444445460 scopus 로고    scopus 로고
    • JNK and tumor necrosis factor-α mediate free fatty acid-induced insulin resistance in 3T3-L1 adipocytes
    • Nguyen M.T., et al. JNK and tumor necrosis factor-α mediate free fatty acid-induced insulin resistance in 3T3-L1 adipocytes. J. Biol. Chem. 280 (2005) 35361-35371
    • (2005) J. Biol. Chem. , vol.280 , pp. 35361-35371
    • Nguyen, M.T.1
  • 23
    • 26244448904 scopus 로고    scopus 로고
    • A paracrine loop between adipocytes and macrophages aggravates inflammatory changes: role of free fatty acids and tumor necrosis factor α
    • Suganami T., et al. A paracrine loop between adipocytes and macrophages aggravates inflammatory changes: role of free fatty acids and tumor necrosis factor α. Arterioscler. Thromb. Vasc. Biol. 25 (2005) 2062-2068
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 2062-2068
    • Suganami, T.1
  • 24
    • 33750584214 scopus 로고    scopus 로고
    • TLR4 links innate immunity and fatty acid-induced insulin resistance
    • Shi H., et al. TLR4 links innate immunity and fatty acid-induced insulin resistance. J. Clin. Invest. 116 (2006) 3015-3025
    • (2006) J. Clin. Invest. , vol.116 , pp. 3015-3025
    • Shi, H.1
  • 25
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and Type 2 diabetes
    • Ozcan U., et al. Endoplasmic reticulum stress links obesity, insulin action, and Type 2 diabetes. Science 306 (2004) 457-461
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1
  • 26
    • 34047119110 scopus 로고    scopus 로고
    • Adipose tissue hypoxia in obesity and its impact on adipocytokine dysregulation
    • Hosogai N., et al. Adipose tissue hypoxia in obesity and its impact on adipocytokine dysregulation. Diabetes 56 (2007) 901-911
    • (2007) Diabetes , vol.56 , pp. 901-911
    • Hosogai, N.1
  • 27
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • Hotamisligil G.S. Inflammation and metabolic disorders. Nature 444 (2006) 860-867
    • (2006) Nature , vol.444 , pp. 860-867
    • Hotamisligil, G.S.1
  • 28
    • 27444437321 scopus 로고    scopus 로고
    • Adipocyte death defines macrophage localization and function in adipose tissue of obese mice and humans
    • Cinti S., et al. Adipocyte death defines macrophage localization and function in adipose tissue of obese mice and humans. J. Lipid Res. 46 (2005) 2347-2355
    • (2005) J. Lipid Res. , vol.46 , pp. 2347-2355
    • Cinti, S.1
  • 29
    • 0031831765 scopus 로고    scopus 로고
    • Qualitative regional differences in adipose tissue growth and cellularity in male Wistar rats fed ad libitum
    • DiGirolamo M., et al. Qualitative regional differences in adipose tissue growth and cellularity in male Wistar rats fed ad libitum. Am. J. Physiol. 274 (1998) R1460-R1467
    • (1998) Am. J. Physiol. , vol.274
    • DiGirolamo, M.1
  • 30
    • 33846323706 scopus 로고    scopus 로고
    • Role of the Toll-like receptor 4/NF-κB pathway in saturated fatty acid-induced inflammatory changes in the interaction between adipocytes and macrophages
    • Suganami T., et al. Role of the Toll-like receptor 4/NF-κB pathway in saturated fatty acid-induced inflammatory changes in the interaction between adipocytes and macrophages. Arterioscler. Thromb. Vasc. Biol. 27 (2007) 84-91
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 84-91
    • Suganami, T.1
  • 31
    • 34047175336 scopus 로고    scopus 로고
    • Uncoupling protein 2 controls adiponectin gene expression in adipose tissue through the modulation of reactive oxygen species production
    • Chevillotte E., et al. Uncoupling protein 2 controls adiponectin gene expression in adipose tissue through the modulation of reactive oxygen species production. Diabetes 56 (2007) 1042-1050
    • (2007) Diabetes , vol.56 , pp. 1042-1050
    • Chevillotte, E.1
  • 32
    • 14944340746 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant treatment in diabetes
