메뉴 건너뛰기




Volumn 35, Issue 9, 2010, Pages 490-496

CJun NH2-terminal kinase 1 (JNK1): Roles in metabolic regulation of insulin resistance

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN RECEPTOR SUBSTRATE 1; INTERLEUKIN 6; LIPOPROTEIN LIPASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; MITOGEN ACTIVATED PROTEIN KINASE KINASE 7; PROTIRELIN; STRESS ACTIVATED PROTEIN KINASE 1; SUPPRESSOR OF CYTOKINE SIGNALING 3; THYROTROPIN; TRIACYLGLYCEROL;

EID: 77956185248     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2010.04.004     Document Type: Review
Times cited : (134)

References (70)
  • 1
    • 33745896155 scopus 로고    scopus 로고
    • Recent advances in the relationship between obesity, inflammation, and insulin resistance
    • Bastard J.P., et al. Recent advances in the relationship between obesity, inflammation, and insulin resistance. Eur. Cytokine Netw. 2006, 17:4-12.
    • (2006) Eur. Cytokine Netw. , vol.17 , pp. 4-12
    • Bastard, J.P.1
  • 2
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • Zimmet P., et al. Global and societal implications of the diabetes epidemic. Nature 2001, 414:782-787.
    • (2001) Nature , vol.414 , pp. 782-787
    • Zimmet, P.1
  • 3
    • 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, 46:3-10.
    • (1997) Diabetes , vol.46 , pp. 3-10
    • Boden, G.1
  • 4
    • 33745861300 scopus 로고    scopus 로고
    • Inflammation and insulin resistance
    • Shoelson S.E., et al. Inflammation and insulin resistance. J. Clin. Invest. 2006, 116:1793-1801.
    • (2006) J. Clin. Invest. , vol.116 , pp. 1793-1801
    • Shoelson, S.E.1
  • 5
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • Hotamisligil G.S. Inflammation and metabolic disorders. Nature 2006, 444:860-867.
    • (2006) Nature , vol.444 , pp. 860-867
    • Hotamisligil, G.S.1
  • 6
    • 0344305782 scopus 로고    scopus 로고
    • Insulin signaling in health and disease
    • White M.F. Insulin signaling in health and disease. Science 2003, 302:1710-1711.
    • (2003) Science , vol.302 , pp. 1710-1711
    • White, M.F.1
  • 8
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis R.J. Signal transduction by the JNK group of MAP kinases. Cell 2000, 103:239-252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 9
    • 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 2002, 420:333-336.
    • (2002) Nature , vol.420 , pp. 333-336
    • Hirosumi, J.1
  • 10
    • 33746101818 scopus 로고    scopus 로고
    • Functional in vivo interactions between JNK1 and JNK2 isoforms in obesity and insulin resistance
    • Tuncman G., et al. Functional in vivo interactions between JNK1 and JNK2 isoforms in obesity and insulin resistance. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:10741-10746.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10741-10746
    • Tuncman, G.1
  • 11
    • 6344233096 scopus 로고    scopus 로고
    • Oxidative stress and the JNK pathway as a potential therapeutic target for diabetes
    • Kaneto H., et al. Oxidative stress and the JNK pathway as a potential therapeutic target for diabetes. Drug News Perspect. 2004, 17:447-453.
    • (2004) Drug News Perspect. , vol.17 , pp. 447-453
    • Kaneto, H.1
  • 12
    • 8544244943 scopus 로고    scopus 로고
    • Modulation of the JNK pathway in liver affects insulin resistance status
    • Nakatani Y., et al. Modulation of the JNK pathway in liver affects insulin resistance status. J. Biol. Chem. 2004, 279:45803-45809.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45803-45809
    • Nakatani, Y.1
  • 13
    • 0041302157 scopus 로고    scopus 로고
    • JNK: a new therapeutic target for diabetes
    • Bennett B.L., et al. JNK: a new therapeutic target for diabetes. Curr. Opin. Pharmacol. 2003, 3:420-425.
    • (2003) Curr. Opin. Pharmacol. , vol.3 , pp. 420-425
    • Bennett, B.L.1
  • 14
    • 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. 2004, 10:1128-1132.
