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Volumn 46, Issue 11, 1997, Pages 1270-1274

Insulin inhibition of 5' adenosine monophosphate-activated protein kinase in the heart results in activation of acetyl coenzyme A carboxylase and inhibition of fatty acid oxidation

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ADENOSINE PHOSPHATE; FATTY ACID; GLUCOSE; INSULIN; PALMITIC ACID; PROTEIN KINASE; TRITIUM;

EID: 0030869792     PISSN: 00260495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0026-0495(97)90229-8     Document Type: Article
Times cited : (119)

References (29)
  • 1
    • 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 36:415-439, 1974
    • (1974) Annu Rev Physiol , vol.36 , pp. 415-439
    • Neely, J.R.1    Morgan, H.E.2
  • 2
    • 0025821485 scopus 로고
    • Myocardial triglyceride turnover and contribution to energy substrate utilization in isolated working rat hearts
    • Saddik M, Lopaschuk GD: Myocardial triglyceride turnover and contribution to energy substrate utilization in isolated working rat hearts. J Biol Chem 266:8162-8170, 1991
    • (1991) J Biol Chem , vol.266 , pp. 8162-8170
    • Saddik, M.1    Lopaschuk, G.D.2
  • 3
    • 0018126246 scopus 로고
    • Characteristics of fatty acid oxidation in liver homogenates and the inhibitory effect of malonyl CoA
    • McGarry JD, Mannaerts GP, Foster DW: Characteristics of fatty acid oxidation in liver homogenates and the inhibitory effect of malonyl CoA. Biochim Biophys Acta 530:305-313, 1978
    • (1978) Biochim Biophys Acta , vol.530 , pp. 305-313
    • McGarry, J.D.1    Mannaerts, G.P.2    Foster, D.W.3
  • 4
    • 0021193646 scopus 로고
    • i values
    • i values. J Biol Chem 259:12030-12033, 1984
    • (1984) J Biol Chem , vol.259 , pp. 12030-12033
    • Cook, G.A.1
  • 5
    • 0027453493 scopus 로고
    • Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart
    • Saddik M, Gamble J, Witters LA, et al: Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart. J Biol Chem 268:25836-25845, 1993
    • (1993) J Biol Chem , vol.268 , pp. 25836-25845
    • Saddik, M.1    Gamble, J.2    Witters, L.A.3
  • 6
    • 0027486343 scopus 로고
    • Malonyl CoA metabolism in cardiac myocytes and its relevance to the control of fatty acid oxidation
    • Awan MM, Saggerson ED: Malonyl CoA metabolism in cardiac myocytes and its relevance to the control of fatty acid oxidation. Biochem J 295:61-66, 1993
    • (1993) Biochem J , vol.295 , pp. 61-66
    • Awan, M.M.1    Saggerson, E.D.2
  • 7
    • 0028116128 scopus 로고
    • Acetyl CoA carboxylase involvement in the rapid maturation of fatty acid oxidation in the newborn rabbit heart
    • Lopaschuk GD, Witters LA, Itoi T, et al: Acetyl CoA carboxylase involvement in the rapid maturation of fatty acid oxidation in the newborn rabbit heart. J Biol Chem 269:25871-25878, 1994
    • (1994) J Biol Chem , vol.269 , pp. 25871-25878
    • Lopaschuk, G.D.1    Witters, L.A.2    Itoi, T.3
  • 8
    • 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 A, Barr, R, et al: 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 270:17513-17520, 1995
    • (1995) J Biol Chem , vol.270 , pp. 17513-17520
    • Kudo, N.1    Barr, A.2    Barr, R.3
  • 9
    • 0025021124 scopus 로고
    • Identification of an isozymic form of acetyl CoA carboxylase
    • Bianchi A, Evans JL, Iverson AJ, et al: Identification of an isozymic form of acetyl CoA carboxylase. J Biol Chem 265:1502-1509, 1990
    • (1990) J Biol Chem , vol.265 , pp. 1502-1509
    • Bianchi, A.1    Evans, J.L.2    Iverson, A.J.3
  • 10
    • 0024459546 scopus 로고
    • Formation of malonyl coenzyme A in rat heart
    • Thampy KG: Formation of malonyl coenzyme A in rat heart. J Biol Chem 264:17631-17634, 1989
    • (1989) J Biol Chem , vol.264 , pp. 17631-17634
    • Thampy, K.G.1
