메뉴 건너뛰기




Volumn 34, Issue 1, 1997, Pages 3-24

Actions of insulin on the mammalian heart: Metabolism, pathology and biochemical mechanisms

Author keywords

Diabetes; Glucose transport; Insulin; Myocardial metabolism; Signal transduction

Indexed keywords

FATTY ACID; GLUCOSE; GLYCOGEN; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR SUBSTRATE 1; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN TYROSINE KINASE; PYRUVATE DEHYDROGENASE COMPLEX; RAS PROTEIN;

EID: 0030900355     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(97)00051-5     Document Type: Review
Times cited : (118)

References (263)
  • 1
    • 0028904053 scopus 로고
    • Insulin action and the insulin signaling network
    • Cheatham B, Kahn CR. Insulin action and the insulin signaling network. Endocr Rev 1995;16:117-142.
    • (1995) Endocr Rev , vol.16 , pp. 117-142
    • Cheatham, B.1    Kahn, C.R.2
  • 2
    • 0027194749 scopus 로고
    • Dissection of the protein phosphorylation cascades involved in insulin and growth factor action
    • Cohen P. Dissection of the protein phosphorylation cascades involved in insulin and growth factor action. Biochem Soc Trans 1993;1:555-567.
    • (1993) Biochem Soc Trans , vol.1 , pp. 555-567
    • Cohen, P.1
  • 3
    • 0026591098 scopus 로고
    • Signal transduction and protein phosphorylation in the regulation of cellular metabolism by insulin
    • Lawrence JC. Signal transduction and protein phosphorylation in the regulation of cellular metabolism by insulin. Annu Rev Physiol 1992;54:177-193.
    • (1992) Annu Rev Physiol , vol.54 , pp. 177-193
    • Lawrence, J.C.1
  • 4
    • 0028278931 scopus 로고
    • The insulin receptor. Structure, function, and signaling
    • Lee J, Pilch PF. The insulin receptor. Structure, function, and signaling. Am J Physiol 1994;266:C319-C334.
    • (1994) Am J Physiol , vol.266
    • Lee, J.1    Pilch, P.F.2
  • 5
    • 33646327467 scopus 로고
    • Mitochondria
    • Drake-Holland AJ, Noble MIM, eds. New York: John Wiley and Sons
    • Williams A. Mitochondria. In: Drake-Holland AJ, Noble MIM, eds. Cardiac Metabolism. New York: John Wiley and Sons, 1983:151.
    • (1983) Cardiac Metabolism , pp. 151
    • Williams, A.1
  • 7
    • 0022634281 scopus 로고
    • The calcium messenger system
    • Rasmussen H. The calcium messenger system. N Engl J Med 1986;314:1094-1101,1164-1170.
    • (1986) N Engl J Med , vol.314 , pp. 1094-1101
    • Rasmussen, H.1
  • 8
    • 0025760022 scopus 로고
    • Some thoughts on the mechanism of action of insulin
    • Exton JH. Some thoughts on the mechanism of action of insulin. Diabetes 1991;40:521-526.
    • (1991) Diabetes , vol.40 , pp. 521-526
    • Exton, J.H.1
  • 9
    • 0014062060 scopus 로고
    • Histochemical and chemical studies of the localization of adrenergic and cholinergic nerves in normal and denervated cat hearts
    • Jacobowitz D, Cooper T, Barner HB. Histochemical and chemical studies of the localization of adrenergic and cholinergic nerves in normal and denervated cat hearts. Circ Res 1967;20:289-298.
    • (1967) Circ Res , vol.20 , pp. 289-298
    • Jacobowitz, D.1    Cooper, T.2    Barner, H.B.3
  • 10
    • 0022635415 scopus 로고
    • Regulation of adenosine formation by the heart
    • Sparks HV, Bardenheuer H. Regulation of adenosine formation by the heart. Circ Res 1986;58:193-201.
    • (1986) Circ Res , vol.58 , pp. 193-201
    • Sparks, H.V.1    Bardenheuer, H.2
  • 11
    • 0026776555 scopus 로고
    • Adenosine modification of energy substrate use in isolated hearts perfused with fatty acids
    • Finegan BA, Clanachan AS, Coulson CS, Lopaschuk GD. Adenosine modification of energy substrate use in isolated hearts perfused with fatty acids. Am J Physiol 1992;262:H1501-H1507.
    • (1992) Am J Physiol , vol.262
    • Finegan, B.A.1    Clanachan, A.S.2    Coulson, C.S.3    Lopaschuk, G.D.4
  • 12
    • 0028331705 scopus 로고
    • The family of guanylyl cyclase receptors and their ligands
    • Drewett JG, Garbers DL. The family of guanylyl cyclase receptors and their ligands. Endocr Rev 1994;15:135-162.
    • (1994) Endocr Rev , vol.15 , pp. 135-162
    • Drewett, J.G.1    Garbers, D.L.2
  • 13
    • 0029896361 scopus 로고    scopus 로고
    • The heart communicates with the kidney exclusively through the guanylyl cyclase-A receptor - Acute handling of sodium and water in response to volume expansion
    • Kishimoto I, Dubois SK, Garbers DL. The heart communicates with the kidney exclusively through the guanylyl cyclase-A receptor - acute handling of sodium and water in response to volume expansion. Proc Natl Acad Sci USA 1996;93:6215-6219.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6215-6219
    • Kishimoto, I.1    Dubois, S.K.2    Garbers, D.L.3
  • 14
    • 0028085621 scopus 로고
    • Hemodynamic actions of insulin
    • Baron AD. Hemodynamic actions of insulin. Am J Physiol 1994;267:E187-E202.
    • (1994) Am J Physiol , vol.267
    • Baron, A.D.1
  • 16
    • 0015172777 scopus 로고
    • Physiology of insulin in man
    • Cahill GF. Physiology of insulin in man. Diabetes 1971;20:785-799.
    • (1971) Diabetes , vol.20 , pp. 785-799
    • Cahill, G.F.1
  • 18
    • 0023118407 scopus 로고
    • Cachectin: More than a tumor necrosis factor
    • Beutler B, Cerami A. Cachectin: more than a tumor necrosis factor. N Engl J Med 1987;316:379-385.
    • (1987) N Engl J Med , vol.316 , pp. 379-385
    • Beutler, B.1    Cerami, A.2
  • 19
    • 50549202600 scopus 로고
    • The glucose fatty acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus
    • Randle PJ, Hales CN, Garland PB, Newsholme EA. The glucose fatty acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus. Lancet 1963;1:785-789.
    • (1963) Lancet , vol.1 , pp. 785-789
    • Randle, P.J.1    Hales, C.N.2    Garland, P.B.3    Newsholme, E.A.4
  • 20
    • 0013979474 scopus 로고
    • Interactions of metabolism and the physiological role of insulin
    • Randle PJ, Garland PB, Hales CN, et al. Interactions of metabolism and the physiological role of insulin. Recent Prog Hormone Res 1966;22:1-44.
    • (1966) Recent Prog Hormone Res , vol.22 , pp. 1-44
    • Randle, P.J.1    Garland, P.B.2    Hales, C.N.3
  • 21
    • 0023101018 scopus 로고
    • Secretion of lipids, apolipoproteins and lipoproteins by human hepatoma cell line, HepG2: Effects of oleic acid and insulin
    • Dashti N, Wofbauer G. Secretion of lipids, apolipoproteins and lipoproteins by human hepatoma cell line, HepG2: effects of oleic acid and insulin. J Lipid Res 1987;28:423-426.
    • (1987) J Lipid Res , vol.28 , pp. 423-426
    • Dashti, N.1    Wofbauer, G.2
  • 22
    • 0028839110 scopus 로고
    • Interaction between free fatty acids and insulin in the acute control of very low density lipoprotein production in humans
    • Lewis GF, Uffelman KD, Szeto LW, Weller B, Steiner G. Interaction between free fatty acids and insulin in the acute control of very low density lipoprotein production in humans. J Clin Invest 1995;95:158-166.
    • (1995) J Clin Invest , vol.95 , pp. 158-166
    • Lewis, G.F.1    Uffelman, K.D.2    Szeto, L.W.3    Weller, B.4    Steiner, G.5
  • 23
    • 0014760937 scopus 로고
    • Effect of fasting on the clearing factor lipase (lipoprotein lipase) activity of defatted preparations of rat heart muscle
    • Bjorensztajn J, Otway S, Robinson DS. Effect of fasting on the clearing factor lipase (lipoprotein lipase) activity of defatted preparations of rat heart muscle. J Lipid Res 1970;11:102-110.
    • (1970) J Lipid Res , vol.11 , pp. 102-110
    • Bjorensztajn, J.1    Otway, S.2    Robinson, D.S.3
  • 24
    • 0014752306 scopus 로고
    • The effect of fasting on the utilization of chylomicron triglyceride fatty acids in relation to clearing factor lipase (lipoprotein lipase) releasable by heparin in the perfused rat heart
    • Bjorensztajn J, Robinson DS. The effect of fasting on the utilization of chylomicron triglyceride fatty acids in relation to clearing factor lipase (lipoprotein lipase) releasable by heparin in the perfused rat heart. J Lipid Res 1970;11:111-117.
    • (1970) J Lipid Res , vol.11 , pp. 111-117
    • Bjorensztajn, J.1    Robinson, D.S.2
  • 25
    • 0025737936 scopus 로고
    • Restoration of lipoprotein lipase activity in insulin-deficient rats by insulin infusion is tissue-specific
    • Deshaies Y, Geloen A, Paulin A, Bukowieki LJ. Restoration of lipoprotein lipase activity in insulin-deficient rats by insulin infusion is tissue-specific. Can J Physiol Pharmacol 1991;69:746-751.
    • (1991) Can J Physiol Pharmacol , vol.69 , pp. 746-751
    • Deshaies, Y.1    Geloen, A.2    Paulin, A.3    Bukowieki, L.J.4
  • 27
    • 0029008947 scopus 로고
    • Insulin, ketones, and mitochondrial energy transduction
    • Satoh K, Kashiwaya Y, Keon CA, et al. Insulin, ketones, and mitochondrial energy transduction. FASEB J 1995;9:651-658.
    • (1995) FASEB J , vol.9 , pp. 651-658
    • Satoh, K.1    Kashiwaya, Y.2    Keon, C.A.3
  • 28
    • 0028986759 scopus 로고
    • Diabetic ketoacidosis
    • Lebovitz HE. Diabetic ketoacidosis. Lancet 1995;345:767-772.
    • (1995) Lancet , vol.345 , pp. 767-772
    • Lebovitz, H.E.1
  • 29
    • 0028030813 scopus 로고
    • Insulin-mediated skeletal muscle vasodilation is nitric oxide dependent. A novel action of insulin to increase nitric oxide release
    • Steinberg HO, Brechtel G, Johnson A, Fineberg N, Baron AD. Insulin-mediated skeletal muscle vasodilation is nitric oxide dependent. A novel action of insulin to increase nitric oxide release. J Clin Invest 1994;94:1171-1179.
    • (1994) J Clin Invest , vol.94 , pp. 1171-1179
    • Steinberg, H.O.1    Brechtel, G.2    Johnson, A.3    Fineberg, N.4    Baron, A.D.5
  • 30
    • 0024160877 scopus 로고
    • Role of insulin resistance in human disease
    • Reaven GM. Role of insulin resistance in human disease. Diabetes 1988;37:1595-1607.
    • (1988) Diabetes , vol.37 , pp. 1595-1607
    • Reaven, G.M.1
  • 31
    • 0029037649 scopus 로고
    • Pathophysiology of insulin resistance in human disease
    • Reaven GM. Pathophysiology of insulin resistance in human disease. Physiol Rev 1995;75:473-486.
    • (1995) Physiol Rev , vol.75 , pp. 473-486
    • Reaven, G.M.1
  • 32
    • 0028901028 scopus 로고
    • Enhancement of insulin sensitivity by troglitazone lowers blood pressure in diabetic hypertensives
    • Ogihara T, Rakugi H, Ikegami H, Mikami H, Masuo K. Enhancement of insulin sensitivity by troglitazone lowers blood pressure in diabetic hypertensives. Am J Hypertens 1995;8:316-320.
    • (1995) Am J Hypertens , vol.8 , pp. 316-320
    • Ogihara, T.1    Rakugi, H.2    Ikegami, H.3    Mikami, H.4    Masuo, K.5
  • 33
    • 0029142479 scopus 로고
    • Blood pressure lowering by pioglitazone. Evidence for a direct vascular effect
    • Buchanan TA, Meehan WP, Jeng YY, et al. Blood pressure lowering by pioglitazone. Evidence for a direct vascular effect. J Clin Invest 1995;96:354-360.
    • (1995) J Clin Invest , vol.96 , pp. 354-360
    • Buchanan, T.A.1    Meehan, W.P.2    Jeng, Y.Y.3
  • 34
    • 0029149884 scopus 로고
    • Clinical implications of insulin resistance syndromes
    • Davidson MB. Clinical implications of insulin resistance syndromes. Am J Med 1995;99:420-426.
    • (1995) Am J Med , vol.99 , pp. 420-426
    • Davidson, M.B.1
  • 35
    • 0028961110 scopus 로고
    • Diabetes and cardiovascular disease: The 'common soil' hypothesis
    • Stern MP. Diabetes and cardiovascular disease: the 'common soil' hypothesis. Diabetes 1995;44:369-374.