    • Scott J.A., and King G.L. Oxidative stress and antioxidant treatment in diabetes. Ann. N. Y. Acad. Sci. 1031 (2004) 204-213
    • (2004) Ann. N. Y. Acad. Sci. , vol.1031 , pp. 204-213
    • Scott, J.A.1    King, G.L.2
  • 33
    • 28244488706 scopus 로고    scopus 로고
    • Inflammation-activated protein kinases as targets for drug development
    • Karin M. Inflammation-activated protein kinases as targets for drug development. Proc. Am. Thorac. Soc. 2 (2005) 386-390
    • (2005) Proc. Am. Thorac. Soc. , vol.2 , pp. 386-390
    • Karin, M.1
  • 34
    • 33846569938 scopus 로고    scopus 로고
    • Targeting mammalian target of rapamycin (mTOR) for health and diseases
    • Tsang C.K., et al. Targeting mammalian target of rapamycin (mTOR) for health and diseases. Drug Discov. Today 12 (2007) 112-124
    • (2007) Drug Discov. Today , vol.12 , pp. 112-124
    • Tsang, C.K.1
  • 35
    • 33847754623 scopus 로고    scopus 로고
    • The JNK signal transduction pathway
    • Weston C.R., and Davis R.J. The JNK signal transduction pathway. Curr. Opin. Cell Biol. 19 (2007) 142-149
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 142-149
    • Weston, C.R.1    Davis, R.J.2
  • 36
    • 18244370762 scopus 로고    scopus 로고
    • Inflammation, stress, and diabetes
    • Wellen K.E., and Hotamisligil G.S. Inflammation, stress, and diabetes. J. Clin. Invest. 115 (2005) 1111-1119
    • (2005) J. Clin. Invest. , vol.115 , pp. 1111-1119
    • Wellen, K.E.1    Hotamisligil, G.S.2
  • 37
    • 0037341276 scopus 로고    scopus 로고
    • Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: potential role of p38 in the downregulation of GLUT4 expression
    • Carlson C.J., et al. Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: potential role of p38 in the downregulation of GLUT4 expression. Diabetes 52 (2003) 634-641
    • (2003) Diabetes , vol.52 , pp. 634-641
    • Carlson, C.J.1
  • 38
    • 33846603289 scopus 로고    scopus 로고
    • Pathophysiological roles of ASK1-MAP kinase signaling pathways
    • Nagai H., et al. Pathophysiological roles of ASK1-MAP kinase signaling pathways. J. Biochem. Mol. Biol. 40 (2007) 1-6
    • (2007) J. Biochem. Mol. Biol. , vol.40 , pp. 1-6
    • Nagai, H.1
  • 39
    • 33144463713 scopus 로고    scopus 로고
    • An RNA interference-based screen identifies MAP4K4/NIK as a negative regulator of PPARγ, adipogenesis, and insulin-responsive hexose transport
    • Tang X., et al. An RNA interference-based screen identifies MAP4K4/NIK as a negative regulator of PPARγ, adipogenesis, and insulin-responsive hexose transport. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 2087-2092
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2087-2092
    • Tang, X.1
  • 40
    • 33244481462 scopus 로고    scopus 로고
    • Ser/Thr phosphorylation of IRS proteins: a molecular basis for insulin resistance
    • Zick Y. Ser/Thr phosphorylation of IRS proteins: a molecular basis for insulin resistance. Sci. STKE 2005 (2005) pe4
    • (2005) Sci. STKE , vol.2005
    • Zick, Y.1
  • 41
    • 0037339991 scopus 로고    scopus 로고
    • Three mitogen-activated protein kinases inhibit insulin signaling by different mechanisms in 3T3-L1 adipocytes
    • Fujishiro M., et al. Three mitogen-activated protein kinases inhibit insulin signaling by different mechanisms in 3T3-L1 adipocytes. Mol. Endocrinol. 17 (2003) 487-497
    • (2003) Mol. Endocrinol. , vol.17 , pp. 487-497
    • Fujishiro, M.1
  • 42
    • 20444458773 scopus 로고    scopus 로고
    • Pharmacological inhibition of p38 MAP kinase results in improved glucose uptake in insulin-resistant 3T3-L1 adipocytes
    • Carlson C.J., and Rondinone C.M. Pharmacological inhibition of p38 MAP kinase results in improved glucose uptake in insulin-resistant 3T3-L1 adipocytes. Metabolism 54 (2005) 895-901
    • (2005) Metabolism , vol.54 , pp. 895-901
    • Carlson, C.J.1    Rondinone, C.M.2
  • 43
