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Volumn 65, Issue 23, 2008, Pages 3737-3755

AMP-activated protein kinase in skeletal muscle: From structure and localization to its role as a master regulator of cellular metabolism

Author keywords

Ca2+ calmodulin dependent protein kinase kinase; Carbohydrate; Glucose; Lipid; LKB1; Protein phosphatase; Transforming growth factor activated kinase 1

Indexed keywords

A 769662; CALCIUM; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; ENZYME ACTIVATOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; METFORMIN; PHOSPHOPROTEIN PHOSPHATASE; PIOGLITAZONE; PROTEIN KINASE LKB1; REACTIVE OXYGEN METABOLITE; ROSIGLITAZONE; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; UNCLASSIFIED DRUG;

EID: 57349094302     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8244-6     Document Type: Review
Times cited : (203)

References (165)
  • 1
    • 0022371303 scopus 로고
    • Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5′-monophosphate
    • Ferrer, A., Caelles, C., Massot, N., and Hegardt, F. G. (1985) Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5′-monophosphate. Biochem. Biophys. Res Commun. 132, 497-504.
    • (1985) Biochem. Biophys. Res Commun , vol.132 , pp. 497-504
    • Ferrer, A.1    Caelles, C.2    Massot, N.3    Hegardt, F.G.4
  • 2
    • 0023642627 scopus 로고
    • A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis
    • Carling, D., Zammit, V. A., and Hardie, D. G. (1987) A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis. FEBS Lett. 223, 217-222.
    • (1987) FEBS Lett , vol.223 , pp. 217-222
    • Carling, D.1    Zammit, V.A.2    Hardie, D.G.3
  • 3
    • 0023789884 scopus 로고
    • Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase
    • Munday, M. R., Campbell, D. G., Carling, D., and Hardie, D. G. (1988) Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase. Eur. J Biochem. 175, 331-338.
    • (1988) Eur. J Biochem , vol.175 , pp. 331-338
    • Munday, M.R.1    Campbell, D.G.2    Carling, D.3    Hardie, D.G.4
  • 4
    • 0022534202 scopus 로고
    • A yeast gene that is essential for release from glucose repression encodes a protein kinase
    • Celenza, J. L. and Carlson, M. (1986) A yeast gene that is essential for release from glucose repression encodes a protein kinase. Science. 233, 1175-1180.
    • (1986) Science , vol.233 , pp. 1175-1180
    • Celenza, J.L.1    Carlson, M.2
  • 5
    • 0028126820 scopus 로고
    • Mammalian 5′-AMP-activated protein kinase non-catalytic subunits are homologs of proteins that interact with yeast Snf1 protein kinase
    • Stapleton, D., Gao, G., Michell, B. J., Widmer, J., Mitchelhill, K., Teh, T., House, C. M., Witters, L. A., and Kemp, B. E. (1994) Mammalian 5′-AMP-activated protein kinase non-catalytic subunits are homologs of proteins that interact with yeast Snf1 protein kinase. J. Biol. Chem. 269, 29343-29346.
    • (1994) J. Biol. Chem , vol.269 , pp. 29343-29346
    • Stapleton, D.1    Gao, G.2    Michell, B.J.3    Widmer, J.4    Mitchelhill, K.5    Teh, T.6    House, C.M.7    Witters, L.A.8    Kemp, B.E.9
  • 6
    • 0028070457 scopus 로고
    • Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo
    • Woods, A., Munday, M. R., Scott, J., Yang, X., Carlson, M., and Carling, D. (1994) Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo. J Biol. Chem. 269, 19509-19515.
    • (1994) J Biol. Chem , vol.269 , pp. 19509-19515
    • Woods, A.1    Munday, M.R.2    Scott, J.3    Yang, X.4    Carlson, M.5    Carling, D.6
  • 7
    • 0027932717 scopus 로고
    • Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase
    • Mitchelhill, K. I., Stapleton, D., Gao, G., House, C., Michell, B., Katsis, f., Witters, L. A., and Kemp, B. E. (1994) Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase. J. Biol. Chem. 269, 2361-2364.