    • (1995) Diabetes , vol.44 , pp. 369-374
    • Stern, M.P.1
  • 36
    • 0015120055 scopus 로고
    • Effects of increased heart work on glycolysis and adenine nucleotides in the perfused heart of normal and diabetic rats
    • Opie LH, Mansford KRL, Owen P. Effects of increased heart work on glycolysis and adenine nucleotides in the perfused heart of normal and diabetic rats. Biochem J 1971;124:475-490.
    • (1971) Biochem J , vol.124 , pp. 475-490
    • Opie, L.H.1    Mansford, K.R.L.2    Owen, P.3
  • 37
    • 0017161616 scopus 로고
    • Effects of mechanical activity and hormones on myocardial glucose and fatty acid utilization
    • Neely JR, Whitmer KM, Mochizuki S. Effects of mechanical activity and hormones on myocardial glucose and fatty acid utilization. Circ Res 1976;38:I22-I30.
    • (1976) Circ Res , vol.38
    • Neely, J.R.1    Whitmer, K.M.2    Mochizuki, S.3
  • 39
    • 33744991595 scopus 로고
    • Fatty acid and glucose metabolism in the perfused heart
    • Shipp JC, Opie LH, Challoner DR. Fatty acid and glucose metabolism in the perfused heart. Nature 1961;189:1018-1019.
    • (1961) Nature , vol.189 , pp. 1018-1019
    • Shipp, J.C.1    Opie, L.H.2    Challoner, D.R.3
  • 40
    • 0000525779 scopus 로고
    • Inhibition of the phosphofructokinase reaction in perfused rat heart by respiration of ketone bodies, fatty acids and pyruvate
    • Newsholme EA, Randle PJ, Manchester KL. Inhibition of the phosphofructokinase reaction in perfused rat heart by respiration of ketone bodies, fatty acids and pyruvate. Nature 1962;193:270-271.
    • (1962) Nature , vol.193 , pp. 270-271
    • Newsholme, E.A.1    Randle, P.J.2    Manchester, K.L.3
  • 41
    • 0001754053 scopus 로고
    • Acetoacetate as fuel of respiration in the perfused rat heart
    • Williamson JR, Krebs HA. Acetoacetate as fuel of respiration in the perfused rat heart . Biochem J 1961;80:540-547.
    • (1961) Biochem J , vol.80 , pp. 540-547
    • Williamson, J.R.1    Krebs, H.A.2
  • 42
    • 0015243566 scopus 로고
    • Relationship in man between plasma free fatty acids and myocardial metabolism of carbohydrate substrates
    • Lassers RW, Kaijser L, Wahlquist ML, Carlson LA. Relationship in man between plasma free fatty acids and myocardial metabolism of carbohydrate substrates. Lancet 1971;2:448-450.
    • (1971) Lancet , vol.2 , pp. 448-450
    • Lassers, R.W.1    Kaijser, L.2    Wahlquist, M.L.3    Carlson, L.A.4
  • 43
    • 0015789942 scopus 로고
    • Effects of dichloroacetate on the metabolism of glucose, pyruvate, acetate, 3-hydroxybutyrate and palmitate in rat diaphragm and heart muscle in vitro and on extractions of glucose, lactate, pyruvate and free fatty acids by dog heart in vivo
    • McAllister A, Allison SP, Randle PJ. Effects of dichloroacetate on the metabolism of glucose, pyruvate, acetate, 3-hydroxybutyrate and palmitate in rat diaphragm and heart muscle in vitro and on extractions of glucose, lactate, pyruvate and free fatty acids by dog heart in vivo. Biochem J 1973;134:1067-1081.
    • (1973) Biochem J , vol.134 , pp. 1067-1081
    • McAllister, A.1    Allison, S.P.2    Randle, P.J.3
  • 44
    • 0026691368 scopus 로고
    • Glucose-free fatty acid cycle operates in human heart and skeletal muscle in vivo
    • Nuutila P, Koivisto VA, Knuuti J, et al. Glucose-free fatty acid cycle operates in human heart and skeletal muscle in vivo. J Clin Invest 1992;89:1767-1774.
    • (1992) J Clin Invest , vol.89 , pp. 1767-1774
    • Nuutila, P.1    Koivisto, V.A.2    Knuuti, J.3
  • 45
    • 1842389677 scopus 로고
    • Relationship between carbohydrate and lipid metabolism and the energy balance of heart muscle
    • Neely JR, Morgan HE. Relationship between carbohydrate and lipid metabolism and the energy balance of heart muscle. Annu Rev Physiol 1974;36:413-459.
    • (1974) Annu Rev Physiol , vol.36 , pp. 413-459
    • Neely, J.R.1    Morgan, H.E.2
  • 46
    • 0028347762 scopus 로고
    • Glucose transport and phosphorylation in single cardiac myocytesrate-limiting steps in glucose metabolism
    • Manchester J, Kong X, Nerbonne J, Lowry OH, Lawrence JC. Glucose transport and phosphorylation in single cardiac myocytesrate-limiting steps in glucose metabolism. Am J Physiol 1994;266:E326-E333.
    • (1994) Am J Physiol , vol.266
    • Manchester, J.1    Kong, X.2    Nerbonne, J.3    Lowry, O.H.4    Lawrence, J.C.5
  • 47
    • 0027970353 scopus 로고
    • Control of glucose utilization in working perfused rat heart
    • Kashiwaya Y, Sato K, Tsuchiya N, et al. Control of glucose utilization in working perfused rat heart. J Biol Chem 1994;269:25502-25514.
    • (1994) J Biol Chem , vol.269 , pp. 25502-25514
    • Kashiwaya, Y.1    Sato, K.2    Tsuchiya, N.3
  • 48
    • 0018820017 scopus 로고
    • Potential mechanism of insulin action on glucose transport in isolated rat adipose cells: Apparent translocation of intracellular transport systems to the plasma membrane
    • Cushman SW, Wardzala LJ. Potential mechanism of insulin action on glucose transport in isolated rat adipose cells: apparent translocation of intracellular transport systems to the plasma membrane. J Biol Chem 1980;255:4758-4762.
    • (1980) J Biol Chem , vol.255 , pp. 4758-4762
    • Cushman, S.W.1    Wardzala, L.J.2
  • 49
    • 0008385878 scopus 로고
    • Evidence that insulin causes the translocation of glucose transport activity to the plasma membrane from an intracellular storage site
    • Suzuki K, Kono T. Evidence that insulin causes the translocation of glucose transport activity to the plasma membrane from an intracellular storage site. Proc Natl Acad Sci USA 1980;77:2542-2545.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2542-2545
    • Suzuki, K.1    Kono, T.2
  • 50
    • 0026490523 scopus 로고
    • Regulation of glucose transport in skeletal muscle
    • Barnard RJ, Youngren JF. Regulation of glucose transport in skeletal muscle. FASEB J 1992;6:3238-3244.
    • (1992) FASEB J , vol.6 , pp. 3238-3244
    • Barnard, R.J.1    Youngren, J.F.2
  • 51
    • 0027420730 scopus 로고
    • The glucose transporter family: Structure, function and tissue-specific expression
    • Gould GW, Holman GD. The glucose transporter family: structure, function and tissue-specific expression. Biochem J 1993;295:329-341.
    • (1993) Biochem J , vol.295 , pp. 329-341
    • Gould, G.W.1    Holman, G.D.2
  • 52
    • 0028152377 scopus 로고
    • Facilitative glucose transporters
    • Mueckler M. Facilitative glucose transporters. Eur J Biochem 1994;219:713-725.
    • (1994) Eur J Biochem , vol.219 , pp. 713-725
    • Mueckler, M.1
  • 53
    • 0027290847 scopus 로고
    • Use of bismannose photolabel to elucidate insulin-regulated GLUT4 subcellular trafficking kinetics in rat adipose cells
    • Satoh S, Nishimura H, Clark AE, et al. Use of bismannose photolabel to elucidate insulin-regulated GLUT4 subcellular trafficking kinetics in rat adipose cells. J Biol Chem 1993;268:17820-17829.
    • (1993) J Biol Chem , vol.268 , pp. 17820-17829
    • Satoh, S.1    Nishimura, H.2    Clark, A.E.3
  • 54
    • 0028321736 scopus 로고
    • Insulin-stimulated GLUT4 glucose transporter recycling: A problem in membrane protein subcellular trafficking through multiple pools
    • Holman GD, Leggio LL, Cushman SW. Insulin-stimulated GLUT4 glucose transporter recycling: a problem in membrane protein subcellular trafficking through multiple pools. J Biol Chem 1994;269:17516-17524.
    • (1994) J Biol Chem , vol.269 , pp. 17516-17524
    • Holman, G.D.1    Leggio, L.L.2    Cushman, S.W.3
  • 55
    • 0021717075 scopus 로고
    • Insulin action on glucose transport in cardiac muscle
    • Watanabe T, Smith MM, Robinson FW, Kono T. Insulin action on glucose transport in cardiac muscle. J Biol Chem 1984;259:13117-13122.
    • (1984) J Biol Chem , vol.259 , pp. 13117-13122
    • Watanabe, T.1    Smith, M.M.2    Robinson, F.W.3    Kono, T.4
  • 57
    • 0028358976 scopus 로고
    • Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: Studies on the role of small-molecular-mass GTP-binding proteins
    • Uphues I, Kolter T, Goud B, Eckel J. Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: studies on the role of small-molecular-mass GTP-binding proteins. Biochem J 1994;301:177-182.
    • (1994) Biochem J , vol.301 , pp. 177-182
    • Uphues, I.1    Kolter, T.2    Goud, B.3    Eckel, J.4
  • 58
    • 33646287617 scopus 로고    scopus 로고
    • Insulin stimulates translocation of both GLUT4 and GLUT1 in the heart
    • Abstract 1794
    • Russell RR, Yin R, Xiaoyue H, et al. Insulin stimulates translocation of both GLUT4 and GLUT1 in the heart. Circulation 1996;24(suppl I):I308. (Abstract 1794).
    • (1996) Circulation , vol.24 , Issue.1 SUPPL.
    • Russell, R.R.1    Yin, R.2    Xiaoyue, H.3
  • 59
    • 0026782176 scopus 로고
    • Immunocytochemical and biochemical studies of GLUT4 in rat skeletal muscle
    • Rodnick KJ, Slot JW, Studelska DR, et al. Immunocytochemical and biochemical studies of GLUT4 in rat skeletal muscle. J Biol Chem 1992;267:6278-6285.
    • (1992) J Biol Chem , vol.267 , pp. 6278-6285
    • Rodnick, K.J.1    Slot, J.W.2    Studelska, D.R.3
  • 60
    • 0023131917 scopus 로고
    • Distribution of glucose transporters and insulin receptors in the plasma membrane and transverse tubules of skeletal muscle
    • Burdett E, Beeler T, Klip A. Distribution of glucose transporters and insulin receptors in the plasma membrane and transverse tubules of skeletal muscle. Arch Biochem Biophys 1987;253:279-286.
    • (1987) Arch Biochem Biophys , vol.253 , pp. 279-286
    • Burdett, E.1    Beeler, T.2    Klip, A.3
  • 61
    • 0027314964 scopus 로고
    • Role of transverse tubules in insulin stimulated muscle glucose transport
    • Dohm GL, Dolan PL, Frisell WR, Dudek RW. Role of transverse tubules in insulin stimulated muscle glucose transport. J Cell Biochem 1993;52:1-7.
    • (1993) J Cell Biochem , vol.52 , pp. 1-7
    • Dohm, G.L.1    Dolan, P.L.2    Frisell, W.R.3    Dudek, R.W.4
  • 62
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE. Mechanisms of intracellular protein transport. Nature 1994;372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 63
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof TC. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 1995;375:645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.C.1
  • 64
    • 0026780311 scopus 로고
    • Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes
    • Cain CC, Trimble WS, Lienhard GE. Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes. J Biol Chem 1992;267:11681-11684.
    • (1992) J Biol Chem , vol.267 , pp. 11681-11684
    • Cain, C.C.1    Trimble, W.S.2    Lienhard, G.E.3
  • 66
    • 0024592462 scopus 로고
    • Molecular cloning and characterization of an insulin-regulatable glucose transporter
    • James DE, Strube M, Mueckler M. Molecular cloning and characterization of an insulin-regulatable glucose transporter. Nature 1989;338:83-87.
    • (1989) Nature , vol.338 , pp. 83-87
    • James, D.E.1    Strube, M.2    Mueckler, M.3
  • 67
    • 0027421707 scopus 로고
    • Glucose transporters and in vivo glucose uptake in skeletal and cardiac muscle: Fasting, insulin stimulation and immunoisolation studies of GLUT1 and GLUT4
    • Kraegen EW, Sowden JA, Halstead MB, et al. Glucose transporters and in vivo glucose uptake in skeletal and cardiac muscle: fasting, insulin stimulation and immunoisolation studies of GLUT1 and GLUT4. Biochem J 1993;295:287-293.
