High levels of palmitic acid lead to insulin resistance due to changes in the level of phosphorylation of the insulin receptor and insulin receptor substrate-1
暂无分享,去创建一个
[1] J. Chen,et al. Protein Kinase C-ζ Phosphorylates Insulin Receptor Substrate-1 and Impairs Its Ability to Activate Phosphatidylinositol 3-Kinase in Response to Insulin* , 2001, The Journal of Biological Chemistry.
[2] C. Schmitz‐Peiffer. Signalling aspects of insulin resistance in skeletal muscle: mechanisms induced by lipid oversupply. , 2000, Cellular signalling.
[3] B. Ursø,et al. Signalling through the insulin receptor. , 2000, Current opinion in cell biology.
[4] H. Klein,et al. Serine residues 994 and 1023/25 are important for insulin receptor kinase inhibition by protein kinase C isoforms beta2 and theta. , 2000, Diabetologia.
[5] G. Müller,et al. Cross-talk mechanisms in the development of insulin resistance of skeletal muscle cells palmitate rather than tumour necrosis factor inhibits insulin-dependent protein kinase B (PKB)/Akt stimulation and glucose uptake. , 1999, European journal of biochemistry.
[6] M. Quon,et al. Insulin signalling: metabolic pathways and mechanisms for specificity. , 1999, Cellular signalling.
[7] M. Czech,et al. Signaling Mechanisms That Regulate Glucose Transport* , 1999, The Journal of Biological Chemistry.
[8] D L Rothman,et al. Effects of free fatty acids on glucose transport and IRS-1-associated phosphatidylinositol 3-kinase activity. , 1999, The Journal of clinical investigation.
[9] R. Roth,et al. Modulation of Insulin Receptor Substrate-1 Tyrosine Phosphorylation and Function by Mitogen-activated Protein Kinase* , 1997, The Journal of Biological Chemistry.
[10] G. Boden. Role of Fatty Acids in the Pathogenesis of Insulin Resistance and NIDDM , 1997, Diabetes.
[11] R. Farese,et al. Chronic Activation of Protein Kinase C in Soleus Muscles and Other Tissues of Insulin-Resistant Type II diabetic Goto-Kakizaki (GK), Obese/Aged, and Obese/Zucker Rats: A Mechanism For Inhibiting Glycogen Synthesis , 1996, Diabetes.
[12] K. Petersen,et al. Mechanism of free fatty acid-induced insulin resistance in humans. , 1996, The Journal of clinical investigation.
[13] R. Considine,et al. Protein kinase C is increased in the liver of humans and rats with non-insulin-dependent diabetes mellitus: an alteration not due to hyperglycemia. , 1995, The Journal of clinical investigation.
[14] F. Giorgino,et al. Insulin receptor phosphorylation, insulin receptor substrate-1 phosphorylation, and phosphatidylinositol 3-kinase activity are decreased in intact skeletal muscle strips from obese subjects. , 1995, The Journal of clinical investigation.
[15] R. Roth,et al. Identification of serines‐1035/1037 in the kinase domain of the insulin receptor as protein kinase Cα mediated phosphorylation sites , 1994, FEBS letters.
[16] L. Rossetti,et al. Mechanisms of fatty acid-induced inhibition of glucose uptake. , 1994, The Journal of clinical investigation.
[17] A. Boneh,et al. Effect of fatty acids and their acyl-CoA esters on protein kinase C activity in fibroblasts: possible implications in fatty acid oxidation defects. , 1994, Biochimica et biophysica acta.
[18] H. Häring,et al. Glucose-induced translocation of protein kinase C isoforms in rat-1 fibroblasts is paralleled by inhibition of the insulin receptor tyrosine kinase. , 1994, The Journal of biological chemistry.
[19] R. Considine,et al. Protein kinase C: Mediator or inhibitor of insulin action? , 1993, Journal of cellular biochemistry.
[20] L. Groop,et al. Contribution of muscle and liver to glucose-fatty acid cycle in humans. , 1993, The American journal of physiology.
[21] J. Tavaré,et al. Overexpression of protein kinase C isoenzymes alpha, beta I, gamma, and epsilon in cells overexpressing the insulin receptor. Effects on receptor phosphorylation and signaling. , 1993, The Journal of biological chemistry.
[22] H. Häring,et al. Prevention by Protein Kinase C Inhibitors of Glucose-Induced Insulin-Receptor Tyrosine Kinase Resistance in Rat Fat Cells , 1991, Diabetes.
[23] H. Yki-Järvinen,et al. Effect of free fatty acids on glucose uptake and nonoxidative glycolysis across human forearm tissues in the basal state and during insulin stimulation. , 1991, The Journal of clinical endocrinology and metabolism.
[24] C. Kahn,et al. Purification and partial sequence analysis of pp185, the major cellular substrate of the insulin receptor tyrosine kinase. , 1991, The Journal of biological chemistry.
[25] P. Björntorp,et al. Free–Fatty Acid Inhibition of Insulin Binding, Degradation, and Action in Isolated Rat Hepatocytes , 1990, Diabetes.
[26] G. Reaven. Role of Insulin Resistance in Human Disease , 1988, Diabetes.
[27] C. Kahn,et al. Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity. , 1988, The Journal of biological chemistry.
[28] E. Ferrannini,et al. Acute elevation of free fatty acid levels leads to hepatic insulin resistance in obese subjects. , 1987, Metabolism: clinical and experimental.
[29] C. Kahn,et al. Effects of Heparin on Insulin Binding and Biological Activity , 1987, Diabetes.
[30] C. Kahn,et al. Maintenance of 3T3-L1 cells in culture media containing saturated fatty acids decreases insulin binding and insulin action. , 1981, Biochemical and biophysical research communications.
[31] K. Itaya,et al. COLORIMETRIC DETERMINATION OF FREE FATTY ACIDS IN BIOLOGICAL FLUIDS. , 1965, Journal of lipid research.
[32] E. Newsholme,et al. The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus. , 1963, Lancet.