    • (2004) Nat. Med. , vol.10 , pp. 1128-1132
    • Kaneto, H.1
  • 15
    • 55949100580 scopus 로고    scopus 로고
    • Identification of a new JNK inhibitor targeting the JNK-JIP interaction site
    • Stebbins J.L., et al. Identification of a new JNK inhibitor targeting the JNK-JIP interaction site. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:16809-16813.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16809-16813
    • Stebbins, J.L.1
  • 16
    • 0034992168 scopus 로고    scopus 로고
    • MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines
    • Tournier C., et al. MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines. Genes Dev. 2001, 15:1419-1426.
    • (2001) Genes Dev. , vol.15 , pp. 1419-1426
    • Tournier, C.1
  • 17
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil G.S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010, 140:900-917.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 18
    • 58149484392 scopus 로고    scopus 로고
    • Inflammation and endoplasmic reticulum stress in obesity and diabetes
    • Hotamisligil G.S. Inflammation and endoplasmic reticulum stress in obesity and diabetes. Int. J. Obes. (Lond.) 2008, 32(Suppl. 7):S52-S54.
    • (2008) Int. J. Obes. (Lond.) , vol.32 , Issue.SUPPL. 7
    • Hotamisligil, G.S.1
  • 19
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • Nakamura T., et al. Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 2010, 140:338-348.
    • (2010) Cell , vol.140 , pp. 338-348
    • Nakamura, T.1
  • 20
    • 34547602916 scopus 로고    scopus 로고
    • Loss-of-function mutation in Toll-like receptor 4 prevents diet-induced obesity and insulin resistance
    • Tsukumo D.M., et al. Loss-of-function mutation in Toll-like receptor 4 prevents diet-induced obesity and insulin resistance. Diabetes 2007, 56:1986-1998.
    • (2007) Diabetes , vol.56 , pp. 1986-1998
    • Tsukumo, D.M.1
  • 21
    • 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. 2006, 116:3015-3025.
    • (2006) J. Clin. Invest. , vol.116 , pp. 3015-3025
    • Shi, H.1
  • 22
    • 34547219895 scopus 로고    scopus 로고
    • Metabolic stress signaling mediated by mixed-lineage kinases
    • Jaeschke A., Davis R.J. Metabolic stress signaling mediated by mixed-lineage kinases. Mol. Cell 2007, 27:498-508.
    • (2007) Mol. Cell , vol.27 , pp. 498-508
    • Jaeschke, A.1    Davis, R.J.2
  • 23
    • 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. 2004, 18:1976-1980.
    • (2004) Genes Dev. , vol.18 , pp. 1976-1980
    • Jaeschke, A.1
  • 24
    • 0030756346 scopus 로고    scopus 로고
    • Protection from obesity-induced insulin resistance in mice lacking TNF-alpha function
    • Uysal K.T., et al. Protection from obesity-induced insulin resistance in mice lacking TNF-alpha function. Nature 1997, 389:610-614.
    • (1997) Nature , vol.389 , pp. 610-614
    • Uysal, K.T.1
  • 25
    • 57349101675 scopus 로고    scopus 로고
    • A stress signaling pathway in adipose tissue regulates hepatic insulin resistance
    • Sabio G., et al. A stress signaling pathway in adipose tissue regulates hepatic insulin resistance. Science 2008, 322:1539-1543.
    • (2008) Science , vol.322 , pp. 1539-1543
    • Sabio, G.1
  • 26
    • 73549091444 scopus 로고    scopus 로고
    • Role of muscle c-Jun NH2-terminal kinase 1 in obesity-induced insulin resistance
    • Sabio G., et al. Role of muscle c-Jun NH2-terminal kinase 1 in obesity-induced insulin resistance. Mol. Cell Biol. 2010, 30:106-115.
    • (2010) Mol. Cell Biol. , vol.30 , pp. 106-115
    • Sabio, G.1
  • 27
    • 0034708832 scopus 로고    scopus 로고
    • The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307)
    • Aguirre V., et al. The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). J. Biol. Chem. 2000, 275:9047-9054.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9047-9054
    • Aguirre, V.1
  • 28
    • 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. 2003, 278:2896-2902.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2896-2902
    • Lee, Y.H.1
  • 29
    • 0037059330 scopus 로고    scopus 로고
    • Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action
    • Aguirre V., et al. Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action. J. Biol. Chem. 2002, 277:1531-1537.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1531-1537
    • Aguirre, V.1
  • 30
    • 72649098413 scopus 로고    scopus 로고
    • Irs1 serine 307 promotes insulin sensitivity in mice
    • Copps K.D., et al. Irs1 serine 307 promotes insulin sensitivity in mice. Cell Metab. 2010, 11:84-92.