    • (1993) Biochem J , vol.295 , pp. 287-293
    • Kraegen, E.W.1    Sowden, J.A.2    Halstead, M.B.3
  • 68
    • 4244212190 scopus 로고
    • Glucose transport in skeletal muscle membrane vesicles from control and exercised rats
    • King PA, Hirshman ME, Horton ES, Horton ED. Glucose transport in skeletal muscle membrane vesicles from control and exercised rats. Am J Physiol 1984;257:C1128-C1134.
    • (1984) Am J Physiol , vol.257
    • King, P.A.1    Hirshman, M.E.2    Horton, E.S.3    Horton, E.D.4
  • 69
    • 0023786062 scopus 로고
    • Acute exercise increases the number of plasma membrane glucose transporters in rat skeletal muscle
    • Hirshman ME, Wallberg-Henriksson H, Wardzala LJ, Horton ED, Horton ES. Acute exercise increases the number of plasma membrane glucose transporters in rat skeletal muscle. FEBS Lett 1988;238:235-239.
    • (1988) FEBS Lett , vol.238 , pp. 235-239
    • Hirshman, M.E.1    Wallberg-Henriksson, H.2    Wardzala, L.J.3    Horton, E.D.4    Horton, E.S.5
  • 70
    • 0027090116 scopus 로고
    • Contraction-induced translocation of the glucose transporter GLUT4 in isolated ventricular cardiomyocytes
    • Kolter T, Uphues I, Wichelhaus A, Reinauer H, Eckel J. Contraction-induced translocation of the glucose transporter GLUT4 in isolated ventricular cardiomyocytes. Biochem Biophys Res Commun 1992;189:1207-1214.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1207-1214
    • Kolter, T.1    Uphues, I.2    Wichelhaus, A.3    Reinauer, H.4    Eckel, J.5
  • 71
    • 0025807694 scopus 로고
    • 2+ to stimulate glucose transport and GLUT4 translocation in perfused rat heart
    • 2+ to stimulate glucose transport and GLUT4 translocation in perfused rat heart. Biochim Biophys Acta 1991;1094:217-223.
    • (1991) Biochim Biophys Acta , vol.1094 , pp. 217-223
    • Rattigan, S.1    Appleby, G.J.2    Clark, M.G.3
  • 72
    • 33646333955 scopus 로고
    • Experiments on the consumption of sugar in the normal and the diabetic heart
    • Knowlton FP, Starling EH. Experiments on the consumption of sugar in the normal and the diabetic heart. J Physiol 1912;45:146-163.
    • (1912) J Physiol , vol.45 , pp. 146-163
    • Knowlton, F.P.1    Starling, E.H.2
  • 73
    • 0025342464 scopus 로고
    • Divergent molecular mechanisms for insulin-resistant glucose transport in muscle and adipose cells in vivo
    • Charron MJ, Kahn BB. Divergent molecular mechanisms for insulin-resistant glucose transport in muscle and adipose cells in vivo. J Biol Chem 1990;265:7994-8000.
    • (1990) J Biol Chem , vol.265 , pp. 7994-8000
    • Charron, M.J.1    Kahn, B.B.2
  • 74
    • 0024309742 scopus 로고
    • Decreased expression of the insulin-responsive glucose transporter in diabetes and fasting
    • Berger JC, Diswas C, Vicario P, Strout HV, Saperstein R, Pilch PF. Decreased expression of the insulin-responsive glucose transporter in diabetes and fasting. Nature 1989;340:70-72.
    • (1989) Nature , vol.340 , pp. 70-72
    • Berger, J.C.1    Diswas, C.2    Vicario, P.3    Strout, H.V.4    Saperstein, R.5    Pilch, P.F.6
  • 75
    • 0024364606 scopus 로고
    • Pretranslational suppression of an insulin-responsive glucose transporter in rats with diabetes mellitus
    • Garvey TW, Huecksteadt TP, Birnbaum MJ. Pretranslational suppression of an insulin-responsive glucose transporter in rats with diabetes mellitus. Science 1989;245:60-63.
    • (1989) Science , vol.245 , pp. 60-63
    • Garvey, T.W.1    Huecksteadt, T.P.2    Birnbaum, M.J.3
  • 76
    • 0024311437 scopus 로고
    • Decrease in glucose transporter number in skeletal muscle of mildly diabetic (streptozotocin-treated) rats
    • Ramlal T, Rastogi S, Vranic M, Klip A. Decrease in glucose transporter number in skeletal muscle of mildly diabetic (streptozotocin-treated) rats. Endocrinology 1989;125:890-897.
    • (1989) Endocrinology , vol.125 , pp. 890-897
    • Ramlal, T.1    Rastogi, S.2    Vranic, M.3    Klip, A.4
  • 77
    • 0025946462 scopus 로고
    • Decreased in vivo glucose uptake but normal expression of GLUT1 and GLUT4 in skeletal muscle of diabetic rats
    • Kahn BB, Rossetti L, Lodish HF, Charron MJ. Decreased in vivo glucose uptake but normal expression of GLUT1 and GLUT4 in skeletal muscle of diabetic rats. J Clin Invest 1991;87:2197-2206.
    • (1991) J Clin Invest , vol.87 , pp. 2197-2206
    • Kahn, B.B.1    Rossetti, L.2    Lodish, H.F.3    Charron, M.J.4
  • 78
    • 0027436767 scopus 로고
    • Regulation of glucose transporter and hexokinase II expression in tissues of diabete rats
    • Burcelin R, Printz RL, Kande J, Assan R, Granner DK, Girard J. Regulation of glucose transporter and hexokinase II expression in tissues of diabete rats. Am J Physiol 1993;265:E392-E401.
    • (1993) Am J Physiol , vol.265
    • Burcelin, R.1    Printz, R.L.2    Kande, J.3    Assan, R.4    Granner, D.K.5    Girard, J.6
  • 79
    • 0026504451 scopus 로고
    • Effect of diabetes and fasting on GLUT-4 (muscle/fat) glucose-transporter expression in insulin-sensitive tissues
    • Camps M, Castello A, Munoz P, et al. Effect of diabetes and fasting on GLUT-4 (muscle/fat) glucose-transporter expression in insulin-sensitive tissues. Biochem J 1992;282:765-772.
    • (1992) Biochem J , vol.282 , pp. 765-772
    • Camps, M.1    Castello, A.2    Munoz, P.3
  • 80
    • 17344389457 scopus 로고
    • Insulin resistance is localized to skeletal but not heart muscle in type 1 diabetes
    • Nuutila P, Knuuti J, Ruotsalainen U, et al. Insulin resistance is localized to skeletal but not heart muscle in type 1 diabetes. Am J Physiol 1993;264:E756-E762.
    • (1993) Am J Physiol , vol.264
    • Nuutila, P.1    Knuuti, J.2    Ruotsalainen, U.3
  • 81
    • 0343753473 scopus 로고
    • The utilization of fat by the aglycaemic mammalian heart
    • Cruickshank EWH, Kosterlitz HW. The utilization of fat by the aglycaemic mammalian heart. J Physiol 1941;99:208-223.
    • (1941) J Physiol , vol.99 , pp. 208-223
    • Cruickshank, E.W.H.1    Kosterlitz, H.W.2
  • 83
    • 0015367773 scopus 로고
    • Myocardial glycogen changes with exercise
    • Judd WT, Poland JL. Myocardial glycogen changes with exercise. Proc Soc Exp Biol Med 1972;140:955-957.
    • (1972) Proc Soc Exp Biol Med , vol.140 , pp. 955-957
    • Judd, W.T.1    Poland, J.L.2
  • 85
    • 0028950452 scopus 로고
    • Glycogen turnover in the isolated working rat heart
    • Goodwin GW, Arteaga JR, Taegtmeyer H. Glycogen turnover in the isolated working rat heart. J Biol Chem 1995;270:9234-9240.
    • (1995) J Biol Chem , vol.270 , pp. 9234-9240
    • Goodwin, G.W.1    Arteaga, J.R.2    Taegtmeyer, H.3
  • 86
    • 0029887676 scopus 로고    scopus 로고
    • Preferential oxidation of glycogen in isolated working rat heart
    • Goodwin G, Ahmad F, Taegtmeyer H. Preferential oxidation of glycogen in isolated working rat heart. J Clin Invest 1996;97:1409-1416.
    • (1996) J Clin Invest , vol.97 , pp. 1409-1416
    • Goodwin, G.1    Ahmad, F.2    Taegtmeyer, H.3
  • 87
    • 0014178224 scopus 로고
    • Transmural gradients of glycolytic enzymes in the ventricular myocardium
    • Lundsgaard-Hansen P, Meyer C, Riedwyl H. Transmural gradients of glycolytic enzymes in the ventricular myocardium. Pflügers Arch Ges Physiol 1967;297:89-106.
    • (1967) Pflügers Arch Ges Physiol , vol.297 , pp. 89-106
    • Lundsgaard-Hansen, P.1    Meyer, C.2    Riedwyl, H.3
  • 89
    • 0027606245 scopus 로고
    • Protein phosphorylation and cellular regulation
    • Krebs EG. Protein phosphorylation and cellular regulation. Biosci Rep 1993;13:127-142.
    • (1993) Biosci Rep , vol.13 , pp. 127-142
    • Krebs, E.G.1
  • 91
    • 0019296389 scopus 로고
    • Purification and properties of the cardiac isozyme of phosphorylase kinase
    • Cooper RH, Sul HS, McCullough TE, Walsh DA. Purification and properties of the cardiac isozyme of phosphorylase kinase. J Biol Chem 1980;255:11794-11801.
    • (1980) J Biol Chem , vol.255 , pp. 11794-11801
    • Cooper, R.H.1    Sul, H.S.2    McCullough, T.E.3    Walsh, D.A.4
  • 92
    • 0021039334 scopus 로고
    • Hormonal regulation of the phosphorylation of glycogen synthase in perfused rat heart. Effects of insulin, catecholamines and glucagon
    • Ramachandran C, Angelos KL, Walsh DA. Hormonal regulation of the phosphorylation of glycogen synthase in perfused rat heart. Effects of insulin, catecholamines and glucagon. J Biol Chem 1983;258:13377-13383.
    • (1983) J Biol Chem , vol.258 , pp. 13377-13383
    • Ramachandran, C.1    Angelos, K.L.2    Walsh, D.A.3
  • 93
    • 0025202408 scopus 로고
    • Control of glycogen synthase by hierarchical protein phosphorylation
    • Roach PJ. Control of glycogen synthase by hierarchical protein phosphorylation. FASEB J 1990;4:2961-2967.
    • (1990) FASEB J , vol.4 , pp. 2961-2967
    • Roach, P.J.1
  • 94
    • 0029156784 scopus 로고
    • Phosphorylation and inactivation of rat heart glycogen synthase by cAMP-dependent and cAMP-independent protein kinases
    • Grekinis D, Reimann EM, Schlender KK. Phosphorylation and inactivation of rat heart glycogen synthase by cAMP-dependent and cAMP-independent protein kinases. Int J Biochem 1995;27:565-573.
    • (1995) Int J Biochem , vol.27 , pp. 565-573
    • Grekinis, D.1    Reimann, E.M.2    Schlender, K.K.3
  • 95
    • 0014601078 scopus 로고
    • Effects of insulin on the pattern of glucose metabolism in the perfused working and Langendorff heart of normal and insulin-deficient rats
    • Chain EB, Mansford KRL, Opie LH. Effects of insulin on the pattern of glucose metabolism in the perfused working and Langendorff heart of normal and insulin-deficient rats. Biochem J 1969;115:537-552.
    • (1969) Biochem J , vol.115 , pp. 537-552
    • Chain, E.B.1    Mansford, K.R.L.2    Opie, L.H.3
  • 96
    • 0015514917 scopus 로고
    • Effect of insulin on glycogen synthesis and synthetase activity in the perfused rat heart
    • Adolfsson S, Isaksson O, Hjalmarson A. Effect of insulin on glycogen synthesis and synthetase activity in the perfused rat heart. Biochim Biophys Acta 1972;279:146-156.
    • (1972) Biochim Biophys Acta , vol.279 , pp. 146-156
    • Adolfsson, S.1    Isaksson, O.2    Hjalmarson, A.3
  • 97
    • 0026684509 scopus 로고
    • Regulation of glycogen metabolism in canine myocardium: Effects of insulin and epinephrine in vivo
    • Laughlin MR, Taylor JF, Chesnick AS, Balaban RS. Regulation of glycogen metabolism in canine myocardium: effects of insulin and epinephrine in vivo. Am J Physiol 1992;262:E875-E883.
    • (1992) Am J Physiol , vol.262
    • Laughlin, M.R.1    Taylor, J.F.2    Chesnick, A.S.3    Balaban, R.S.4
  • 98
    • 0018144698 scopus 로고
    • A dual role for insulin in the regulation of cardiac glycogen synthase
    • Miller TB. A dual role for insulin in the regulation of cardiac glycogen synthase. J Biol Chem 1978;253:5389-5394.
    • (1978) J Biol Chem , vol.253 , pp. 5389-5394
    • Miller, T.B.1
  • 99
    • 0020841991 scopus 로고
    • Altered regulation of cardiac metabolism in sponta-neously diabetic rats
    • Miller TB. Altered regulation of cardiac metabolism in sponta-neously diabetic rats. Am J Physiol 1983;245:E379-E383.
