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Volumn 33, Issue 2, 2014, Pages 341-350

The role of quantitative changes in the epxression of insulin receptor substrate-1 and nuclear ubiquitin in abnormal glycometabolism in the livers of KKay mice and the relative therapeutic mechanisms of Astragalus polysaccharide

Author keywords

Astragalus polysaccharide; Glycometabolism; Insulin receptor substrate 1; Ubiquitination

Indexed keywords

ASTRAGALUS POLYSACCHARIDE; GLUCOSE; HERBACEOUS AGENT; INSULIN RECEPTOR SUBSTRATE 1; POLYSACCHARIDE; TRIACYLGLYCEROL; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84893797158     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm.2013.1580     Document Type: Article
Times cited : (20)

References (34)
  • 1
    • 84862543951 scopus 로고    scopus 로고
    • From signal transduction to signal interpretation: An alternative model for the molecular function of insulin receptor substrates
    • Boller S, Joblin BA, Xu L, et al: From signal transduction to signal interpretation: An alternative model for the molecular function of insulin receptor substrates. Arch Physiol Biochem 118: 148-155, 2012.
    • (2012) Arch Physiol Biochem , vol.118 , pp. 148-155
    • Boller, S.1    Joblin, B.A.2    Xu, L.3
  • 2
    • 0036710280 scopus 로고    scopus 로고
    • IRS proteins and the common path to diabetes
    • White MF: IRS proteins and the common path to diabetes. Am J Physiol Endocrinol Metab 283: E413-E422, 2002.
    • (2002) Am J Physiol Endocrinol Metab , vol.283
    • White, M.F.1
  • 3
    • 0028032894 scopus 로고
    • Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1
    • Tamemoto H, Kadowaki T, Tobe K, et al: Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1. Nature 372: 182-186, 1994.
    • (1994) Nature , vol.372 , pp. 182-186
    • Tamemoto, H.1    Kadowaki, T.2    Tobe, K.3
  • 4
    • 33749342069 scopus 로고    scopus 로고
    • Molecular mechanisms of insulin resistance: Serine phosphorylation of insulin receptor substrate-1 and increased expression of p85alpha: The two sides of a coin
    • Draznin B: Molecular mechanisms of insulin resistance: Serine phosphorylation of insulin receptor substrate-1 and increased expression of p85alpha: The two sides of a coin. Diabetes 55: 2392-2397, 2006.
    • (2006) Diabetes , vol.55 , pp. 2392-2397
    • Draznin, B.1
  • 5
    • 14544271905 scopus 로고    scopus 로고
    • Positive and negative regulation of insulin signaling through IRS-1 phosphorylation
    • Gual P, Le Marchand-Brustel Y and Tanti JF: Positive and negative regulation of insulin signaling through IRS-1 phos-phorylation. Biochimie 87: 99-109, 2005.
    • (2005) Biochimie , vol.87 , pp. 99-109
    • Gual, P.1    Le Marchand-Brustel, Y.2    Tanti, J.F.3
  • 6
    • 0033982719 scopus 로고    scopus 로고
    • Insulin-like growth factor I-induced degradation of insulin receptor substrate 1 is mediated by the 26S proteasome and blocked by phosphatidylinositol 3'-kinase inhibition
    • Lee AV, Gooch JL, Oesterreich S, Guler RL and Yee D: Insulin-like growth factor I-induced degradation of insulin receptor substrate 1 is mediated by the 26S proteasome and blocked by phosphatidylinositol 3'-kinase inhibition. Mol Cell Biol 20: 1489-1496, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 1489-1496
    • Lee, A.V.1    Gooch, J.L.2    Oesterreich, S.3    Guler, R.L.4    Yee, D.5
  • 7
    • 84864185481 scopus 로고    scopus 로고
    • Improvement of myocardial glycolipid metabolic disorder in diabetic hamster with Astragalus polysaccharides treatment
    • Chen W, Xia YP, Chen WJ, Yu MH, Li YM and Ye HY: Improvement of myocardial glycolipid metabolic disorder in diabetic hamster with Astragalus polysaccharides treatment. Mol Biol Rep 39: 7609-7615, 2012.