    • (2010) Cell Metab. , vol.11 , pp. 84-92
    • Copps, K.D.1
  • 31
    • 70449724835 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance: role of stress-regulated serine kinases and insulin receptor substrates (IRS) serine phosphorylation
    • Tanti J.F., Jager J. Cellular mechanisms of insulin resistance: role of stress-regulated serine kinases and insulin receptor substrates (IRS) serine phosphorylation. Curr. Opin. Pharmacol. 2009, 9:753-762.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 753-762
    • Tanti, J.F.1    Jager, J.2
  • 32
    • 34548333594 scopus 로고    scopus 로고
    • Phosphorylation of Irs1 at SER-522 inhibits insulin signaling
    • Giraud J., et al. Phosphorylation of Irs1 at SER-522 inhibits insulin signaling. Mol. Endocrinol. 2007, 21:2294-2302.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 2294-2302
    • Giraud, J.1
  • 33
    • 34748845043 scopus 로고    scopus 로고
    • Phosphorylation of human insulin receptor substrate-1 at Serine 629 plays a positive role in insulin signaling
    • Luo M., et al. Phosphorylation of human insulin receptor substrate-1 at Serine 629 plays a positive role in insulin signaling. Endocrinology 2007, 148:4895-4905.
    • (2007) Endocrinology , vol.148 , pp. 4895-4905
    • Luo, M.1
  • 34
    • 24944576051 scopus 로고    scopus 로고
    • Identification of insulin receptor substrate 1 serine/threonine phosphorylation sites using mass spectrometry analysis: regulatory role of serine 1223
    • Luo M., et al. Identification of insulin receptor substrate 1 serine/threonine phosphorylation sites using mass spectrometry analysis: regulatory role of serine 1223. Endocrinology 2005, 146:4410-4416.
    • (2005) Endocrinology , vol.146 , pp. 4410-4416
    • Luo, M.1
  • 35
    • 34249661732 scopus 로고    scopus 로고
    • Global assessment of regulation of phosphorylation of insulin receptor substrate-1 by insulin in vivo in human muscle
    • Yi Z., et al. Global assessment of regulation of phosphorylation of insulin receptor substrate-1 by insulin in vivo in human muscle. Diabetes 2007, 56:1508-1516.
    • (2007) Diabetes , vol.56 , pp. 1508-1516
    • Yi, Z.1
  • 36
    • 42649127400 scopus 로고    scopus 로고
    • IRS1-independent defects define major nodes of insulin resistance
    • Hoehn K.L., et al. IRS1-independent defects define major nodes of insulin resistance. Cell Metab. 2008, 7:421-433.
    • (2008) Cell Metab. , vol.7 , pp. 421-433
    • Hoehn, K.L.1
  • 37
    • 58249093873 scopus 로고    scopus 로고
    • Induction of hepatitis by JNK-mediated expression of TNF-alpha
    • Das M., et al. Induction of hepatitis by JNK-mediated expression of TNF-alpha. Cell 2009, 136:249-260.
    • (2009) Cell , vol.136 , pp. 249-260
    • Das, M.1
  • 38
    • 52349105273 scopus 로고    scopus 로고
    • A predominant role for parenchymal c-Jun amino terminal kinase (JNK) in the regulation of systemic insulin sensitivity
    • Vallerie S.N., et al. A predominant role for parenchymal c-Jun amino terminal kinase (JNK) in the regulation of systemic insulin sensitivity. PLoS One 2008, 3:e3151.
    • (2008) PLoS One , vol.3
    • Vallerie, S.N.1
  • 39
    • 35548943962 scopus 로고    scopus 로고
    • JNK1 in hematopoietically derived cells contributes to diet-induced inflammation and insulin resistance without affecting obesity
    • Solinas G., et al. JNK1 in hematopoietically derived cells contributes to diet-induced inflammation and insulin resistance without affecting obesity. Cell Metab. 2007, 6:386-397.
    • (2007) Cell Metab. , vol.6 , pp. 386-397
    • Solinas, G.1
  • 40
    • 57349199263 scopus 로고    scopus 로고
    • Cell signaling. Fat stress and liver resistance
    • Ogawa W., Kasuga M. Cell signaling. Fat stress and liver resistance. Science 2008, 322:1483-1484.