    • (1983) Am J Physiol , vol.245
    • Miller, T.B.1
  • 100
    • 0017131580 scopus 로고
    • Insulin stimulation of glycogen synthase D phosphatase (protein phosphatase)
    • Nuttall FQ, Gannon MC, Corbett VA, Wheeler MP. Insulin stimulation of glycogen synthase D phosphatase (protein phosphatase). J Biol Chem 1976;251:6724-6729.
    • (1976) J Biol Chem , vol.251 , pp. 6724-6729
    • Nuttall, F.Q.1    Gannon, M.C.2    Corbett, V.A.3    Wheeler, M.P.4
  • 101
    • 0025015028 scopus 로고
    • Measurement of myocardial glycogen synthesis in diabetic and fasted rats
    • Laughlin MR, Petit WA, Shulman RG, Barrett EJ. Measurement of myocardial glycogen synthesis in diabetic and fasted rats. Am J Physiol 1990;258:E184-E190.
    • (1990) Am J Physiol , vol.258
    • Laughlin, M.R.1    Petit, W.A.2    Shulman, R.G.3    Barrett, E.J.4
  • 102
    • 0025979358 scopus 로고
    • Multiple defects in muscle glycogen synthase activity contribute to reduced glycogen synthesis in non-insulin dependent diabetes mellitus
    • Thorburn AW, Gumbiner B, Bulacan F, Brechtel G, Henry RR. Multiple defects in muscle glycogen synthase activity contribute to reduced glycogen synthesis in non-insulin dependent diabetes mellitus. J Clin Invest 1991;87:489-495.
    • (1991) J Clin Invest , vol.87 , pp. 489-495
    • Thorburn, A.W.1    Gumbiner, B.2    Bulacan, F.3    Brechtel, G.4    Henry, R.R.5
  • 103
    • 0029069525 scopus 로고
    • Identification of the molecular basis for phosphorylase hypersensitivity in cultured diabetic cardiomyocytes
    • Buczek-Thomas JA, Miller TB. Identification of the molecular basis for phosphorylase hypersensitivity in cultured diabetic cardiomyocytes. Mol Cell Biochem 1995;145:131-139.
    • (1995) Mol Cell Biochem , vol.145 , pp. 131-139
    • Buczek-Thomas, J.A.1    Miller, T.B.2
  • 104
    • 0014461121 scopus 로고
    • Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation
    • Linn TC, Pettit FH, Reed LJ. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation. Proc Natl Acad Sci USA 1969;62:234-241.
    • (1969) Proc Natl Acad Sci USA , vol.62 , pp. 234-241
    • Linn, T.C.1    Pettit, F.H.2    Reed, L.J.3
  • 105
    • 0002119889 scopus 로고
    • Control of pyruvate dehydrogenase in perfused rat heart by intracellular concentrations of acetyl CoA
    • Garland PB, Randle PJ. Control of pyruvate dehydrogenase in perfused rat heart by intracellular concentrations of acetyl CoA. Biochem J 1964;91:6C-7C.
    • (1964) Biochem J , vol.91
    • Garland, P.B.1    Randle, P.J.2
  • 106
    • 0016343539 scopus 로고
    • Regulation of heart muscle pyruvate dehydrogenase kinase
    • Cooper RH, Randle PJ, Denton RM. Regulation of heart muscle pyruvate dehydrogenase kinase. Biochem J 1974;143:625-641.
    • (1974) Biochem J , vol.143 , pp. 625-641
    • Cooper, R.H.1    Randle, P.J.2    Denton, R.M.3
  • 107
    • 0016285850 scopus 로고
    • Mechanism of activation of pyruvate dehydrogenase by dichloroacetate and other halogenated carboxylic acids
    • Whitehouse S, Cooper RH, Randle PJ. Mechanism of activation of pyruvate dehydrogenase by dichloroacetate and other halogenated carboxylic acids. Biochem J 1974;141:761-774.
    • (1974) Biochem J , vol.141 , pp. 761-774
    • Whitehouse, S.1    Cooper, R.H.2    Randle, P.J.3
  • 108
    • 0015347784 scopus 로고
    • Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase
    • Martin BR, Denton RM, Randle PJ. Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase. Biochem J 1972;128:161-163.
    • (1972) Biochem J , vol.128 , pp. 161-163
    • Martin, B.R.1    Denton, R.M.2    Randle, P.J.3
  • 109
    • 0027248230 scopus 로고
    • 2+ in the regulation of oxidative phosphorylation in mammalian tissues
    • 2+ in the regulation of oxidative phosphorylation in mammalian tissues. Biochem Soc Trans 1993;21:793-799.
    • (1993) Biochem Soc Trans , vol.21 , pp. 793-799
    • McCormack, J.G.1    Denton, R.M.2
  • 110
    • 0017103831 scopus 로고
    • i into pyruvate dehydrogenase phosphate in mitochondria from control and insulin-treated adipose tissue
    • i into pyruvate dehydrogenase phosphate in mitochondria from control and insulin-treated adipose tissue. Nature 1976;264:471-473.
    • (1976) Nature , vol.264 , pp. 471-473
    • Hughes, W.A.1    Denton, R.M.2
  • 111
    • 0016210982 scopus 로고
    • Calcium and magnesium ions as effectors of adipose tissue pyruvate dehydrogenase phosphate phosphatase
    • Severson DL, Denton RM, Pask HT, Randle PJ. Calcium and magnesium ions as effectors of adipose tissue pyruvate dehydrogenase phosphate phosphatase. Biochem J 1974;140:225-237.
    • (1974) Biochem J , vol.140 , pp. 225-237
    • Severson, D.L.1    Denton, R.M.2    Pask, H.T.3    Randle, P.J.4
  • 112
    • 0020565625 scopus 로고
    • Ruthenium red inhibits the activation of pyruvate dehydrogenase caused by positive inotropic agents in the perfused heart
    • McCormack GJ, England PJ. Ruthenium red inhibits the activation of pyruvate dehydrogenase caused by positive inotropic agents in the perfused heart. Biochem J 1983;214:581-585.
    • (1983) Biochem J , vol.214 , pp. 581-585
    • McCormack, G.J.1    England, P.J.2
  • 113
    • 0023653723 scopus 로고
    • Effects of calcium and magnesium on the activity of pyruvate dehydrogenase phosphate phosphatase within toluene-permeabilized mitochondria
    • Midgley PJW, Rutter GA, Thomas AP, Denton RM. Effects of calcium and magnesium on the activity of pyruvate dehydrogenase phosphate phosphatase within toluene-permeabilized mitochondria. Biochem J 1987;241:371-377.
    • (1987) Biochem J , vol.241 , pp. 371-377
    • Midgley, P.J.W.1    Rutter, G.A.2    Thomas, A.P.3    Denton, R.M.4
  • 114
    • 0026629588 scopus 로고
    • Regulation of pyruvate dehydrogenase by insulin and polyamines within electropermeabilized fat-cells and isolated mitochondria
    • Rutter GA, Diggle TA, Denton RM. Regulation of pyruvate dehydrogenase by insulin and polyamines within electropermeabilized fat-cells and isolated mitochondria. Biochem J 1992;285:435-439.
    • (1992) Biochem J , vol.285 , pp. 435-439
    • Rutter, G.A.1    Diggle, T.A.2    Denton, R.M.3
  • 115
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack GJ, Halestrap AP, Denton RM. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol Rev 1990;70:391-425.
    • (1990) Physiol Rev , vol.70 , pp. 391-425
    • McCormack, G.J.1    Halestrap, A.P.2    Denton, R.M.3
  • 116
    • 0028333838 scopus 로고
    • Role of protein synthesis and of fatty acid metabolism in the longer-term regulation of pyruvate dehydrogenase kinase
    • Priestman DA, Mistry SC, Halsall A, Randle PJ. Role of protein synthesis and of fatty acid metabolism in the longer-term regulation of pyruvate dehydrogenase kinase. Biochem J 1994;300:659-664.
    • (1994) Biochem J , vol.300 , pp. 659-664
    • Priestman, D.A.1    Mistry, S.C.2    Halsall, A.3    Randle, P.J.4
  • 117
    • 0025907030 scopus 로고
    • Long-term regulation of pyruvate dehydrogenase complex. Evidence that kinase activator protein (KAP) is free pyruvate dehydrogenase kinase
    • Jones BS, Yeaman SJ. Long-term regulation of pyruvate dehydrogenase complex. Evidence that kinase activator protein (KAP) is free pyruvate dehydrogenase kinase. Biochem J 1991;275:780-783.
    • (1991) Biochem J , vol.275 , pp. 780-783
    • Jones, B.S.1    Yeaman, S.J.2
  • 118
    • 84961033894 scopus 로고
    • Regulation of glucose uptake in muscle. I. the effects of insulin and anoxia on glucose transport and phosphorylation in the isolated perfused heart of normal rats
    • Morgan HE, Henderson MJ, Regen DM, Park CR. Regulation of glucose uptake in muscle. I. The effects of insulin and anoxia on glucose transport and phosphorylation in the isolated perfused heart of normal rats. J Biol Chem 1961;236:253-261.
    • (1961) J Biol Chem , vol.236 , pp. 253-261
    • Morgan, H.E.1    Henderson, M.J.2    Regen, D.M.3    Park, C.R.4
  • 120
    • 0029003144 scopus 로고
    • Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: Insights into autoregulation of a bifunctional enzyme
    • Kurland IJ, Pilkis SJ. Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: insights into autoregulation of a bifunctional enzyme. Protein Sci 1995;4:1023-1037.
    • (1995) Protein Sci , vol.4 , pp. 1023-1037
    • Kurland, I.J.1    Pilkis, S.J.2
  • 121
    • 0023258411 scopus 로고
    • Effects of insulin and work on fructose 2,6-bisphosphate content and phosphofructokinase activity in perfused rat hearts
    • Lawson JWR, Uyeda K. Effects of insulin and work on fructose 2,6-bisphosphate content and phosphofructokinase activity in perfused rat hearts. J Biol Chem 1987;262:3165-3173.
    • (1987) J Biol Chem , vol.262 , pp. 3165-3173
    • Lawson, J.W.R.1    Uyeda, K.2
  • 122
    • 0022343820 scopus 로고
    • Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase
    • Rider MH, Foret D, Hue L. Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Biochem J 1985;231:193-196.
    • (1985) Biochem J , vol.231 , pp. 193-196
    • Rider, M.H.1    Foret, D.2    Hue, L.3
  • 123
    • 0025914685 scopus 로고
    • Hepatic gluconeogenesis/glycolysis: Regulation and structure/function relationships of substrate cycle enzymes
    • Pilkis SJ, Claus TH. Hepatic gluconeogenesis/glycolysis: regulation and structure/function relationships of substrate cycle enzymes. Annu Rev Nutr 1991;11:465-515.
    • (1991) Annu Rev Nutr , vol.11 , pp. 465-515
    • Pilkis, S.J.1    Claus, T.H.2
  • 124
    • 0014787834 scopus 로고
    • Control of the tricarboxylate cycle and its interactions with glycolysis during acetate utilization in the heart
    • Randle PJ, England PJ, Denton RM. Control of the tricarboxylate cycle and its interactions with glycolysis during acetate utilization in the heart. Biochem J 1970;117:677-695.
    • (1970) Biochem J , vol.117 , pp. 677-695
    • Randle, P.J.1    England, P.J.2    Denton, R.M.3
  • 125
    • 33646277118 scopus 로고
    • The effect of adrenal cortex and anterior pituitary extracts and insulin on the hexokinase reaction
    • Colowick SP, Cori GT, Slein MW. The effect of adrenal cortex and anterior pituitary extracts and insulin on the hexokinase reaction. J Biol Chem 1947;168:583-596.
    • (1947) J Biol Chem , vol.168 , pp. 583-596
    • Colowick, S.P.1    Cori, G.T.2    Slein, M.W.3
  • 126
    • 0021365310 scopus 로고
    • Regulation of alternative pathways of glucose metabolism in rat heart by alloxan diabetes: Changes in pentose phosphate pathway
    • Sochor M, Gonzalez A-M, McLean P. Regulation of alternative pathways of glucose metabolism in rat heart by alloxan diabetes: changes in pentose phosphate pathway. Biochem Biophys Res Commun 1984;118:110-116.
    • (1984) Biochem Biophys Res Commun , vol.118 , pp. 110-116
    • Sochor, M.1    Gonzalez, A.-M.2    McLean, P.3
  • 127
    • 0027529195 scopus 로고
    • Hexokinase II mRNA and gene structure, regulation by insulin and evolution
    • Printz RL, Koch S, Potter LR, et al. Hexokinase II mRNA and gene structure, regulation by insulin and evolution. J Biol Chem 1993;268:5209-5219.
    • (1993) J Biol Chem , vol.268 , pp. 5209-5219
    • Printz, R.L.1    Koch, S.2    Potter, L.R.3
  • 128
    • 0014094890 scopus 로고
    • Utilization of endogenous lipid by the isolated perfused rat heart
    • Olson RE, Hoeschen RJ. Utilization of endogenous lipid by the isolated perfused rat heart. Biochem J 1967;108:796-801.
    • (1967) Biochem J , vol.108 , pp. 796-801
    • Olson, R.E.1    Hoeschen, R.J.2
  • 129
    • 0013768542 scopus 로고
    • Pyruvate metabolism in the perfused rat heart
    • Evans JR, Opie LH, Renold AE. Pyruvate metabolism in the perfused rat heart. Am J Physiol 1963;205:971-976.