  • 11
    • 0024460580 scopus 로고
    • Role of reversible phosphorylation of acetyl CoA carboxylase in long chain fatty acid biosynthesis
    • Kim KH, Lopez-Casillas F, Bai DH, et al: Role of reversible phosphorylation of acetyl CoA carboxylase in long chain fatty acid biosynthesis. FASEB J 3:2250-2256, 1989
    • (1989) FASEB J , vol.3 , pp. 2250-2256
    • Kim, K.H.1    Lopez-Casillas, F.2    Bai, D.H.3
  • 12
    • 0030015194 scopus 로고    scopus 로고
    • Characterization of 5′ AMP-activated protein kinase activity in the heart and its role in inhibiting acetyl CoA carboxylase during reperfusion following ischemia
    • Kudo N, Gillespie JG, Kung L, et al: Characterization of 5′ AMP-activated protein kinase activity in the heart and its role in inhibiting acetyl CoA carboxylase during reperfusion following ischemia. Biochim Biophys Acta 1301:67-75, 1996
    • (1996) Biochim Biophys Acta , vol.1301 , pp. 67-75
    • Kudo, N.1    Gillespie, J.G.2    Kung, L.3
  • 13
    • 0025192341 scopus 로고
    • Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase
    • Davies SP, Sim ATR, Hardie DG: Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase. Eur J Biochem 187:183-190, 1990
    • (1990) Eur J Biochem , vol.187 , pp. 183-190
    • Davies, S.P.1    Sim, A.T.R.2    Hardie, D.G.3
  • 14
    • 0026782061 scopus 로고
    • Insulin activation of acetyl CoA carboxylase accompanied by inhibition of 5′-AMP-activated protein kinase
    • Witters LA, Kemp BE: Insulin activation of acetyl CoA carboxylase accompanied by inhibition of 5′-AMP-activated protein kinase. J Biol Chem 267;2864-2867, 1992
    • (1992) J Biol Chem , vol.267 , pp. 2864-2867
    • Witters, L.A.1    Kemp, B.E.2
  • 15
    • 10244271029 scopus 로고
    • Effect of epinephrine, norepinephrine, glucose, and insulin on extraction and oxidation of free fatty acid by the myocardium
    • Gousios A, Felts JM: Effect of epinephrine, norepinephrine, glucose, and insulin on extraction and oxidation of free fatty acid by the myocardium. Circulation 28:729-734, 1963
    • (1963) Circulation , vol.28 , pp. 729-734
    • Gousios, A.1    Felts, J.M.2
  • 16
    • 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 28:117-146, 1989
    • (1989) Prog Lipid Res , vol.28 , pp. 117-146
    • Hardie, D.G.1
  • 17
    • 0024786438 scopus 로고
    • Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl CoA reductase kinase activities
    • Carling D, Clarke PR, Zammit V, et al: Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl CoA reductase kinase activities. Eur J Biochem 186:129-136, 1989
    • (1989) Eur J Biochem , vol.186 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.3
  • 18
    • 0025915269 scopus 로고
    • Evidence that AMP triggers phosphorylation as well as direct allosteric activation of fat liver AMP-activated protein kinase. A sensitive mechanism to protect the cell against ATP depletion
    • Moore F, Weekes J, Hardie DG: Evidence that AMP triggers phosphorylation as well as direct allosteric activation of fat liver AMP-activated protein kinase. A sensitive mechanism to protect the cell against ATP depletion. Eur J Biochem 199:691-697, 1991
    • (1991) Eur J Biochem , vol.199 , pp. 691-697
    • Moore, F.1    Weekes, J.2    Hardie, D.G.3
  • 19
    • 0028845251 scopus 로고
    • 2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
    • 2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J Biol Chem 2:27186-27191, 1995
    • (1995) J Biol Chem , vol.2 , pp. 27186-27191
    • Hawley, S.A.1    Selbert, M.A.2    Goldstein, D.G.3
  • 20
    • 0029561919 scopus 로고
    • 5′ AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC
    • Davies SP, Helps NR, Cohen PTW, et al: 5′ AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC. FEBS Lett 377:421-425, 1995