    • 3442895916 scopus 로고    scopus 로고
    • Inhibition of insulin sensitivity by free fatty acids requires activation of multiple serine kinases in 3T3-L1 adipocytes
    • Gao Z., et al. Inhibition of insulin sensitivity by free fatty acids requires activation of multiple serine kinases in 3T3-L1 adipocytes. Mol. Endocrinol. 18 (2004) 2024-2034
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2024-2034
    • Gao, Z.1
  • 44
    • 0034463918 scopus 로고    scopus 로고
    • A rapamycin-sensitive pathway down-regulates insulin signaling via phosphorylation and proteasomal degradation of insulin receptor substrate-1
    • Haruta T., et al. A rapamycin-sensitive pathway down-regulates insulin signaling via phosphorylation and proteasomal degradation of insulin receptor substrate-1. Mol. Endocrinol. 14 (2000) 783-794
    • (2000) Mol. Endocrinol. , vol.14 , pp. 783-794
    • Haruta, T.1
  • 45
    • 0035979775 scopus 로고    scopus 로고
    • Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkβ
    • Yuan M., et al. Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkβ. Science 293 (2001) 1673-1677
    • (2001) Science , vol.293 , pp. 1673-1677
    • Yuan, M.1
  • 46
    • 5644301067 scopus 로고    scopus 로고
    • Rosiglitazone ameliorates insulin resistance in brown adipocytes of Wistar rats by impairing TNF-α induction of p38 and p42/p44 mitogen-activated protein kinases
    • Hernandez R., et al. Rosiglitazone ameliorates insulin resistance in brown adipocytes of Wistar rats by impairing TNF-α induction of p38 and p42/p44 mitogen-activated protein kinases. Diabetologia 47 (2004) 1615-1624
    • (2004) Diabetologia , vol.47 , pp. 1615-1624
    • Hernandez, R.1
  • 47
    • 11144344885 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase is involved in the suppression of adiponectin expression by TNF-α in 3T3-L1 adipocytes
    • Kim K.Y., et al. c-Jun N-terminal kinase is involved in the suppression of adiponectin expression by TNF-α in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 327 (2005) 460-467
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , pp. 460-467
    • Kim, K.Y.1
  • 48
    • 11144356766 scopus 로고    scopus 로고
    • Conditional disruption of IκB kinase 2 fails to prevent obesity-induced insulin resistance
    • Rohl M., et al. Conditional disruption of IκB kinase 2 fails to prevent obesity-induced insulin resistance. J. Clin. Invest. 113 (2004) 474-481
    • (2004) J. Clin. Invest. , vol.113 , pp. 474-481
    • Rohl, M.1
  • 49
    • 0034903710 scopus 로고    scopus 로고
    • Prevention of fat-induced insulin resistance by salicylate
    • Kim J.K., et al. Prevention of fat-induced insulin resistance by salicylate. J. Clin. Invest. 108 (2001) 437-446
    • (2001) J. Clin. Invest. , vol.108 , pp. 437-446
    • Kim, J.K.1
  • 50
    • 33748069813 scopus 로고    scopus 로고
    • Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of Type 2 diabetes
    • Ozcan U., et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of Type 2 diabetes. Science 313 (2006) 1137-1140
    • (2006) Science , vol.313 , pp. 1137-1140
    • Ozcan, U.1
  • 51
    • 0037153158 scopus 로고    scopus 로고
    • A central role for JNK in obesity and insulin resistance
    • Hirosumi J., et al. A central role for JNK in obesity and insulin resistance. Nature 420 (2002) 333-336
    • (2002) Nature , vol.420 , pp. 333-336
    • Hirosumi, J.1
  • 52
    • 4043073652 scopus 로고    scopus 로고
    • An essential role of the JIP1 scaffold protein for JNK activation in adipose tissue
    • Jaeschke A., et al. An essential role of the JIP1 scaffold protein for JNK activation in adipose tissue. Genes Dev. 18 (2004) 1976-1980
    • (2004) Genes Dev. , vol.18 , pp. 1976-1980
    • Jaeschke, A.1
  • 53
    • 20044364733 scopus 로고    scopus 로고
    • Western diet modulates insulin signaling, c-Jun N-terminal kinase activity, and insulin receptor substrate-1ser307 phosphorylation in a tissue-specific fashion