    • (1963) Am J Physiol , vol.205 , pp. 971-976
    • Evans, J.R.1    Opie, L.H.2    Renold, A.E.3
  • 130
    • 0025821485 scopus 로고
    • Myocardial triacylglycerol turnover and contribution to energy substrate utilization in isolated working rat hearts
    • Saddik M, Lopaschuk GD. Myocardial triacylglycerol turnover and contribution to energy substrate utilization in isolated working rat hearts. J Biol Chem 1991;266:8162-8170.
    • (1991) J Biol Chem , vol.266 , pp. 8162-8170
    • Saddik, M.1    Lopaschuk, G.D.2
  • 131
    • 0023126669 scopus 로고
    • Lipoprotein lipase in diabetes
    • Taskinen M-R. Lipoprotein lipase in diabetes. Diabetes Metab Rev 1987;3:551-570.
    • (1987) Diabetes Metab Rev , vol.3 , pp. 551-570
    • Taskinen, M.-R.1
  • 132
    • 0029075830 scopus 로고
    • Triglyceride lipases and atherosclerosis
    • Olivecrona G, Olivecrona T. Triglyceride lipases and atherosclerosis. Curr Opin Lipidol 1995;6:291-305.
    • (1995) Curr Opin Lipidol , vol.6 , pp. 291-305
    • Olivecrona, G.1    Olivecrona, T.2
  • 133
    • 0021066374 scopus 로고
    • Insulin-mediated modification of myocardial lipoprotein lipase and lipoprotein metabolism
    • O'Looney P, Vander Maten M, Vahouny GV. Insulin-mediated modification of myocardial lipoprotein lipase and lipoprotein metabolism. J Biol Chem 1983;258:12994-13001.
    • (1983) J Biol Chem , vol.258 , pp. 12994-13001
    • O'Looney, P.1    Vander Maten, M.2    Vahouny, G.V.3
  • 134
    • 0021955140 scopus 로고
    • Lipoprotein composition as a component in the lipoprotein clearance defect in experimental diabetes
    • O'Looney P, Irwin D, Briscoe P, Vahouny GV. Lipoprotein composition as a component in the lipoprotein clearance defect in experimental diabetes. J Biol Chem 1985;260:428-432.
    • (1985) J Biol Chem , vol.260 , pp. 428-432
    • O'Looney, P.1    Irwin, D.2    Briscoe, P.3    Vahouny, G.V.4
  • 135
    • 0025893906 scopus 로고
    • Diabetes reduces the heparin- And phospholipase C-releasable lipoprotein lipase from cardiomyocytes
    • Braun JEA, Severson DL. Diabetes reduces the heparin- and phospholipase C-releasable lipoprotein lipase from cardiomyocytes. Am J Physiol 1991;260:E477-E485.
    • (1991) Am J Physiol , vol.260
    • Braun, J.E.A.1    Severson, D.L.2
  • 136
    • 0029123465 scopus 로고
    • Post-transcriptional mechanisms are responsible for the reduction in lipoprotein lipase activity in cardiomyocytes from diabetic rat hearts
    • Carroll R, Liu L, Severson DL. Post-transcriptional mechanisms are responsible for the reduction in lipoprotein lipase activity in cardiomyocytes from diabetic rat hearts. Biochem J 1995;310:67-72.
    • (1995) Biochem J , vol.310 , pp. 67-72
    • Carroll, R.1    Liu, L.2    Severson, D.L.3
  • 137
    • 0342882694 scopus 로고
    • The effects of insulin, adrenaline and nutrients on the oxygen uptake of the perfused rat heart
    • Fisher RB, Williamson JR. The effects of insulin, adrenaline and nutrients on the oxygen uptake of the perfused rat heart. J Physiol 1961;158:102-112.
    • (1961) J Physiol , vol.158 , pp. 102-112
    • Fisher, R.B.1    Williamson, J.R.2
  • 138
    • 37049050772 scopus 로고
    • Hormonal control of lipid concentration in rat heart and gastrocnemius
    • Denton RM, Randle PJ. Hormonal control of lipid concentration in rat heart and gastrocnemius. Nature 1965;208:488.
    • (1965) Nature , vol.208 , pp. 488
    • Denton, R.M.1    Randle, P.J.2
  • 139
    • 0013773447 scopus 로고
    • Regulation of glucose uptake by muscle. 10. Effects of alloxan-diabetes, starvation, hypophysectomy and adrenalectomy, and of fatty acids, ketone bodies and pyruvate on the glycerol output and concentrations of free fatty acids, long-chain fatty acyl-CoA, glycerol phosphate and citrate-cycle intermediates in rat heart and diaphragm muscles
    • Garland PB, Randle PJ. Regulation of glucose uptake by muscle. 10. Effects of alloxan-diabetes, starvation, hypophysectomy and adrenalectomy, and of fatty acids, ketone bodies and pyruvate on the glycerol output and concentrations of free fatty acids, long-chain fatty acyl-CoA, glycerol phosphate and citrate-cycle intermediates in rat heart and diaphragm muscles. Biochem J 1964;93:678-687.
    • (1964) Biochem J , vol.93 , pp. 678-687
    • Garland, P.B.1    Randle, P.J.2
  • 140
    • 0028589356 scopus 로고
    • Triacylglycerol turnover in isolated working hearts of acutely diabetic rats
    • Saddik M, Lopaschuk GD. Triacylglycerol turnover in isolated working hearts of acutely diabetic rats. Can J Physiol Pharmacol 1994;72:1110-1119.
    • (1994) Can J Physiol Pharmacol , vol.72 , pp. 1110-1119
    • Saddik, M.1    Lopaschuk, G.D.2
  • 141
    • 0013882021 scopus 로고
    • Effect of epinephrine on myocardial triglyceride and free fatty acid utilization
    • Kreisberg RA. Effect of epinephrine on myocardial triglyceride and free fatty acid utilization. Am J Physiol 1966;210:385-389.
    • (1966) Am J Physiol , vol.210 , pp. 385-389
    • Kreisberg, R.A.1
  • 142
    • 0017730050 scopus 로고
    • The effect of adrenaline-induced endogenous lipolysis upon the mechanical and metabolic performance of ischaemically-perfused rat hearts
    • Brownsey RW, Brunt RV. The effect of adrenaline-induced endogenous lipolysis upon the mechanical and metabolic performance of ischaemically-perfused rat hearts. Clin Sci Mol Med 1977;53:513-521.
    • (1977) Clin Sci Mol Med , vol.53 , pp. 513-521
    • Brownsey, R.W.1    Brunt, R.V.2
  • 143
    • 0016611507 scopus 로고
    • Effects of catecholamines on myocardial endogenous substrates and contractility
    • Crass MF, Shipp JC, Pieper GM. Effects of catecholamines on myocardial endogenous substrates and contractility. Am J Physiol 1975;228:618-627.
    • (1975) Am J Physiol , vol.228 , pp. 618-627
    • Crass, M.F.1    Shipp, J.C.2    Pieper, G.M.3
  • 144
    • 0024600820 scopus 로고
    • The presence and role of hormone-sensitive lipase in heart muscle
    • Small CA, Garton AJ, Yeaman SJ. The presence and role of hormone-sensitive lipase in heart muscle. Biochem J 1989;258:67-72.
    • (1989) Biochem J , vol.258 , pp. 67-72
    • Small, C.A.1    Garton, A.J.2    Yeaman, S.J.3
  • 145
    • 0018680204 scopus 로고
    • Regulation of lipid metabolism in adipose tissue and heart
    • Severson DL. Regulation of lipid metabolism in adipose tissue and heart. Can J Physiol Pharmacol 1979;57:923-937.
    • (1979) Can J Physiol Pharmacol , vol.57 , pp. 923-937
    • Severson, D.L.1
  • 146
    • 0011682519 scopus 로고
    • Hormonal regulation of hormone-sensitive lipase in intact adipocytes: Identification of phosphorylated sites and effects on the phosphorylation by lipolytic hormones and insulin
    • Stralfors P, Bjorgell P, Belfrage P. Hormonal regulation of hormone-sensitive lipase in intact adipocytes: identification of phosphorylated sites and effects on the phosphorylation by lipolytic hormones and insulin. Proc Natl Acad Sci USA 1984;81:3317-3321.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3317-3321
    • Stralfors, P.1    Bjorgell, P.2    Belfrage, P.3
  • 147
    • 0015497067 scopus 로고
    • Exogenous substrate effects on endogenous lipid metabolism in the working rat heart
    • Crass MF. Exogenous substrate effects on endogenous lipid metabolism in the working rat heart. Biochim Biophys Acta 1972;280:71-81.
    • (1972) Biochim Biophys Acta , vol.280 , pp. 71-81
    • Crass, M.F.1
  • 148
    • 0014116416 scopus 로고
    • Concentrations of glycerides and phospholipids in rat heart and gastrocnemius muscles. Effects of alloxan-diabetes and perfusion
    • Denton RM, Randle PJ. Concentrations of glycerides and phospholipids in rat heart and gastrocnemius muscles. Effects of alloxan-diabetes and perfusion. Biochem J 1967;104:416-422.
    • (1967) Biochem J , vol.104 , pp. 416-422
    • Denton, R.M.1    Randle, P.J.2
  • 149
    • 0017738601 scopus 로고
    • A possible role for malonyl-CoA in the regulation of hepatic fatty acid oxidation and ketogenesis
    • McGarry JD, Mannaerts GP, Foster DW. A possible role for malonyl-CoA in the regulation of hepatic fatty acid oxidation and ketogenesis. J Clin Invest 1977;60:265-270.
    • (1977) J Clin Invest , vol.60 , pp. 265-270
    • McGarry, J.D.1    Mannaerts, G.P.2    Foster, D.W.3
  • 150
    • 0028091713 scopus 로고
    • Use of a selective inhibitor of liver carnitine palmitoyltransferase I (CPT I) allows quantification of its contribution to total CPT I activity in rat heart
    • Weis BC, Cowan AT, Brown N, Foster DW, McGarry JD. Use of a selective inhibitor of liver carnitine palmitoyltransferase I (CPT I) allows quantification of its contribution to total CPT I activity in rat heart. J Biol Chem 1994;269:26443-26448.
    • (1994) J Biol Chem , vol.269 , pp. 26443-26448
    • Weis, B.C.1    Cowan, A.T.2    Brown, N.3    Foster, D.W.4    McGarry, J.D.5
  • 151
    • 0020624753 scopus 로고
    • Observations on the affinity of carnitine, and malonyl-CoA sensitivity of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the rat
    • McGarry JD, Mills SE, Long CS, Foster DW. Observations on the affinity of carnitine, and malonyl-CoA sensitivity of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the rat. Biochem J 1983;214:21-28.
    • (1983) Biochem J , vol.214 , pp. 21-28
    • McGarry, J.D.1    Mills, S.E.2    Long, C.S.3    Foster, D.W.4
  • 152
    • 0021193646 scopus 로고
    • i values
    • i values. J Biol Chem 1984;259:12030-12033.
    • (1984) J Biol Chem , vol.259 , pp. 12030-12033
    • Cook, G.A.1
  • 154
    • 0028908129 scopus 로고
    • Insulin-associated changes in carnitine palmitoyltransferase in cultured neonatal rat cardiac myocytes
    • Hudson EK, Liu M-H, Buja LM, McMillin JB. Insulin-associated changes in carnitine palmitoyltransferase in cultured neonatal rat cardiac myocytes. J Mol Cell Cardiol 1995;27:599-613.
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 599-613
    • Hudson, E.K.1    Liu, M.-H.2    Buja, L.M.3    McMillin, J.B.4
  • 156
    • 0024459546 scopus 로고
    • Formation of malonyl-CoA in rat heart
    • Thampy KG. Formation of malonyl-CoA in rat heart. J Biol Chem 1989;264:17631-17634.
    • (1989) J Biol Chem , vol.264 , pp. 17631-17634
    • Thampy, K.G.1
  • 158
    • 0027453493 scopus 로고
    • Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart
    • Saddik M, Gamble J, Witters LA, Lopaschuk GD. Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart. J Biol Chem 1993;268:25836-25845.
    • (1993) J Biol Chem , vol.268 , pp. 25836-25845
    • Saddik, M.1    Gamble, J.2    Witters, L.A.3    Lopaschuk, G.D.4
  • 159
    • 0028303911 scopus 로고
    • Unique structural features and differential phosphorylation of the 280-kDa component (isozyme) of rat liver acetyl-CoA carboxylase
    • Winz R, Hess D, Aebersold R, Brownsey RW. Unique structural features and differential phosphorylation of the 280-kDa component (isozyme) of rat liver acetyl-CoA carboxylase. J Biol Chem 1994;269:14438-14445.
    • (1994) J Biol Chem , vol.269 , pp. 14438-14445
    • Winz, R.1    Hess, D.2    Aebersold, R.3    Brownsey, R.W.4
  • 160
    • 0028522881 scopus 로고
    • Acetyl-CoA carboxylase: An important regulator of fatty acid oxidation in the heart
    • Lopaschuk GD, Gamble J. Acetyl-CoA carboxylase: an important regulator of fatty acid oxidation in the heart. Can J Physiol Pharmacol 1994;72:1101-1109.