    • (2012) Mol Biol Rep , vol.39 , pp. 7609-7615
    • Chen, W.1    Xia, Y.P.2    Chen, W.J.3    Yu, M.H.4    Li, Y.M.5    Ye, H.Y.6
  • 8
    • 67349167991 scopus 로고    scopus 로고
    • Astragalus polysaccharides decreased the expression of PTP1B through relieving ER stress induced activation of ATF6 in a rat model of type 2 diabetes
    • Wang N, Zhang D, Mao X, Zou F, Jin H and Ouyang J: Astragalus polysaccharides decreased the expression of PTP1B through relieving ER stress induced activation of ATF6 in a rat model of type 2 diabetes. Mol Cell Endocrinol 307: 89-98, 2009.
    • (2009) Mol Cell Endocrinol , vol.307 , pp. 89-98
    • Wang, N.1    Zhang, D.2    Mao, X.3    Zou, F.4    Jin, H.5    Ouyang, J.6
  • 9
    • 84893767772 scopus 로고    scopus 로고
    • Astragalus polysaccharide enhances immunity and inhibits H9N2 avian influenza virus in vitro and in vivo
    • Kallon S, Li X, Ji J, et al: Astragalus polysaccharide enhances immunity and inhibits H9N2 avian influenza virus in vitro and in vivo. J Anim Sci Biotechnol 4: 22, 2013.
    • (2013) J Anim Sci Biotechnol , vol.4 , pp. 22
    • Kallon, S.1    Li, X.2    Ji, J.3
  • 10
    • 84876399830 scopus 로고    scopus 로고
    • Astragalus polysaccharide induces anti-inflammatory effects dependent on AMPK activity in palmitate-treated RAW264.7 cells
    • Lu J, Chen X, Zhang Y, et al: Astragalus polysaccharide induces anti-inflammatory effects dependent on AMPK activity in palmitate-treated RAW264.7 cells. Int J Mol Med 31: 1463-1470, 2013.
    • (2013) Int J Mol Med , vol.31 , pp. 1463-1470
    • Lu, J.1    Chen, X.2    Zhang, Y.3
  • 11
    • 15244348325 scopus 로고    scopus 로고
    • Hypoglycemic effect of Astragalus polysaccharide and its effect on PTP1B
    • Wu Y, Ou-Yang JP, Wu K, Wang Y, Zhou YF and Wen CY: Hypoglycemic effect of Astragalus polysaccharide and its effect on PTP1B. Acta Pharmacol Sin 26: 345-352, 2005.
    • (2005) Acta Pharmacol Sin , vol.26 , pp. 345-352
    • Wu, Y.1    Ou-Yang, J.P.2    Wu, K.3    Wang, Y.4    Zhou, Y.F.5    Wen, C.Y.6
  • 12
    • 36649011202 scopus 로고    scopus 로고
    • Astragalus polysaccharide reduces hepatic endoplasmic reticulum stress and restores glucose homeostasis in a diabetic KKAy mouse model
    • Mao XQ, Wu Y, Wu K, Liu M, Zhang JF, Zou F and Ou-Yang JP: Astragalus polysaccharide reduces hepatic endoplasmic reticulum stress and restores glucose homeostasis in a diabetic KKAy mouse model. Acta Pharmacol Sin 28: 1947-1956, 2007.
    • (2007) Acta Pharmacol Sin , vol.28 , pp. 1947-1956
    • Mao, X.Q.1    Wu, Y.2    Wu, K.3    Liu, M.4    Zhang, J.F.5    Zou, F.6    Ou-Yang, J.P.7
  • 13
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel AR and Kahn CR: Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414: 799-806, 2001.
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 14
    • 0033913213 scopus 로고    scopus 로고
    • Signaling pathways in insulin action: Molecular targets of insulin resistance
    • Pessin JE and Saltiel AR: Signaling pathways in insulin action: Molecular targets of insulin resistance. J Clin Invest 106: 165-169, 2000.
    • (2000) J Clin Invest , vol.106 , pp. 165-169
    • Pessin, J.E.1    Saltiel, A.R.2
  • 15
    • 0014743725 scopus 로고
    • General survey of diabetic features of yellow KK mice
    • Iwatsuka H, Shino A and Suzuoki Z: General survey of diabetic features of yellow KK mice. Endocrinol Jpn 17: 23-35, 1970.
    • (1970) Endocrinol Jpn , vol.17 , pp. 23-35
    • Iwatsuka, H.1    Shino, A.2    Suzuoki, Z.3
  • 16
    • 0028912848 scopus 로고
    • Insulin receptor substrate-1 gene mutations in NIDDM; implications for the study of polygenic disease
    • Hitman GA, Hawrami K, McCarthy MI, et al: Insulin receptor substrate-1 gene mutations in NIDDM; implications for the study of polygenic disease. Diabetologia 38: 481-486, 1995.