    • (1994) J. Biol. Chem , vol.269 , pp. 2361-2364
    • Mitchelhill, K.I.1    Stapleton, D.2    Gao, G.3    House, C.4    Michell, B.5    Katsis, F.6    Witters, L.A.7    Kemp, B.E.8
  • 8
    • 0028068882 scopus 로고
    • Purification of the AMP-activated protein kinase on ATP-gamma-sepharose and analysis of its subunit structure
    • Davies, S. P., Hawley, S. A., Woods, A., Carling, D., Haystead, T. A., and Hardie, D. G. (1994) Purification of the AMP-activated protein kinase on ATP-gamma-sepharose and analysis of its subunit structure. Eur. J Biochem. 223, 351-357.
    • (1994) Eur. J Biochem , vol.223 , pp. 351-357
    • Davies, S.P.1    Hawley, S.A.2    Woods, A.3    Carling, D.4    Haystead, T.A.5    Hardie, D.G.6
  • 9
    • 0029925785 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro
    • Woods, A., Cheung, P. C., Smith, F. C., Davison, M. D., Scott, J., Beri, R. K., and Carling, D. (1996) Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro. J. Biol. Chem. 271, 10282-10290.
    • (1996) J. Biol. Chem , vol.271 , pp. 10282-10290
    • Woods, A.1    Cheung, P.C.2    Smith, F.C.3    Davison, M.D.4    Scott, J.5    Beri, R.K.6    Carling, D.7
  • 11
    • 0030592623 scopus 로고    scopus 로고
    • The alpha1 and alpha2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
    • Woods, A., Salt, I., Scott, J., Hardie, D. G., and Carling, D. (1996) The alpha1 and alpha2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro. FEBS Lett. 397, 347-351.
    • (1996) FEBS Lett , vol.397 , pp. 347-351
    • Woods, A.1    Salt, I.2    Scott, J.3    Hardie, D.G.4    Carling, D.5
  • 14
    • 0032524622 scopus 로고    scopus 로고
    • Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle
    • Thornton, C., Snowden, M. A., and Carling, D. (1998) Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle. J. Biol. Chem. 273, 12443-12450.
    • (1998) J. Biol. Chem , vol.273 , pp. 12443-12450
    • Thornton, C.1    Snowden, M.A.2    Carling, D.3
  • 15
    • 0034654362 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding
    • Cheung, P. C., Salt, I. P., Davies, S. P., Hardie, D. G., and Carling, D. (2000) Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. Biochem. J. 346 Pt 3, 659-669.
    • (2000) Biochem. J , vol.346 , Issue.PART 3 , pp. 659-669
    • Cheung, P.C.1    Salt, I.P.2    Davies, S.P.3    Hardie, D.G.4    Carling, D.5
  • 17
    • 33846945033 scopus 로고    scopus 로고
    • Conserved alpha-helix acts as autoinhibitory sequence in AMP-activated protein kinase alpha subunits
    • Pang, T., Xiong, B., Li, J. Y., Qiu, B. Y., Jin, G. Z., Shen, J. K., and Li, J. (2007) Conserved alpha-helix acts as autoinhibitory sequence in AMP-activated protein kinase alpha subunits. J. Biol. Chem. 282, 495-506.
    • (2007) J. Biol. Chem , vol.282 , pp. 495-506
    • Pang, T.1    Xiong, B.2    Li, J.Y.3    Qiu, B.Y.4    Jin, G.Z.5    Shen, J.K.6    Li, J.7
  • 18
    • 0032567252 scopus 로고    scopus 로고
    • Functional domains of the alpha1 catalytic subunit of the AMP- activated protein kinase
    • Crute, B. E., Seefeld, K., Gamble, J., Kemp, B. E., and Witters, L. A. (1998) Functional domains of the alpha1 catalytic subunit of the AMP- activated protein kinase. J. Biol. Chem. 273, 35347-35354.