    • (1994) Can J Physiol Pharmacol , vol.72 , pp. 1101-1109
    • Lopaschuk, G.D.1    Gamble, J.2
  • 161
    • 0024795323 scopus 로고
    • Regulation of fatty acid synthesis via phosphorylation of acetyl-CoA carboxylase
    • Hardie DG. Regulation of fatty acid synthesis via phosphorylation of acetyl-CoA carboxylase. Prog Lipid Res 1989;28:117-146.
    • (1989) Prog Lipid Res , vol.28 , pp. 117-146
    • Hardie, D.G.1
  • 162
    • 0024460580 scopus 로고
    • Role of reversible phosphorylation of acetyl-CoA carboxylase in long-chain fatty acid synthesis
    • Kim K-H, Lopez-Casillas F, Bai DH, Luo X, Pape ME. Role of reversible phosphorylation of acetyl-CoA carboxylase in long-chain fatty acid synthesis. FASEB J 1989;3:2250-2256.
    • (1989) FASEB J , vol.3 , pp. 2250-2256
    • Kim, K.-H.1    Lopez-Casillas, F.2    Bai, D.H.3    Luo, X.4    Pape, M.E.5
  • 163
    • 0018680040 scopus 로고
    • Adrenaline and the regulation of acetyl-CoA carboxylase in rat epididymal adipose tissue: Inactivation of the enzyme is associated with phosphorylation and can be reversed upon dephosphorylation
    • Brownsey RW, Hughes WA, Denton RM. Adrenaline and the regulation of acetyl-CoA carboxylase in rat epididymal adipose tissue: inactivation of the enzyme is associated with phosphorylation and can be reversed upon dephosphorylation. Biochem J 1979;184:23-32.
    • (1979) Biochem J , vol.184 , pp. 23-32
    • Brownsey, R.W.1    Hughes, W.A.2    Denton, R.M.3
  • 164
    • 0018696224 scopus 로고
    • Regulation of hepatic acetyl-CoA carboxylase by insulin and glucagon
    • Witters LA, Moriarty D, Martin DB. Regulation of hepatic acetyl-CoA carboxylase by insulin and glucagon. J Biol Chem 1979;254:6644-6649.
    • (1979) J Biol Chem , vol.254 , pp. 6644-6649
    • Witters, L.A.1    Moriarty, D.2    Martin, D.B.3
  • 165
    • 0029093341 scopus 로고
    • High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase
    • Kudo N, Barr AJ, Barr RL, Desai S, Lopaschuk GD. High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase. J Biol Chem 1995;270:17513-17520.
    • (1995) J Biol Chem , vol.270 , pp. 17513-17520
    • Kudo, N.1    Barr, A.J.2    Barr, R.L.3    Desai, S.4    Lopaschuk, G.D.5
  • 166
    • 0027486343 scopus 로고
    • Malonyl-CoA metabolism in cardiac myocytes and its relevance to the control of fatty acid oxidation
    • Anwan MM, Saggerson DE. Malonyl-CoA metabolism in cardiac myocytes and its relevance to the control of fatty acid oxidation. Biochem J 1993;295:61-65.
    • (1993) Biochem J , vol.295 , pp. 61-65
    • Anwan, M.M.1    Saggerson, D.E.2
  • 168
    • 0018132822 scopus 로고
    • Purification and properties of malonyl-CoA decarboxylase from rat liver mitochondria and its immunological comparison with the enzymes from rat brain, heart and mammary gland
    • Kim YS, Kolattukudy PE. Purification and properties of malonyl-CoA decarboxylase from rat liver mitochondria and its immunological comparison with the enzymes from rat brain, heart and mammary gland. Arch Biochem Biophys 1978;190:234-246.
    • (1978) Arch Biochem Biophys , vol.190 , pp. 234-246
    • Kim, Y.S.1    Kolattukudy, P.E.2
  • 169
    • 33646294161 scopus 로고    scopus 로고
    • Malonyl CoA degradation in the reperfused heart
    • Abstract
    • Barrn RL, Kozak R, Lopaschuk GD. Malonyl CoA degradation in the reperfused heart. Circulation 1996;44:I-12. (Abstract).
    • (1996) Circulation , vol.44
    • Barrn, R.L.1    Kozak, R.2    Lopaschuk, G.D.3
  • 170
    • 0027170056 scopus 로고
    • Mutational analysis of insulin receptor function. Consensus and controversy
    • Tavare JM, Siddle K. Mutational analysis of insulin receptor function. Consensus and controversy. Biochim Biophys Acta 1993;1178:21-39.
    • (1993) Biochim Biophys Acta , vol.1178 , pp. 21-39
    • Tavare, J.M.1    Siddle, K.2
  • 171
    • 0021985413 scopus 로고
    • Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
    • Ullrich A, Bell JR, Chen EY, et al. Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 1985;313:756-761.
    • (1985) Nature , vol.313 , pp. 756-761
    • Ullrich, A.1    Bell, J.R.2    Chen, E.Y.3
  • 172
    • 0021924895 scopus 로고
    • The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling
    • Ebina Y, Ellis L, Jarnagin K, et al. The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell 1985;40:747-758.
    • (1985) Cell , vol.40 , pp. 747-758
    • Ebina, Y.1    Ellis, L.2    Jarnagin, K.3
  • 173
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling
    • De Meyts P. The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling. Diabetologia 1994;37:S135-S148.
    • (1994) Diabetologia , vol.37
    • De Meyts, P.1
  • 174
    • 0026642585 scopus 로고
    • Identification of determinants that confer ligand specificity on the insulin receptor
    • Andersen AS, Kjeldsen T, Wiberg FC, et al. Identification of determinants that confer ligand specificity on the insulin receptor. J Biol Chem 1992;267:13681-13686.
    • (1992) J Biol Chem , vol.267 , pp. 13681-13686
    • Andersen, A.S.1    Kjeldsen, T.2    Wiberg, F.C.3
  • 175
    • 13344279398 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of a C-terminal ligand binding domain of the insulin receptor alpha-subunits
    • Mynarcik DC, Yu GQ, Whittaker J. Alanine-scanning mutagenesis of a C-terminal ligand binding domain of the insulin receptor alpha-subunits. J Biol Chem 1996;271:2439-2442.
    • (1996) J Biol Chem , vol.271 , pp. 2439-2442
    • Mynarcik, D.C.1    Yu, G.Q.2    Whittaker, J.3
  • 176
    • 0025362295 scopus 로고
    • Functionally distinct insulin receptors generated by tissue-specific alternative splicing
    • Mosthaf L, Gralko K, Dull TJ, Coussens L, Ullrich A, McClain DA. Functionally distinct insulin receptors generated by tissue-specific alternative splicing. EMBO J 1990;9:2409-2413.
    • (1990) EMBO J , vol.9 , pp. 2409-2413
    • Mosthaf, L.1    Gralko, K.2    Dull, T.J.3    Coussens, L.4    Ullrich, A.5    McClain, D.A.6
  • 177
    • 0025801714 scopus 로고
    • Altered expression of insulin receptor types a and B in the skeletal muscle of non-insulin-dependent diabetes mellitus patients
    • Mosthaf L, Vogt B, Haring H-U, Ullrich A. Altered expression of insulin receptor types A and B in the skeletal muscle of non-insulin-dependent diabetes mellitus patients. Proc Natl Acad Sci USA 1991;88:4728-4730.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4728-4730
    • Mosthaf, L.1    Vogt, B.2    Haring, H.-U.3    Ullrich, A.4
  • 178
    • 0029095525 scopus 로고
    • The B isoform of the insulin receptor signals more efficiently, than the a isoform in HepG2 cells
    • Kosaki A, Pillay TS, Xu L, Webster NJG. The B isoform of the insulin receptor signals more efficiently, than the A isoform in HepG2 cells. J Biol Chem 1995;270:20816-20823.
    • (1995) J Biol Chem , vol.270 , pp. 20816-20823
    • Kosaki, A.1    Pillay, T.S.2    Xu, L.3    Webster, N.J.G.4
  • 179
    • 0021907605 scopus 로고
    • Receptor-mediated transport of insulin across endothelial cells
    • King GL, Johnson SM. Receptor-mediated transport of insulin across endothelial cells. Science 1985;227:1583-1586.
    • (1985) Science , vol.227 , pp. 1583-1586
    • King, G.L.1    Johnson, S.M.2
  • 180
    • 84914498808 scopus 로고
    • The action of insulin in the isolated rat heart
    • Bleehen NM, Fisher RB. The action of insulin in the isolated rat heart. J Physiol 1954;123:260-276.
    • (1954) J Physiol , vol.123 , pp. 260-276
    • Bleehen, N.M.1    Fisher, R.B.2
  • 181
    • 0015240302 scopus 로고
    • The relationship between the insulin-binding capacity of fat cells and the cellular response to insulin: Studies with intact and trypsin-treated fat cells
    • Kono T, Barham FW. The relationship between the insulin-binding capacity of fat cells and the cellular response to insulin: studies with intact and trypsin-treated fat cells. J Biol Chem 1971;246:6210-6216.
    • (1971) J Biol Chem , vol.246 , pp. 6210-6216
    • Kono, T.1    Barham, F.W.2
  • 182
    • 0026656320 scopus 로고
    • Lilly Lecture: Molecular mechanisms of insulin resistance. Lessons from patients with mutations in the insulin-receptor gene
    • Taylor SI. Lilly Lecture: Molecular mechanisms of insulin resistance. Lessons from patients with mutations in the insulin-receptor gene. Diabetes 1992;41:1473-1490.
    • (1992) Diabetes , vol.41 , pp. 1473-1490
    • Taylor, S.I.1
  • 183
    • 0026742983 scopus 로고
    • Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function
    • Wilden PA, Kahn CR, Siddle K, Whit F. Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function. J Biol Chem 1992;267:16660-16668.
    • (1992) J Biol Chem , vol.267 , pp. 16660-16668
    • Wilden, P.A.1    Kahn, C.R.2    Siddle, K.3    Whit, F.4
  • 184
  • 185
    • 0028957904 scopus 로고
    • Expression, characterization, and crystallization of the catalytic core of the human insulin receptor protein-tyrosine kinase domain
    • Wei L, Hubbard SR, Hendrickson WA, Ellis L. Expression, characterization, and crystallization of the catalytic core of the human insulin receptor protein-tyrosine kinase domain. J Biol Chem 1995;270:8122-8130.
    • (1995) J Biol Chem , vol.270 , pp. 8122-8130
    • Wei, L.1    Hubbard, S.R.2    Hendrickson, W.A.3    Ellis, L.4
  • 188
    • 0027143218 scopus 로고
    • Nek associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
    • Lee C-H, Li W, Nishimura R, et al. Nek associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells. Proc Natl Acad Sci USA 1993;90:11713-11717.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11713-11717
    • Lee, C.-H.1    Li, W.2    Nishimura, R.3
  • 189
    • 0027158159 scopus 로고
    • The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhn MR, Pawson T, Lienhard GE, Feng G-S. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J Biol Chem 1993;268:11479-11481.
    • (1993) J Biol Chem , vol.268 , pp. 11479-11481
    • Kuhn, M.R.1    Pawson, T.2    Lienhard, G.E.3    Feng, G.-S.4
  • 190
    • 0027091611 scopus 로고
    • Insulin-dependent formation of a complex containing an 85-kDa subunit of phosphatidylinositol 3-kinase and tyrosine-phosphorylated insulin receptor substrate 1
    • Yonezawa K, Ueda H, Hara K, et al. Insulin-dependent formation of a complex containing an 85-kDa subunit of phosphatidylinositol 3-kinase and tyrosine-phosphorylated insulin receptor substrate 1. J Biol Chem 1992;267:25958-25966.
    • (1992) J Biol Chem , vol.267 , pp. 25958-25966
    • Yonezawa, K.1    Ueda, H.2    Hara, K.3
  • 191
    • 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 1994;372:182-186.
    • (1994) Nature , vol.372 , pp. 182-186
    • Tamemoto, H.1    Kadowaki, T.2    Tobe, K.3
  • 192
    • 0028785265 scopus 로고
    • Cloning of a cDNA encoding a 190-kDa insulin receptor substrate-1-like protein of simian COS cells
    • Wang LH, Hayashi H, Mitani Y, et al. Cloning of a cDNA encoding a 190-kDa insulin receptor substrate-1-like protein of simian COS cells. Biochem Biophys Res Commun 1995;216:321-328.
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 321-328
    • Wang, L.H.1    Hayashi, H.2    Mitani, Y.3
  • 193
    • 0029148591 scopus 로고
    • Role of IRS-2 in insulin and cytokine signalling
    • Sun XJ, Wang LM, Zhang Y, et al. Role of IRS-2 in insulin and cytokine signalling. Nature 1995;377:173-177.