    • (1995) Diabetologia , vol.38 , pp. 481-486
    • Hitman, G.A.1    Hawrami, K.2    McCarthy, M.I.3
  • 17
    • 0031918624 scopus 로고    scopus 로고
    • The IRS-signalling system: A network of docking proteins that mediate insulin action
    • White MF: The IRS-signalling system: A network of docking proteins that mediate insulin action. Mol Cell Biochem 182: 3-11, 1998.
    • (1998) Mol Cell Biochem , vol.182 , pp. 3-11
    • White, M.F.1
  • 18
    • 0030605399 scopus 로고    scopus 로고
    • The IRS-signalling system in insulin and cytokine action
    • White MF: The IRS-signalling system in insulin and cytokine action. Philos Trans R Soc Lond B Biol Sci 351: 181-189, 1996.
    • (1996) Philos Trans R Soc Lond B Biol Sci , vol.351 , pp. 181-189
    • White, M.F.1
  • 19
    • 33644514920 scopus 로고    scopus 로고
    • Tissue-specific roles of IRS proteins in insulin signaling and glucose transport
    • Thirone AC, Huang C and Klip A: Tissue-specific roles of IRS proteins in insulin signaling and glucose transport. Trends Endocrinol Metab 17: 72-78, 2006.
    • (2006) Trends Endocrinol Metab , vol.17 , pp. 72-78
    • Thirone, A.C.1    Huang, C.2    Klip, A.3
  • 20
    • 45549087567 scopus 로고    scopus 로고
    • Dynamic functional relay between insulin receptor substrate 1 and 2 in hepatic insulin signaling during fasting and feeding
    • Kubota N, Kubota T, Itoh S, et al: Dynamic functional relay between insulin receptor substrate 1 and 2 in hepatic insulin signaling during fasting and feeding. Cell Metab 8: 49-64, 2008.
    • (2008) Cell Metab , vol.8 , pp. 49-64
    • Kubota, N.1    Kubota, T.2    Itoh, S.3
  • 21
    • 0028903232 scopus 로고
    • Insulin receptor phosphorylation, insulin receptor substrate-1 phosphorylation, and phosphatidylinositol 3-kinase activity are decreased in intact skeletal muscle strips from obese subjects
    • Goodyear LJ, Giorgino F, Sherman LA, Carey J, Smith RJ and Dohm GL: Insulin receptor phosphorylation, insulin receptor substrate-1 phosphorylation, and phosphatidylinositol 3-kinase activity are decreased in intact skeletal muscle strips from obese subjects. J Clin Invest 95: 2195-2204, 1995.
    • (1995) J Clin Invest , vol.95 , pp. 2195-2204
    • Goodyear, L.J.1    Giorgino, F.2    Sherman, L.A.3    Carey, J.4    Smith, R.J.5    Dohm, G.L.6
  • 22
    • 0031057526 scopus 로고    scopus 로고
    • Insulin receptor substrate-1 phosphorylation and phosphatidylinositol 3-kinase activity in skeletal muscle from NIDDM subjects after in vivo insulin stimulation
    • Björnholm M, Kawano Y, Lehtihet M and Zierath JR: Insulin receptor substrate-1 phosphorylation and phosphatidylinositol 3-kinase activity in skeletal muscle from NIDDM subjects after in vivo insulin stimulation. Diabetes 46: 524-527, 1997.
    • (1997) Diabetes , vol.46 , pp. 524-527
    • Björnholm, M.1    Kawano, Y.2    Lehtihet, M.3    Zierath, J.R.4
  • 23
    • 0343314906 scopus 로고    scopus 로고
    • Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients
    • Krook A, Björnholm M, Galuska D, et al: Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients. Diabetes 49: 284-292, 2000.
    • (2000) Diabetes , vol.49 , pp. 284-292
    • Krook, A.1    Björnholm, M.2    Galuska, D.3
  • 24
    • 0032523085 scopus 로고    scopus 로고
    • Hypertension, hypertriglyceridemia, and impaired endothelium-dependent vascular relaxation in mice lacking insulin receptor substrate-1
    • Abe H, Yamada N, Kamata K, et al: Hypertension, hypertriglyceridemia, and impaired endothelium-dependent vascular relaxation in mice lacking insulin receptor substrate-1. J Clin Invest 101: 1784-1788, 1998.
    • (1998) J Clin Invest , vol.101 , pp. 1784-1788