    • (2008) Science , vol.322 , pp. 1483-1484
    • Ogawa, W.1    Kasuga, M.2
  • 41
    • 34347354309 scopus 로고    scopus 로고
    • Macrophage-specific PPARgamma controls alternative activation and improves insulin resistance
    • Odegaard J.I., et al. Macrophage-specific PPARgamma controls alternative activation and improves insulin resistance. Nature 2007, 447:1116-1120.
    • (2007) Nature , vol.447 , pp. 1116-1120
    • Odegaard, J.I.1
  • 42
    • 44349112305 scopus 로고    scopus 로고
    • Adipocyte-derived Th2 cytokines and myeloid PPARdelta regulate macrophage polarization and insulin sensitivity
    • Kang K., et al. Adipocyte-derived Th2 cytokines and myeloid PPARdelta regulate macrophage polarization and insulin sensitivity. Cell Metab. 2008, 7:485-495.
    • (2008) Cell Metab. , vol.7 , pp. 485-495
    • Kang, K.1
  • 43
    • 27444445460 scopus 로고    scopus 로고
    • JNK and tumor necrosis factor-alpha mediate free fatty acid-induced insulin resistance in 3T3-L1 adipocytes
    • Nguyen M.T., et al. JNK and tumor necrosis factor-alpha mediate free fatty acid-induced insulin resistance in 3T3-L1 adipocytes. J. Biol. Chem. 2005, 280:35361-35371.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35361-35371
    • Nguyen, M.T.1
  • 44
    • 57849137363 scopus 로고    scopus 로고
    • Knockdown of JNK rescues 3T3-L1 adipocytes from insulin resistance induced by mitochondrial dysfunction
    • Kim T., et al. Knockdown of JNK rescues 3T3-L1 adipocytes from insulin resistance induced by mitochondrial dysfunction. Biochem. Biophys. Res. Commun. 2009, 378:772-776.
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 772-776
    • Kim, T.1
  • 45
    • 48149085566 scopus 로고    scopus 로고
    • Silencing Jnk1 and Jnk2 accelerates basal lipolysis and promotes fatty acid re-esterification in mouse adipocytes
    • Rozo A.V., et al. Silencing Jnk1 and Jnk2 accelerates basal lipolysis and promotes fatty acid re-esterification in mouse adipocytes. Diabetologia 2008, 51:1493-1504.
    • (2008) Diabetologia , vol.51 , pp. 1493-1504
    • Rozo, A.V.1
  • 46
    • 0034717062 scopus 로고    scopus 로고
    • SOCS-3 is an insulin-induced negative regulator of insulin signaling
    • Emanuelli B., et al. SOCS-3 is an insulin-induced negative regulator of insulin signaling. J. Biol. Chem. 2000, 275:15985-15991.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15985-15991
    • Emanuelli, B.1
  • 47
    • 0036830636 scopus 로고    scopus 로고
    • SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2
    • Rui L., et al. SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2. J. Biol. Chem. 2002, 277:42394-42398.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42394-42398
    • Rui, L.1
  • 48
    • 0035854723 scopus 로고    scopus 로고
    • Suppressors of cytokine signaling-1 and -6 associate with and inhibit the insulin receptor. A potential mechanism for cytokine-mediated insulin resistance
    • Mooney R.A., et al. Suppressors of cytokine signaling-1 and -6 associate with and inhibit the insulin receptor. A potential mechanism for cytokine-mediated insulin resistance. J. Biol. Chem. 2001, 276:25889-25893.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25889-25893
    • Mooney, R.A.1
  • 49
    • 0037853260 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling-3 (SOCS-3), a potential mediator of interleukin-6-dependent insulin resistance in hepatocytes
    • Senn J.J., et al. Suppressor of cytokine signaling-3 (SOCS-3), a potential mediator of interleukin-6-dependent insulin resistance in hepatocytes. J. Biol. Chem. 2003, 278:13740-13746.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13740-13746
    • Senn, J.J.1
  • 50
    • 0035930605 scopus 로고    scopus 로고
    • SOCS-3 inhibits insulin signaling and is up-regulated in response to tumor necrosis factor-alpha in the adipose tissue of obese mice
    • Emanuelli B., et al. SOCS-3 inhibits insulin signaling and is up-regulated in response to tumor necrosis factor-alpha in the adipose tissue of obese mice. J. Biol. Chem. 2001, 276:47944-47949.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47944-47949
    • Emanuelli, B.1
  • 51
    • 33947518747 scopus 로고    scopus 로고
    • Counterpoint: interleukin-6 does not have a beneficial role in insulin sensitivity and glucose homeostasis
    • discussion 818-819
    • Mooney R.A. Counterpoint: interleukin-6 does not have a beneficial role in insulin sensitivity and glucose homeostasis. J. Appl. Physiol. 2007, 102:816-818. discussion 818-819.