    • (1995) Nature , vol.377 , pp. 173-177
    • Sun, X.J.1    Wang, L.M.2    Zhang, Y.3
  • 194
    • 0027292532 scopus 로고
    • Identification of SHC as a substrate of the insulin receptor kinase distinct from the GAP-associated 62 kDa tyrosine phosphoprotein
    • Kovacina KS, Roth RA. Identification of SHC as a substrate of the insulin receptor kinase distinct from the GAP-associated 62 kDa tyrosine phosphoprotein. Biochem Biophys Res Commun 1993;192:1303-1311.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 1303-1311
    • Kovacina, K.S.1    Roth, R.A.2
  • 195
    • 0029130717 scopus 로고
    • She isoform-specific tyrosine phosphorylation by the insulin and epidermal growth factor receptors
    • Okada S, Yamauchi K, Pessin JE. She isoform-specific tyrosine phosphorylation by the insulin and epidermal growth factor receptors. J Biol Chem 1995;270:20737-20741.
    • (1995) J Biol Chem , vol.270 , pp. 20737-20741
    • Okada, S.1    Yamauchi, K.2    Pessin, J.E.3
  • 196
    • 0029882789 scopus 로고    scopus 로고
    • Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
    • Hansen H, Svensson U, Zhu JW, et al. Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus. J Biol Chem 1996;271:8882-8886.
    • (1996) J Biol Chem , vol.271 , pp. 8882-8886
    • Hansen, H.1    Svensson, U.2    Zhu, J.W.3
  • 199
    • 0028036795 scopus 로고
    • Localization of the insulin receptor binding sites for the SH2 domain proteins p85, Syp, and GAP
    • Staubs PA, Reichart DR, Saltiel AR, et al. Localization of the insulin receptor binding sites for the SH2 domain proteins p85, Syp, and GAP. J Biol Chem 1994;269:27186-27192.
    • (1994) J Biol Chem , vol.269 , pp. 27186-27192
    • Staubs, P.A.1    Reichart, D.R.2    Saltiel, A.R.3
  • 200
    • 0028124189 scopus 로고
    • Essential role of phosphatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes. Studies with a selective inhibitor wortmannin
    • Okada T, Kawano Y, Sakakibara T, Hazeki O, Ui M. Essential role of phosphatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes. Studies with a selective inhibitor wortmannin. J Biol Chem 1994;269:3568-3573.
    • (1994) J Biol Chem , vol.269 , pp. 3568-3573
    • Okada, T.1    Kawano, Y.2    Sakakibara, T.3    Hazeki, O.4    Ui, M.5
  • 201
    • 0028986738 scopus 로고
    • Normal activation of p70 S6 kinase by insulin in cells overexpressing dominant negative 85kD subunit of phosphoinositide 3-kinase
    • Hara K, Yonezawa K, Sakaue H, et al. Normal activation of p70 S6 kinase by insulin in cells overexpressing dominant negative 85kD subunit of phosphoinositide 3-kinase. Biochem Biophys Res Commun 1995;208:735-741.
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 735-741
    • Hara, K.1    Yonezawa, K.2    Sakaue, H.3
  • 202
    • 0028829053 scopus 로고
    • Multiple signalling pathways involved in the stimulation of fatty acid and glycogen synthesis by insulin in rat epididymal fat cells
    • Moule SK, Edgell NJ, Welsh GI, et al. Multiple signalling pathways involved in the stimulation of fatty acid and glycogen synthesis by insulin in rat epididymal fat cells. Biochem J 1995;311:595-601.
    • (1995) Biochem J , vol.311 , pp. 595-601
    • Moule, S.K.1    Edgell, N.J.2    Welsh, G.I.3
  • 203
    • 0027535742 scopus 로고
    • Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi H, Brewer KA, Exton JH. Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 1993;268:13-16.
    • (1993) J Biol Chem , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 204
    • 0029143388 scopus 로고
    • Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase
    • Kohn AD, Kovacina KS, Roth RA. Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase. EMBO J 1995;14:4288-4295.
    • (1995) EMBO J , vol.14 , pp. 4288-4295
    • Kohn, A.D.1    Kovacina, K.S.2    Roth, R.A.3
  • 205
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross DAE, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 1995;378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 206
    • 0029810181 scopus 로고    scopus 로고
    • Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation
    • Kohn AD, Takeuchi F, Roth RA. Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. J Biol Chem 1996;271:21920-21926.
    • (1996) J Biol Chem , vol.271 , pp. 21920-21926
    • Kohn, A.D.1    Takeuchi, F.2    Roth, R.A.3
  • 208
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active akt ser/thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and GLUT4 translocation
    • in press
    • Kohn, A.D., Summers, S.A., Birnbaum, M.J., Roth, R.A. Expression of a constitutively active akt ser/thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and GLUT4 translocation. J. Biol. Chem. 1996 (in press).
    • (1996) J. Biol. Chem.
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 209
    • 0028341446 scopus 로고
    • She is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation
    • Sasaoka T, Draznin B, Leitner JW, Langlois WJ, Olefsky JM. She is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation. J Biol Chem 1994;269:10734-10738.
    • (1994) J Biol Chem , vol.269 , pp. 10734-10738
    • Sasaoka, T.1    Draznin, B.2    Leitner, J.W.3    Langlois, W.J.4    Olefsky, J.M.5
  • 210
    • 0027466903 scopus 로고
    • Insulin-induced phosphorylation of the 46- And 52-kDa She proteins
    • Pronk GJ, McGlade J, Pelicci G, Pawson T, Bos JL. Insulin-induced phosphorylation of the 46- and 52-kDa She proteins. J Biol Chem 1993;268:5748-5753.
    • (1993) J Biol Chem , vol.268 , pp. 5748-5753
    • Pronk, G.J.1    McGlade, J.2    Pelicci, G.3    Pawson, T.4    Bos, J.L.5
  • 211
    • 0027304731 scopus 로고
    • Human Sos1A guanine nucleotide exchange factor for Ras that binds to GRB2
    • Chardin P, Camonis JH, Gale NW, et al. Human Sos1A guanine nucleotide exchange factor for Ras that binds to GRB2. Science 1993;260:1338-1343.
    • (1993) Science , vol.260 , pp. 1338-1343
    • Chardin, P.1    Camonis, J.H.2    Gale, N.W.3
  • 212
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis RJ. The mitogen-activated protein kinase signal transduction pathway. J Biol Chem 1993;268:14553-14556.
    • (1993) J Biol Chem , vol.268 , pp. 14553-14556
    • Davis, R.J.1
  • 213
    • 0029011218 scopus 로고
    • The MAP kinase signaling cascade
    • Seger R, Krebs EG. The MAP kinase signaling cascade. FASEB J 1995;9:726-735.
    • (1995) FASEB J , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 214
    • 0005261734 scopus 로고
    • Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein-2 in vitro
    • Ray LB, Sturgill TW. Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein-2 in vitro. Proc Natl Acad Sci USA 1987;84:1502-1506.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1502-1506
    • Ray, L.B.1    Sturgill, T.W.2
  • 215
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne PH, Viciana PR, Downward J. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 1993;364:352-355.
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Viciana, P.R.2    Downward, J.3
  • 216
    • 0029077563 scopus 로고
    • Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1)
    • Russell M, Lange-Carter CA, Johnson GL. Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1). J Biol Chem 1995;270:11757-11760.
    • (1995) J Biol Chem , vol.270 , pp. 11757-11760
    • Russell, M.1    Lange-Carter, C.A.2    Johnson, G.L.3
  • 217
    • 0027964170 scopus 로고
    • The post-translational modification of ras p21 is important for Raf-1 activation
    • Kikuchi A, Williams LT. The post-translational modification of ras p21 is important for Raf-1 activation. J Biol Chem 1994;269:20054-20059.
    • (1994) J Biol Chem , vol.269 , pp. 20054-20059
    • Kikuchi, A.1    Williams, L.T.2
  • 218
    • 0029807304 scopus 로고    scopus 로고
    • Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
    • Farrar MA, Alberola-Ila J, Perlmutter RM. Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization. Nature 1996;383:178-181.
    • (1996) Nature , vol.383 , pp. 178-181
    • Farrar, M.A.1    Alberola-Ila, J.2    Perlmutter, R.M.3
  • 220
    • 0027428530 scopus 로고
    • Raf-1 forms a stable complex with Mek1 and activates Mek1 by serine phosphorylation
    • Huang W, Alessandrini A, Crews CM, Erikson RL. Raf-1 forms a stable complex with Mek1 and activates Mek1 by serine phosphorylation. Proc Natl Acad Sci USA 1993;90:10947-10951.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10947-10951
    • Huang, W.1    Alessandrini, A.2    Crews, C.M.3    Erikson, R.L.4
  • 221
    • 0027304607 scopus 로고
    • Extracellular signals and reversible protein phosphorylation: What to Mek of it all?
    • Crews CM, Erikson. Extracellular signals and reversible protein phosphorylation: What to Mek of it all?. Cell 1993;74:215-217.
    • (1993) Cell , vol.74 , pp. 215-217
    • Crews, C.M.1    Erikson2
  • 222
    • 0029964537 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK) in cardiac tissues
    • Page C, Doubell AF. Mitogen-activated protein kinase (MAPK) in cardiac tissues. Mol Cell Biochem 1996;157:49-57.
    • (1996) Mol Cell Biochem , vol.157 , pp. 49-57
    • Page, C.1    Doubell, A.F.2
  • 223
    • 0028868828 scopus 로고
    • Intracellular signalling through protein kinases in the heart
    • Sugden PH, Bogoyevitch MA. Intracellular signalling through protein kinases in the heart. Cardiovasc Res 1995;30:478-492.
    • (1995) Cardiovasc Res , vol.30 , pp. 478-492
    • Sugden, P.H.1    Bogoyevitch, M.A.2
  • 224
    • 0023766145 scopus 로고
    • Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
    • Sturgill TW, Ray LB, Erikson E, Maller JL. Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II. Nature 1988;334:715-718.
    • (1988) Nature , vol.334 , pp. 715-718
    • Sturgill, T.W.1    Ray, L.B.2    Erikson, E.3    Maller, J.L.4
  • 225
    • 0027991899 scopus 로고
    • Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase
    • Welsh GI, Foulstone EJ, Young SW, Tavare JM, Proud CG. Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase. Biochem J 1994;303:15-20.
    • (1994) Biochem J , vol.303 , pp. 15-20
    • Welsh, G.I.1    Foulstone, E.J.2    Young, S.W.3    Tavare, J.M.4    Proud, C.G.5
  • 226
    • 0027978816 scopus 로고
    • The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor I in the rat skeletal muscle cell line L6 is blocked by wortmannin but not by rapamycin. Evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf
    • Cross DAE, Alessi DR, Vandenheede JR, McDowell HE, Cohen P. The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor I in the rat skeletal muscle cell line L6 is blocked by wortmannin but not by rapamycin. Evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf. Biochem J 1994;303:21-26.
    • (1994) Biochem J , vol.303 , pp. 21-26
    • Cross, D.A.E.1    Alessi, D.R.2    Vandenheede, J.R.3    McDowell, H.E.4    Cohen, P.5
  • 227
    • 0028891049 scopus 로고
    • Does mitogen-activated-protein kinase have a role in insulin action? the cases for and against
    • Denton RM, Tavare JM. Does mitogen-activated-protein kinase have a role in insulin action? The cases for and against. Eur J Biochem 1995;227:597-611.
    • (1995) Eur J Biochem , vol.227 , pp. 597-611
    • Denton, R.M.1    Tavare, J.M.2
  • 228
    • 0027379099 scopus 로고
    • Mitogen-activated protein kinase activation is not sufficient for stimulation of glucose transport or glycogen synthase in 3T3-L1 adipocytes
    • Robinson LJ, Razzack ZF, Lawrence JC. Jr, James, D.E. Mitogen-activated protein kinase activation is not sufficient for stimulation of glucose transport or glycogen synthase in 3T3-L1 adipocytes. J Biol Chem 1993;268:26422-26427.
    • (1993) J Biol Chem , vol.268 , pp. 26422-26427
    • Robinson, L.J.1    Razzack, Z.F.2    Lawrence Jr., J.C.3    James, D.E.4
  • 229
    • 0027181695 scopus 로고
    • Divergence of signaling pathways for insulin in PC-12 pheochromocytoma cells
    • Ohmichi M, Pang L, Ribon V, Saltiel AR. Divergence of signaling pathways for insulin in PC-12 pheochromocytoma cells. Endocrinology 1993;133:46-56.
    • (1993) Endocrinology , vol.133 , pp. 46-56
    • Ohmichi, M.1    Pang, L.2    Ribon, V.3    Saltiel, A.R.4
  • 230
    • 0030329988 scopus 로고    scopus 로고
    • Cell volume and the metabolic actions of insulin
    • Zhande R, Brownsey RW. Cell volume and the metabolic actions of insulin. Biochem Cell Biol 1996;74:513-522.
    • (1996) Biochem Cell Biol , vol.74 , pp. 513-522
    • Zhande, R.1    Brownsey, R.W.2
  • 231
    • 0029981389 scopus 로고    scopus 로고
    • Regulation of both glycogen synthase and PHAS-I by insulin in rat skeletal muscle involves mitogen-activated protein kinase-independent and rapamycin-sensitive pathways
    • Apiazu I, Saltiel AR, DePaoli-Roach AA, Lawrence JC Jr.. Regulation of both glycogen synthase and PHAS-I by insulin in rat skeletal muscle involves mitogen-activated protein kinase-independent and rapamycin-sensitive pathways. J Biol Chem 1996;271:5033-5039.