    • (1995) FEBS Lett , vol.377 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.W.3
  • 21
    • 0026808466 scopus 로고
    • Glucose regulation of acetyl-CoA carboxylase in hepatoma and islet cells
    • Louis NA, Witters LA: Glucose regulation of acetyl-CoA carboxylase in hepatoma and islet cells. J Biol Chem 267:2287-2293, 1992
    • (1992) J Biol Chem , vol.267 , pp. 2287-2293
    • Louis, N.A.1    Witters, L.A.2
  • 22
    • 0026350712 scopus 로고
    • Regulation of intracellular acetyl CoA carboxylase by ATP depletors mimics the action of the 5′-AMP-activated protein kinase
    • Witters LA, Nordlund A, Marshall L: Regulation of intracellular acetyl CoA carboxylase by ATP depletors mimics the action of the 5′-AMP-activated protein kinase. Biochem Biophys Res Commun 181:1486-1492, 1991
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 1486-1492
    • Witters, L.A.1    Nordlund, A.2    Marshall, L.3
  • 23
    • 0028406897 scopus 로고
    • Role of the AMP-activated protein kinase in the cellular stress
    • Corton JM, Gillespie JG, Hardie DG: Role of the AMP-activated protein kinase in the cellular stress. Curr Biol 4:315-324, 1994
    • (1994) Curr Biol , vol.4 , pp. 315-324
    • Corton, J.M.1    Gillespie, J.G.2    Hardie, D.G.3
  • 24
    • 0028961963 scopus 로고
    • Catalytic subunits of the porcine and rat 5′-AMP-activated protein kinase are members of the SNF1 protein kinase family
    • Gao G, Widmer J, Stapleton D, et al: Catalytic subunits of the porcine and rat 5′-AMP-activated protein kinase are members of the SNF1 protein kinase family. Biochim Biophys Acta 1266:73-82, 1995
    • (1995) Biochim Biophys Acta , vol.1266 , pp. 73-82
    • Gao, G.1    Widmer, J.2    Stapleton, D.3
  • 25
    • 0028922528 scopus 로고
    • The AMP-activated protein kinase gene is highly expressed in skeletal muscle: Alternative splicing and tissue distribution of the mRNA
    • Verhoeven AJ, Woods A, Brennan CH, et al: The AMP-activated protein kinase gene is highly expressed in skeletal muscle: Alternative splicing and tissue distribution of the mRNA. Eur J Biochem 228:236-243, 1995
    • (1995) Eur J Biochem , vol.228 , pp. 236-243
    • Verhoeven, A.J.1    Woods, A.2    Brennan, C.H.3
  • 26
    • 0027985194 scopus 로고
    • Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: A major regulator of lipid metabolism in mammals
    • Aguan K, Scoot J, See CG, et al: Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: A major regulator of lipid metabolism in mammals. Gene 149:345-350, 1994
    • (1994) Gene , vol.149 , pp. 345-350
    • Aguan, K.1    Scoot, J.2    See, C.G.3
  • 27
    • 13344285343 scopus 로고    scopus 로고
    • Mammalian AMP-activated protein kinase subfamily
    • Stapleton D, Mitchelhill KI, Gao G, et al: Mammalian AMP-activated protein kinase subfamily. J Biol Chem 271:611-614, 1996
    • (1996) J Biol Chem , vol.271 , pp. 611-614
    • Stapleton, D.1    Mitchelhill, K.I.2    Gao, G.3
  • 28
    • 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, et al: Unique structural features and differential phosphorylation of the 280-kDa component (isozyme) of rat liver acetyl CoA carboxylase. J Biol Chem 269:14438-14445, 1994
    • (1994) J Biol Chem , vol.269 , pp. 14438-14445
    • Winz, R.1    Hess, D.2    Aebersold, R.3
  • 29
    • 0030029586 scopus 로고    scopus 로고
    • Acetyl coenzyme a carboxylase activity in neonatal rat cardiac myocytes in culture: Citrate dependence and effects of hypoxia
    • Wang D, Buja LM, McMillin JB: Acetyl coenzyme A carboxylase activity in neonatal rat cardiac myocytes in culture: Citrate dependence and effects of hypoxia. Arch Biochem Biophys 325:249-255, 1996
    • (1996) Arch Biochem Biophys , vol.325 , pp. 249-255
    • Wang, D.1    Buja, L.M.2    McMillin, J.B.3


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