    • Prada P.O., et al. Western diet modulates insulin signaling, c-Jun N-terminal kinase activity, and insulin receptor substrate-1ser307 phosphorylation in a tissue-specific fashion. Endocrinology 146 (2005) 1576-1587
    • (2005) Endocrinology , vol.146 , pp. 1576-1587
    • Prada, P.O.1
  • 54
    • 0942268725 scopus 로고    scopus 로고
    • Rosiglitazone, an agonist of peroxisome-proliferator-activated receptor gamma (PPARγ), decreases inhibitory serine phosphorylation of IRS1 in vitro and in vivo
    • Jiang G., et al. Rosiglitazone, an agonist of peroxisome-proliferator-activated receptor gamma (PPARγ), decreases inhibitory serine phosphorylation of IRS1 in vitro and in vivo. Biochem. J. 377 (2004) 339-346
    • (2004) Biochem. J. , vol.377 , pp. 339-346
    • Jiang, G.1
  • 55
    • 4544220704 scopus 로고    scopus 로고
    • Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
    • Um S.H., et al. Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity. Nature 431 (2004) 200-205
    • (2004) Nature , vol.431 , pp. 200-205
    • Um, S.H.1
  • 56
    • 33846806078 scopus 로고    scopus 로고
    • Elevated sensitivity to diet-induced obesity and insulin resistance in mice lacking 4E-BP1 and 4E-BP2
    • Le Bacquer O., et al. Elevated sensitivity to diet-induced obesity and insulin resistance in mice lacking 4E-BP1 and 4E-BP2. J. Clin. Invest. 117 (2007) 387-396
    • (2007) J. Clin. Invest. , vol.117 , pp. 387-396
    • Le Bacquer, O.1
  • 57
    • 33846841155 scopus 로고    scopus 로고
    • A link between protein translation and body weight
    • Rui L. A link between protein translation and body weight. J. Clin. Invest. 117 (2007) 310-313
    • (2007) J. Clin. Invest. , vol.117 , pp. 310-313
    • Rui, L.1
  • 58
    • 34250863505 scopus 로고    scopus 로고
    • MAP kinases, IKK and insulin signaling in human omental versus subcutaneous adipose tissue in obesity
    • Bashan N., et al. MAP kinases, IKK and insulin signaling in human omental versus subcutaneous adipose tissue in obesity. Endocrinology 148 (2007) 2955-2962
    • (2007) Endocrinology , vol.148 , pp. 2955-2962
    • Bashan, N.1
  • 59
    • 14244269217 scopus 로고    scopus 로고
    • Sulfasalazine and BAY 11-7082 interfere with the nuclear factor-κB and IκB kinase pathway to regulate the release of proinflammatory cytokines from human adipose tissue and skeletal muscle in vitro
    • Lappas M., et al. Sulfasalazine and BAY 11-7082 interfere with the nuclear factor-κB and IκB kinase pathway to regulate the release of proinflammatory cytokines from human adipose tissue and skeletal muscle in vitro. Endocrinology 146 (2005) 1491-1497
    • (2005) Endocrinology , vol.146 , pp. 1491-1497
    • Lappas, M.1
  • 60
    • 27544487938 scopus 로고    scopus 로고
    • JNK: bridging the insulin signaling and inflammatory pathway
    • Liu G., and Rondinone C.M. JNK: bridging the insulin signaling and inflammatory pathway. Curr. Opin. Investig. Drugs 6 (2005) 979-987
    • (2005) Curr. Opin. Investig. Drugs , vol.6 , pp. 979-987
    • Liu, G.1    Rondinone, C.M.2
  • 61
    • 7044230885 scopus 로고    scopus 로고
    • Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide
    • Kaneto H., et al. Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide. Nat. Med. 10 (2004) 1128-1132
    • (2004) Nat. Med. , vol.10 , pp. 1128-1132
    • Kaneto, H.1
  • 62
    • 0037474274 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase (JNK) mediates feedback inhibition of the insulin signaling cascade
    • Lee Y.H., et al. c-Jun N-terminal kinase (JNK) mediates feedback inhibition of the insulin signaling cascade. J. Biol. Chem. 278 (2003) 2896-2902
    • (2003) J. Biol. Chem. , vol.278 , pp. 2896-2902
    • Lee, Y.H.1
  • 63
    • 0036796875 scopus 로고    scopus 로고
    • Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of Type 2 diabetes