    • (1996) J Biol Chem , vol.271 , pp. 5033-5039
    • Apiazu, I.1    Saltiel, A.R.2    DePaoli-Roach, A.A.3    Lawrence Jr., J.C.4
  • 232
    • 0029131895 scopus 로고
    • Mitogen-activated protein kinase kinase inhibition does not block the stimulation of glucose utilization by insulin
    • Lazar DF, Wiese RJ, Brady MJ, et al. Mitogen-activated protein kinase kinase inhibition does not block the stimulation of glucose utilization by insulin. J Biol Chem 1995;270:20801-20807.
    • (1995) J Biol Chem , vol.270 , pp. 20801-20807
    • Lazar, D.F.1    Wiese, R.J.2    Brady, M.J.3
  • 233
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinases
    • Karin M. The regulation of AP-1 activity by mitogen-activated protein kinases. J Biol Chem 1995;270:16483-16486.
    • (1995) J Biol Chem , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 234
    • 0025826137 scopus 로고
    • Regulation of gene expression by insulin
    • O'Brien RM, Granner DK. Regulation of gene expression by insulin. Biochem J 1991;278:609-619.
    • (1991) Biochem J , vol.278 , pp. 609-619
    • O'Brien, R.M.1    Granner, D.K.2
  • 235
    • 0026695645 scopus 로고
    • TCF by MAP kinase stimulates ternary complex formation by c-fos promoter
    • TCF by MAP kinase stimulates ternary complex formation by c-fos promoter. Nature 1992;358:414-417.
    • (1992) Nature , vol.358 , pp. 414-417
    • Gille, H.1    Sharrocks, A.D.2    Shaw, P.E.3
  • 236
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase
    • Xing J, Ginty DD, Greenberg ME. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 1996;273:959-963.
    • (1996) Science , vol.273 , pp. 959-963
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 237
    • 0029943487 scopus 로고    scopus 로고
    • Insulin stimulates the serine phosphorylation of the signal transducer and activator of transcription (STAT3) isoform
    • Ceresa BP, Pessin JE. Insulin stimulates the serine phosphorylation of the signal transducer and activator of transcription (STAT3) isoform. J Biol Chem 1996;271:12121-12124.
    • (1996) J Biol Chem , vol.271 , pp. 12121-12124
    • Ceresa, B.P.1    Pessin, J.E.2
  • 238
    • 0028008882 scopus 로고
    • Molecular mechanisms in the control of translation by hormones and growth factors
    • Redpath NT, Proud CG. Molecular mechanisms in the control of translation by hormones and growth factors. Biochim Biophys Acta 1994;1220:147-162.
    • (1994) Biochim Biophys Acta , vol.1220 , pp. 147-162
    • Redpath, N.T.1    Proud, C.G.2
  • 239
    • 0026688510 scopus 로고
    • Substrate recognition determinants of the mitogen-activated 70K S6 kinase from rat liver
    • Flotow H, Thomas G. Substrate recognition determinants of the mitogen-activated 70K S6 kinase from rat liver. J Biol Chem 1992;267:3074-3078.
    • (1992) J Biol Chem , vol.267 , pp. 3074-3078
    • Flotow, H.1    Thomas, G.2
  • 240
    • 0025352294 scopus 로고
    • Differential stimulation of phosphorylation of initiation factors eIF-4F, eIF-4B and eIF-3, and ribosomal protein S6 by insulin and phorbol esters
    • Morley SJ, Traugh JA. Differential stimulation of phosphorylation of initiation factors eIF-4F, eIF-4B and eIF-3, and ribosomal protein S6 by insulin and phorbol esters. J Biol Chem 1990;265:10611-10616.
    • (1990) J Biol Chem , vol.265 , pp. 10611-10616
    • Morley, S.J.1    Traugh, J.A.2
  • 241
    • 0025277333 scopus 로고
    • Energy substrate utilization by isolated working hearts from newborn rabbits
    • Lopaschuk GD, Spafford MA. Energy substrate utilization by isolated working hearts from newborn rabbits. Am J Physiol 1990;258:H1274-H1280.
    • (1990) Am J Physiol , vol.258
    • Lopaschuk, G.D.1    Spafford, M.A.2
  • 242
    • 0029609649 scopus 로고
    • Differential expression of alpha- And beta-enolase genes during rat heart development and hypertrophy
    • Keller A, Rouzeau J-D, Farhadian F, et al. Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy. Am J Physiol 1995;269:H1843-H1851.
    • (1995) Am J Physiol , vol.269
    • Keller, A.1    Rouzeau, J.-D.2    Farhadian, F.3
  • 243
    • 0019818758 scopus 로고
    • Glucose intolerance and aging
    • Defronzo RA. Glucose intolerance and aging. Diabetes Care 1981;4:493-501.
    • (1981) Diabetes Care , vol.4 , pp. 493-501
    • Defronzo, R.A.1
  • 245
    • 0026021161 scopus 로고
    • Insulin resistance. a multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidemia, and atherosclerotic cardiovascular disease
    • Defronzo RA, Ferrannini E. Insulin resistance. A multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidemia, and atherosclerotic cardiovascular disease. Diab Care 1991;14:173-194.
    • (1991) Diab Care , vol.14 , pp. 173-194
    • Defronzo, R.A.1    Ferrannini, E.2
  • 246
    • 0023191508 scopus 로고
    • Insulin resistance in essential hypertension
    • Ferrannini E, Buzzigoli G, Bonadonna R, et al. Insulin resistance in essential hypertension. N Engl J Med 1987;317:350-357.
    • (1987) N Engl J Med , vol.317 , pp. 350-357
    • Ferrannini, E.1    Buzzigoli, G.2    Bonadonna, R.3
  • 247
    • 0029117576 scopus 로고
    • Decreased GLUT4 mRNA content and insulin-sensitive deoxyglucose uptake show insulin resistance in hypertensive rat heart
    • Paternostro G, Clarke K, Heath J, Seymour A-ML, Radda GK. Decreased GLUT4 mRNA content and insulin-sensitive deoxyglucose uptake show insulin resistance in hypertensive rat heart. Cardiovasc Res 1995;30:205-211.
    • (1995) Cardiovasc Res , vol.30 , pp. 205-211
    • Paternostro, G.1    Clarke, K.2    Heath, J.3    Seymour, A.-M.L.4    Radda, G.K.5
  • 248
    • 0017759141 scopus 로고
    • Evidence for cardiomyopathy in familial diabetes mellitus
    • Regan TJ, Lyons MM, Ahmad SS, et al. Evidence for cardiomyopathy in familial diabetes mellitus. J Clin Invest 1977;60:885-899.
    • (1977) J Clin Invest , vol.60 , pp. 885-899
    • Regan, T.J.1    Lyons, M.M.2    Ahmad, S.S.3
  • 250
    • 0029120517 scopus 로고
    • Insulin action on heart and skeletal muscle glucose uptake in essential hypertension
    • Nuutila P, Maki M, Laine H, et al. Insulin action on heart and skeletal muscle glucose uptake in essential hypertension. J Clin Invest 1995;96:1003-1009.
    • (1995) J Clin Invest , vol.96 , pp. 1003-1009
    • Nuutila, P.1    Maki, M.2    Laine, H.3
  • 252
    • 0343753399 scopus 로고
    • Pretranslational regulation of glucose transporter isoform expression in hearts with pressure-overload left ventricular hypertrophy
    • Abstract
    • Weinberg EO, Thienelt CD, Lorell BH. Pretranslational regulation of glucose transporter isoform expression in hearts with pressure-overload left ventricular hypertrophy. Circulation 1995;92:I-365. (Abstract).
    • (1995) Circulation , vol.92
    • Weinberg, E.O.1    Thienelt, C.D.2    Lorell, B.H.3
  • 253
    • 0028656481 scopus 로고
    • Calcium overload during reperfusion is accelerated in isolated hypertrophied rat hearts
    • Allard MF, Flint JDA, English JC, et al. Calcium overload during reperfusion is accelerated in isolated hypertrophied rat hearts. J Mol Cell Cardiol 1994;26:1551-1563.
    • (1994) J Mol Cell Cardiol , vol.26 , pp. 1551-1563
    • Allard, M.F.1    Flint, J.D.A.2    English, J.C.3
  • 254
    • 0029124119 scopus 로고
    • Propionyl L-carnitine improvement of hypertrophied heart function is accompanied by an increase in carbohydrate oxidation
    • Schönekess BO, Allard MF, Lopaschuk GD. Propionyl L-carnitine improvement of hypertrophied heart function is accompanied by an increase in carbohydrate oxidation. Circ Res 1995;77:726-734.
    • (1995) Circ Res , vol.77 , pp. 726-734
    • Schönekess, B.O.1    Allard, M.F.2    Lopaschuk, G.D.3
  • 255
    • 33750707633 scopus 로고    scopus 로고
    • Recovery of glycolysis and oxidative metabolism during postischemic reperfusion of hypertrophied rat hearts
    • Schönekess BO, Allard MF, Lopaschuk GD. Recovery of glycolysis and oxidative metabolism during postischemic reperfusion of hypertrophied rat hearts. Am J Physiol 1996;271:H798-H805.
    • (1996) Am J Physiol , vol.271
    • Schönekess, B.O.1    Allard, M.F.2    Lopaschuk, G.D.3
  • 256
    • 0023885409 scopus 로고
    • Effects of moderate hypertension on cardiac function and metabolism in the rabbit
    • Taegtmeyer H, Overturf ML. Effects of moderate hypertension on cardiac function and metabolism in the rabbit. Hypertension 1988;11:416-426.
    • (1988) Hypertension , vol.11 , pp. 416-426
    • Taegtmeyer, H.1    Overturf, M.L.2
  • 257
    • 0002531199 scopus 로고
    • Evidence for increased glycolytic metabolism in cardiac hypertrophy and congestive heart failure
    • Alpert N, ed. New York: Academic Press
    • Bishop SP, Aultschuld RA. Evidence for increased glycolytic metabolism in cardiac hypertrophy and congestive heart failure. In: Alpert N, ed. Cardiac Hypertrophy. New York: Academic Press, 1971:567-585.
    • (1971) Cardiac Hypertrophy , pp. 567-585
    • Bishop, S.P.1    Aultschuld, R.A.2
  • 258
    • 0042671505 scopus 로고
    • Insulin effects on protein synthesis are independent of glucose and energy metabolism
    • Flaim KE, Kochel PJ, Kira Y, et al. Insulin effects on protein synthesis are independent of glucose and energy metabolism. Am J Physiol 1983;245:C133-C143.
    • (1983) Am J Physiol , vol.245
    • Flaim, K.E.1    Kochel, P.J.2    Kira, Y.3
  • 259
    • 0030450322 scopus 로고    scopus 로고
    • Serum from patients with chronic renal insufficiency alters growth characteristics and ANP mRNA expression of adult rat cardiac myocytes
    • in press
    • Yu JZ, Bondy GP, Allard MF, et al. Serum from patients with chronic renal insufficiency alters growth characteristics and ANP mRNA expression of adult rat cardiac myocytes. J Mol Cell Cardiol 1996;in press.
    • (1996) J Mol Cell Cardiol
    • Yu, J.Z.1    Bondy, G.P.2    Allard, M.F.3
  • 260
    • 0029148426 scopus 로고
    • Cardiac and adipose tissue abnormalities but not diabetes in mice deficient in GLUT4
    • Katz EB, Stenbit AE, Hatton K, DePinho R, Charron MJ. Cardiac and adipose tissue abnormalities but not diabetes in mice deficient in GLUT4. Nature 1995;377:151-155.
    • (1995) Nature , vol.377 , pp. 151-155
    • Katz, E.B.1    Stenbit, A.E.2    Hatton, K.3    DePinho, R.4    Charron, M.J.5
  • 261
    • 0028847159 scopus 로고
    • Rapamycin selectively inhibits angiotensin II-induced increase in protein synthesis in cardiac myocytes in vitro. Potential role of 70-kD S6 kinase in angiotensin II-induced cardiac hypertrophy
    • Sadoshima J, Izumo S. Rapamycin selectively inhibits angiotensin II-induced increase in protein synthesis in cardiac myocytes in vitro. Potential role of 70-kD S6 kinase in angiotensin II-induced cardiac hypertrophy. Circ Res 1995;77:1040-1052.
    • (1995) Circ Res , vol.77 , pp. 1040-1052
    • Sadoshima, J.1    Izumo, S.2
  • 262
    • 0026759874 scopus 로고
    • Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase
    • Price DJ, Grove JR, Calvo V, Avruch J, Bierer BE. Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase. Science 1992;257:973-977.
    • (1992) Science , vol.257 , pp. 973-977
    • Price, D.J.1    Grove, J.R.2    Calvo, V.3    Avruch, J.4    Bierer, B.E.5
  • 263
    • 0029147360 scopus 로고
    • Angiotensin II induces tyrosine phosphorylation of insulin receptor substrate 1 and its association with phosphatidylinositol 3-kinase in rat heart
    • Saad MJA, Velloso LA, Carvalho CRO. Angiotensin II induces tyrosine phosphorylation of insulin receptor substrate 1 and its association with phosphatidylinositol 3-kinase in rat heart. Biochem J 1995;310:741-744.
    • (1995) Biochem J , vol.310 , pp. 741-744
    • Saad, M.J.A.1    Velloso, L.A.2    Carvalho, C.R.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.