    • (2007) J. Appl. Physiol. , vol.102 , pp. 816-818
    • Mooney, R.A.1
  • 52
    • 33846883060 scopus 로고    scopus 로고
    • Point: interleukin-6 does have a beneficial role in insulin sensitivity and glucose homeostasis
    • Pedersen B.K., Febbraio M.A. Point: interleukin-6 does have a beneficial role in insulin sensitivity and glucose homeostasis. J. Appl. Physiol. 2007, 102:814-816.
    • (2007) J. Appl. Physiol. , vol.102 , pp. 814-816
    • Pedersen, B.K.1    Febbraio, M.A.2
  • 53
    • 33645579324 scopus 로고    scopus 로고
    • Role of hepatic STAT3 in brain-insulin action on hepatic glucose production
    • Inoue H., et al. Role of hepatic STAT3 in brain-insulin action on hepatic glucose production. Cell Metab. 2006, 3:267-275.
    • (2006) Cell Metab. , vol.3 , pp. 267-275
    • Inoue, H.1
  • 54
    • 0036152683 scopus 로고    scopus 로고
    • Interleukin-6-deficient mice develop mature-onset obesity
    • Wallenius V., et al. Interleukin-6-deficient mice develop mature-onset obesity. Nat. Med. 2002, 8:75-79.
    • (2002) Nat. Med. , vol.8 , pp. 75-79
    • Wallenius, V.1
  • 55
    • 0242268894 scopus 로고    scopus 로고
    • Chronic exposure to interleukin-6 causes hepatic insulin resistance in mice
    • Klover P.J., et al. Chronic exposure to interleukin-6 causes hepatic insulin resistance in mice. Diabetes 2003, 52:2784-2789.
    • (2003) Diabetes , vol.52 , pp. 2784-2789
    • Klover, P.J.1
  • 56
    • 12144290761 scopus 로고    scopus 로고
    • Differential effects of interleukin-6 and -10 on skeletal muscle and liver insulin action in vivo
    • Kim H.J., et al. Differential effects of interleukin-6 and -10 on skeletal muscle and liver insulin action in vivo. Diabetes 2004, 53:1060-1067.
    • (2004) Diabetes , vol.53 , pp. 1060-1067
    • Kim, H.J.1
  • 57
    • 23044468612 scopus 로고    scopus 로고
    • Interleukin-6 depletion selectively improves hepatic insulin action in obesity
    • Klover P.J., et al. Interleukin-6 depletion selectively improves hepatic insulin action in obesity. Endocrinology 2005, 146:3417-3427.
    • (2005) Endocrinology , vol.146 , pp. 3417-3427
    • Klover, P.J.1
  • 58
    • 33846512401 scopus 로고    scopus 로고
    • The dual function of hepatic SOCS3 in insulin resistance in vivo
    • Torisu T., et al. The dual function of hepatic SOCS3 in insulin resistance in vivo. Genes Cells 2007, 12:143-154.
    • (2007) Genes Cells , vol.12 , pp. 143-154
    • Torisu, T.1
  • 59
    • 34248581989 scopus 로고    scopus 로고
    • Disordered lipid metabolism and the pathogenesis of insulin resistance
    • Savage D.B., et al. Disordered lipid metabolism and the pathogenesis of insulin resistance. Physiol. Rev. 2007, 87:507-520.
    • (2007) Physiol. Rev. , vol.87 , pp. 507-520
    • Savage, D.B.1
  • 60
    • 77956094473 scopus 로고    scopus 로고
    • JNK deficiency enhances fatty acid utilization and diverts glucose from oxidation to glycogen storage in cultured myotubes
    • Vijayvargia R., et al. JNK deficiency enhances fatty acid utilization and diverts glucose from oxidation to glycogen storage in cultured myotubes. Obesity 2010, 10.1038/oby.2009.501.