    • Abe, H.1    Yamada, N.2    Kamata, K.3
  • 25
    • 14644426519 scopus 로고    scopus 로고
    • Complementary roles of IRS-1 and IRS-2 in the hepatic regulation of metabolism
    • Taniguchi CM, Ueki K and Kahn R: 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
  • 26
    • 84874189145 scopus 로고    scopus 로고
    • Central role of E3 ubiquitin ligase MG53 in insulin resistance and metabolic disorders
    • Song R, Peng W, Zhang Y, et al: Central role of E3 ubiquitin ligase MG53 in insulin resistance and metabolic disorders. Nature 494: 375-379, 2013.
    • (2013) Nature , vol.494 , pp. 375-379
    • Song, R.1    Peng, W.2    Zhang, Y.3
  • 27
    • 84876346064 scopus 로고    scopus 로고
    • Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells
    • Chen YC, Fueger PT and Wang Z: Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells. Islets 5: 22-28, 2013.
    • (2013) Islets , vol.5 , pp. 22-28
    • Chen, Y.C.1    Fueger, P.T.2    Wang, Z.3
  • 28
    • 84874273753 scopus 로고    scopus 로고
    • An extract of Artemisia dracunculus L. Inhibits ubiquitin-proteasome activity and preserves skeletal muscle mass in a murine model of diabetes
    • Kirk-Ballard H, Wang ZQ, Acharya P, et al: An extract of Artemisia dracunculus L. inhibits ubiquitin-proteasome activity and preserves skeletal muscle mass in a murine model of diabetes. PLoS One 8: E57112, 2013.
    • (2013) PLoS One , vol.8
    • Kirk-Ballard, H.1    Wang, Z.Q.2    Acharya, P.3
  • 29
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • Conaway RC, Brower CS and Conaway JW: Emerging roles of ubiquitin in transcription regulation. Science 296: 1254-1258, 2002.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 30
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M and Tansey WP: How the ubiquitin-proteasome system controls transcription. Nat Rev Mol Cell Biol 4: 192-201, 2003.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 31
    • 84856487109 scopus 로고    scopus 로고
    • The story so far: Post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation
    • Wadosky KM and Willis MS: The story so far: Post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation. Am J Physiol Heart Circ Physiol 302: H515-H526, 2012.
    • (2012) Am J Physiol Heart Circ Physiol , vol.302
    • Wadosky, K.M.1    Willis, M.S.2
  • 32
    • 84876436586 scopus 로고    scopus 로고
    • Upregulation of SIRT1 by 17β-estradiol depends on ubiquitin-proteasome degradation of PPAR-? Mediated by NEDD4-1
    • Han L, Wang P, Zhao G, Wang H, Wang M, Chen J and Tong T: Upregulation of SIRT1 by 17β-estradiol depends on ubiquitin-proteasome degradation of PPAR-? mediated by NEDD4-1. Protein Cell 4: 310-321, 2013.
    • (2013) Protein Cell , vol.4 , pp. 310-321
    • Han, L.1    Wang, P.2    Zhao, G.3    Wang, H.4    Wang, M.5    Chen, J.6    Tong, T.7
  • 33
    • 84857393204 scopus 로고    scopus 로고
    • The ubiquitin ligase Siah2 regulates PPAR? Activity in adipocytes
    • Kilroy G, Kirk-Ballard H, Carter LE and Floyd ZE: The ubiquitin ligase Siah2 regulates PPAR? activity in adipocytes. Endocrinology 153: 1206-1218, 2012.
    • (2012) Endocrinology , vol.153 , pp. 1206-1218
    • Kilroy, G.1    Kirk-Ballard, H.2    Carter, L.E.3    Floyd, Z.E.4
  • 34
    • 84867369739 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma and regulations by the ubiquitin-proteasome system in pancreatic cancer
    • Stravodimou A, Mazzoccoli G and Voutsadakis IA: Peroxisome proliferator-activated receptor gamma and regulations by the ubiquitin-proteasome system in pancreatic cancer. PPAR Res 2012: 367450, 2012.
    • (2012) PPAR Res , vol.2012 , pp. 367450
    • Stravodimou, A.1    Mazzoccoli, G.2    Voutsadakis, I.A.3


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