    • (1998) J. Biol. Chem , vol.273 , pp. 35347-35354
    • Crute, B.E.1    Seefeld, K.2    Gamble, J.3    Kemp, B.E.4    Witters, L.A.5
  • 19
    • 17144362480 scopus 로고    scopus 로고
    • AMP-activated protein kinase beta subunit tethers alpha and gamma subunits via its C-terminal sequence (186-270)
    • Iseli, T. J., Walter, M., van Denderen, B. J., Katsis, f., Witters, L. A., Kemp, B. E., Michell, B. J., and Stapleton, D. (2005) AMP-activated protein kinase beta subunit tethers alpha and gamma subunits via its C-terminal sequence (186-270). J. Biol. Chem. 280, 13395-13400.
    • (2005) J. Biol. Chem , vol.280 , pp. 13395-13400
    • Iseli, T.J.1    Walter, M.2    van Denderen, B.J.3    Katsis, F.4    Witters, L.A.5    Kemp, B.E.6    Michell, B.J.7    Stapleton, D.8
  • 21
    • 33847080728 scopus 로고    scopus 로고
    • AMP-activated protein kinase in metabolic control and insulin signaling
    • Towler, M. C. and Hardie, D. G. (2007) AMP-activated protein kinase in metabolic control and insulin signaling. Circ Res. 100, 328-341.
    • (2007) Circ Res , vol.100 , pp. 328-341
    • Towler, M.C.1    Hardie, D.G.2
  • 22
    • 0032529139 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Greater AMP dependence, and preferential nuclear localization, of complexes containing the alpha2 isoform
    • Salt, I., Celler, J. W., Hawley, S. A., Prescott, A., Woods, A., Carling, D., and Hardie, D. G. (1998) AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the alpha2 isoform. Biochem. J. 334 ( Pt 1), 177-187.
    • (1998) Biochem. J , vol.334 , Issue.PART 1 , pp. 177-187
    • Salt, I.1    Celler, J.W.2    Hawley, S.A.3    Prescott, A.4    Woods, A.5    Carling, D.6    Hardie, D.G.7
  • 23
    • 0035282062 scopus 로고    scopus 로고
    • Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization
    • Warden, S. M., Richardson, C., O'donnell, J. J., Stapleton, D., Kemp, B. E., and Witters, L. A. (2001) Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization. Biochem. J. 354, 275-283.
    • (2001) Biochem. J , vol.354 , pp. 275-283
    • Warden, S.M.1    Richardson, C.2    O'donnell, J.J.3    Stapleton, D.4    Kemp, B.E.5    Witters, L.A.6
  • 26
    • 0038814313 scopus 로고    scopus 로고
    • A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias
    • Hudson, E. R., Pan, D. A., James, J., Lucocq, J. M., Hawley, S. A., Green, K. A., Baba, O., Terashima, T., and Hardie, D. G. (2003) A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias. Curr. Biol. 13, 861-866.
    • (2003) Curr. Biol , vol.13 , pp. 861-866
    • Hudson, E.R.1    Pan, D.A.2    James, J.3    Lucocq, J.M.4    Hawley, S.A.5    Green, K.A.6    Baba, O.7    Terashima, T.8    Hardie, D.G.9
  • 27
    • 1342332128 scopus 로고    scopus 로고
    • Bateman domains and adenosine derivatives form a binding contract
    • Kemp, B. E. (2004) Bateman domains and adenosine derivatives form a binding contract. J Clin. Invest. 113, 182-184.
    • (2004) J Clin. Invest , vol.113 , pp. 182-184
    • Kemp, B.E.1
  • 28
    • 85047691317 scopus 로고    scopus 로고
    • CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations
    • Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., and Hardie, D. G. (2004) CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 113, 274-284.