    • Evans J.L., et al. Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of Type 2 diabetes. Endocr. Rev. 23 (2002) 599-622
    • (2002) Endocr. Rev. , vol.23 , pp. 599-622
    • Evans, J.L.1
  • 64
    • 33748781446 scopus 로고    scopus 로고
    • Role of MAPKs in development and differentiation: lessons from knockout mice
    • Aouadi M., et al. Role of MAPKs in development and differentiation: lessons from knockout mice. Biochimie 88 (2006) 1091-1098
    • (2006) Biochimie , vol.88 , pp. 1091-1098
    • Aouadi, M.1
  • 65
    • 33845873659 scopus 로고    scopus 로고
    • Interleukin-1β-induced insulin resistance in adipocytes through down-regulation of insulin receptor substrate-1 expression
    • Jager J., et al. Interleukin-1β-induced insulin resistance in adipocytes through down-regulation of insulin receptor substrate-1 expression. Endocrinology 148 (2007) 241-251
    • (2007) Endocrinology , vol.148 , pp. 241-251
    • Jager, J.1
  • 66
    • 19944433322 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase isoform ERK1 is specifically required for in vitro and in vivo adipogenesis
    • Bost F., et al. The extracellular signal-regulated kinase isoform ERK1 is specifically required for in vitro and in vivo adipogenesis. Diabetes 54 (2005) 402-411
    • (2005) Diabetes , vol.54 , pp. 402-411
    • Bost, F.1
  • 67
    • 0033773334 scopus 로고    scopus 로고
    • Tumor necrosis factor α-mediated insulin resistance, but not dedifferentiation, is abrogated by MEK1/2 inhibitors in 3T3-L1 adipocytes
    • Engelman J.A., et al. Tumor necrosis factor α-mediated insulin resistance, but not dedifferentiation, is abrogated by MEK1/2 inhibitors in 3T3-L1 adipocytes. Mol. Endocrinol. 14 (2000) 1557-1569
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1557-1569
    • Engelman, J.A.1
  • 68
    • 0042591261 scopus 로고    scopus 로고
    • Aspirin inhibits serine phosphorylation of insulin receptor substrate 1 in tumor necrosis factor-treated cells through targeting multiple serine kinases
    • Gao Z., et al. Aspirin inhibits serine phosphorylation of insulin receptor substrate 1 in tumor necrosis factor-treated cells through targeting multiple serine kinases. J. Biol. Chem. 278 (2003) 24944-24950
    • (2003) J. Biol. Chem. , vol.278 , pp. 24944-24950
    • Gao, Z.1
  • 69
    • 1542616960 scopus 로고    scopus 로고
    • Mammalian target of rapamycin regulates IRS-1 serine 307 phosphorylation
    • Carlson C.J., et al. Mammalian target of rapamycin regulates IRS-1 serine 307 phosphorylation. Biochem. Biophys. Res. Commun. 316 (2004) 533-539
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 533-539
    • Carlson, C.J.1
  • 70
    • 33644886769 scopus 로고    scopus 로고
    • Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation
    • Tzatsos A., and Kandror K.V. Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation. Mol. Cell. Biol. 26 (2006) 63-76
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 63-76
    • Tzatsos, A.1    Kandror, K.V.2
  • 71
    • 14244252683 scopus 로고    scopus 로고
    • Activation of the mammalian target of rapamycin pathway acutely inhibits insulin signaling to Akt and glucose transport in 3T3-L1 and human adipocytes
    • Tremblay F., et al. Activation of the mammalian target of rapamycin pathway acutely inhibits insulin signaling to Akt and glucose transport in 3T3-L1 and human adipocytes. Endocrinology 146 (2005) 1328-1337
    • (2005) Endocrinology , vol.146 , pp. 1328-1337
    • Tremblay, F.1
  • 72
    • 8544244084 scopus 로고    scopus 로고
    • PKC-theta knockout mice are protected from fat-induced insulin resistance
    • Kim J.K., et al. PKC-theta knockout mice are protected from fat-induced insulin resistance. J. Clin. Invest. 114 (2004) 823-827
    • (2004) J. Clin. Invest. , vol.114 , pp. 823-827
    • Kim, J.K.1


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