    • (2010) Obesity
    • Vijayvargia, R.1
  • 61
    • 58149347680 scopus 로고    scopus 로고
    • Muscle-specific IRS-1 Ser->Ala transgenic mice are protected from fat-induced insulin resistance in skeletal muscle
    • Morino K., et al. Muscle-specific IRS-1 Ser->Ala transgenic mice are protected from fat-induced insulin resistance in skeletal muscle. Diabetes 2008, 57:2644-2651.
    • (2008) Diabetes , vol.57 , pp. 2644-2651
    • Morino, K.1
  • 62
    • 63249101983 scopus 로고    scopus 로고
    • Skeletal muscle-specific deletion of lipoprotein lipase enhances insulin signaling in skeletal muscle but causes insulin resistance in liver and other tissues
    • Wang H., et al. Skeletal muscle-specific deletion of lipoprotein lipase enhances insulin signaling in skeletal muscle but causes insulin resistance in liver and other tissues. Diabetes 2009, 58:116-124.
    • (2009) Diabetes , vol.58 , pp. 116-124
    • Wang, H.1
  • 63
    • 34547942526 scopus 로고    scopus 로고
    • Liver-specific knockdown of JNK1 up-regulates proliferator-activated receptor gamma coactivator 1 beta and increases plasma triglyceride despite reduced glucose and insulin levels in diet-induced obese mice
    • Yang R., et al. Liver-specific knockdown of JNK1 up-regulates proliferator-activated receptor gamma coactivator 1 beta and increases plasma triglyceride despite reduced glucose and insulin levels in diet-induced obese mice. J. Biol. Chem. 2007, 282:22765-22774.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22765-22774
    • Yang, R.1
  • 64
    • 42149155999 scopus 로고    scopus 로고
    • Overexpression of the dual-specificity phosphatase MKP-4/DUSP-9 protects against stress-induced insulin resistance
    • Emanuelli B., et al. Overexpression of the dual-specificity phosphatase MKP-4/DUSP-9 protects against stress-induced insulin resistance. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:3545-3550.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 3545-3550
    • Emanuelli, B.1
  • 65
    • 70449927269 scopus 로고    scopus 로고
    • Prevention of steatosis by hepatic JNK1
    • Sabio G., et al. Prevention of steatosis by hepatic JNK1. Cell Metab. 2009, 10:491-498.
    • (2009) Cell Metab. , vol.10 , pp. 491-498
    • Sabio, G.1
  • 66
    • 56849099017 scopus 로고    scopus 로고
    • Central and peripheral regulation of food intake and physical activity: pathways and genes
    • Lenard N.R., Berthoud H.R. Central and peripheral regulation of food intake and physical activity: pathways and genes. Obesity 2008, 16(Suppl. 3):S11-S22.
    • (2008) Obesity , vol.16 , Issue.SUPPL. 3
    • Lenard, N.R.1    Berthoud, H.R.2
  • 67
    • 76149090834 scopus 로고    scopus 로고
    • Role of the hypothalamic-pituitary-thyroid axis in metabolic regulation by JNK1
    • Sabio G., et al. Role of the hypothalamic-pituitary-thyroid axis in metabolic regulation by JNK1. Genes Dev. 2010, 24:256-264.
    • (2010) Genes Dev. , vol.24 , pp. 256-264
    • Sabio, G.1
  • 68
    • 77950532905 scopus 로고    scopus 로고
    • Hypothalamic and pituitary c-Jun N-terminal kinase 1 signaling coordinately regulates glucose metabolism
    • Belgardt B.F., et al. Hypothalamic and pituitary c-Jun N-terminal kinase 1 signaling coordinately regulates glucose metabolism. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:6028-6033.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 6028-6033
    • Belgardt, B.F.1
  • 69
    • 33846434443 scopus 로고    scopus 로고
    • Involvement of oxidative stress in the pathogenesis of diabetes
    • Kaneto H., et al. Involvement of oxidative stress in the pathogenesis of diabetes. Antioxid. Redox Signal. 2007, 9:355-366.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 355-366
    • Kaneto, H.1
  • 70
    • 59149084125 scopus 로고    scopus 로고
    • Inhibition of C-jun N-terminal kinase improves insulin sensitivity but worsens albuminuria in experimental diabetes
    • Ijaz A., et al. Inhibition of C-jun N-terminal kinase improves insulin sensitivity but worsens albuminuria in experimental diabetes. Kidney Int. 2009, 75:381-388.
    • (2009) Kidney Int. , vol.75 , pp. 381-388
    • Ijaz, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.