    • (2004) J. Clin. Invest , vol.113 , pp. 274-284
    • Scott, J.W.1    Hawley, S.A.2    Green, K.A.3    Anis, M.4    Stewart, G.5    Scullion, G.A.6    Norman, D.G.7    Hardie, D.G.8
  • 29
    • 0033054706 scopus 로고    scopus 로고
    • Cellular distribution and developmental expression of AMP-activated protein kinase isoforms in mouse central nervous system
    • Turnley, A. M., Stapleton, D., Mann, R. J., Witters, L. A., Kemp, B. E., and Bartlett, P. F. (1999) Cellular distribution and developmental expression of AMP-activated protein kinase isoforms in mouse central nervous system. J. Neurochem. 72, 1707-1716.
    • (1999) J. Neurochem , vol.72 , pp. 1707-1716
    • Turnley, A.M.1    Stapleton, D.2    Mann, R.J.3    Witters, L.A.4    Kemp, B.E.5    Bartlett, P.F.6
  • 31
    • 36048930364 scopus 로고    scopus 로고
    • Localization of AMP kinase is regulated by stress, cell density, and signaling through the MEK - > ERK1/2 pathway
    • Kodiha, M., Rassi, J. G., Brown, C. M., and Stochaj, U. (2007) Localization of AMP kinase is regulated by stress, cell density, and signaling through the MEK - > ERK1/2 pathway. Am. J. Physiol. Cell Physiol. 293, C1427-C1436.
    • (2007) Am. J. Physiol. Cell Physiol , vol.293
    • Kodiha, M.1    Rassi, J.G.2    Brown, C.M.3    Stochaj, U.4
  • 32
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
    • Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., and Hardie, D. G. (1996) Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J. Biol. Chem. 271, 27879-27887.
    • (1996) J. Biol. Chem , vol.271 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 33
    • 0018963044 scopus 로고
    • Regulation of rat liver acetyl-CoA carboxylase. Regulation of phosphorylation and inactivation of acetyl-CoA carboxylase by the adenylate energy charge
    • Yeh, L. A., Lee, K. H., and Kim, K. H. (1980) Regulation of rat liver acetyl-CoA carboxylase. Regulation of phosphorylation and inactivation of acetyl-CoA carboxylase by the adenylate energy charge. J. Biol. Chem. 255, 2308-2314.
    • (1980) J. Biol. Chem , vol.255 , pp. 2308-2314
    • Yeh, L.A.1    Lee, K.H.2    Kim, K.H.3
  • 34
    • 85047689953 scopus 로고
    • 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells?
    • Corton, J. M., Gillespie, J. G., Hawley, S. A., and Hardie, D. G. (1995) 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells? Eur. J. Biochem. 229, 558-565.
    • (1995) Eur. J. Biochem , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 35
    • 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, S. P., Helps, N. R., Cohen, P. T., and Hardie, D. G. (1995) 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) FEBS Lett , vol.377 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.3    Hardie, D.G.4
  • 36
    • 33845949733 scopus 로고    scopus 로고
    • Dissecting the role of 5′-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase
    • Suter, M., Riek, U., Tuerk, R., Schlattner, U., Wallimann, T., and Neumann, D. (2006) Dissecting the role of 5′-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase. J. Biol. Chem. 281, 32207-32216.
    • (2006) J. Biol. Chem , vol.281 , pp. 32207-32216
    • Suter, M.1    Riek, U.2    Tuerk, R.3    Schlattner, U.4    Wallimann, T.5    Neumann, D.6
  • 38
    • 0345107247 scopus 로고    scopus 로고
    • Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Makela, T. P., Alessi, D. R., and Hardie, D. G. (2003) Complexes between the LKB1 tumor suppressor, STRADalpha/beta and MO25alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J. Biol. 2, 28-
    • Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Makela, T. P., Alessi, D. R., and Hardie, D. G. (2003) Complexes between the LKB1 tumor suppressor, STRADalpha/beta and MO25alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J. Biol. 2, 28-
  • 39
    • 0041305909 scopus 로고    scopus 로고
    • Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases
    • Hong, S. P., Leiper, F. C., Woods, A., Carling, D., and Carlson, M. (2003) Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases. Proc. Natl. Acad. Sci. U. S. A 100, 8839-8843.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 8839-8843
    • Hong, S.P.1    Leiper, F.C.2    Woods, A.3    Carling, D.4    Carlson, M.5
  • 40
  • 41
    • 0036499467 scopus 로고    scopus 로고
    • Identification and characterization of four novel phosphorylation sites (Ser31, Ser325, Thr336 and Thr366) on LKB1/STK11, the protein kinase mutated in Peutz-Jeghers cancer syndrome
    • Sapkota, G. P., Boudeau, J., Deak, M., Kieloch, A., Morrice, N., and Alessi, D. R. (2002) Identification and characterization of four novel phosphorylation sites (Ser31, Ser325, Thr336 and Thr366) on LKB1/STK11, the protein kinase mutated in Peutz-Jeghers cancer syndrome. Biochem. J. 362, 481-490.
    • (2002) Biochem. J , vol.362 , pp. 481-490
    • Sapkota, G.P.1    Boudeau, J.2    Deak, M.3    Kieloch, A.4    Morrice, N.5    Alessi, D.R.6
  • 42
    • 0032925146 scopus 로고    scopus 로고
    • The catalytic subunit of cAMP-dependent protein kinase: Prototype for an extended network of communication
    • Smith, C. M., Radzio-Andzelm, E., Madhusudan, Akamine, P., and Taylor, S. S. (1999) The catalytic subunit of cAMP-dependent protein kinase: prototype for an extended network of communication. Prog. Biophys. Mol. Biol. 71, 313-341.
    • (1999) Prog. Biophys. Mol. Biol , vol.71 , pp. 313-341
    • Smith, C.M.1    Andzelm, R.2    Madhusudan, E.3    Akamine, P.4    Taylor, S.S.5
  • 43
    • 0035375261 scopus 로고    scopus 로고
    • Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth
    • Sapkota, G. P., Kieloch, A., Lizcano, J. M., Lain, S., Arthur, J. S., Williams, M. R., Morrice, N., Deak, M., and Alessi, D. R. (2001) Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth. J. Biol. Chem. 276, 19469-19482.
    • (2001) J. Biol. Chem , vol.276 , pp. 19469-19482
    • Sapkota, G.P.1    Kieloch, A.2    Lizcano, J.M.3    Lain, S.4    Arthur, J.S.5    Williams, M.R.6    Morrice, N.7    Deak, M.8    Alessi, D.R.9
  • 45
    • 0141753981 scopus 로고    scopus 로고
    • MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm
    • Boudeau, J., Baas, A. F., Deak, M., Morrice, N. A., Kieloch, A., Schutkowski, M., Prescott, A. R., Clevers, H. C., and Alessi, D. R. (2003) MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm. EMBO. J. 22, 5102-5114.
    • (2003) EMBO. J , vol.22 , pp. 5102-5114
    • Boudeau, J.1    Baas, A.F.2    Deak, M.3    Morrice, N.A.4    Kieloch, A.5    Schutkowski, M.6    Prescott, A.R.7    Clevers, H.C.8    Alessi, D.R.9
  • 47
    • 17144474893 scopus 로고    scopus 로고
    • Activity of LKB1 and AMPK-related kinases in skeletal muscle: Effects of contraction, phenformin, and AICAR
    • Sakamoto, K., Goransson, O., Hardie, D. G., and Alessi, D. R. (2004) Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR. Am. J. Physiol. Endocrinol. Metab. 287, E310-E317.
    • (2004) Am. J. Physiol. Endocrinol. Metab , vol.287
    • Sakamoto, K.1    Goransson, O.2    Hardie, D.G.3    Alessi, D.R.4
  • 48
    • 0028845251 scopus 로고
    • 5′-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
    • Hawley, S. A., Selbert, M. A., Goldstein, E. G., Edelman, A. M., Carling, D., and Hardie, D. G. (1995) 5′-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J. Biol. Chem. 270, 27186-27191.
    • (1995) J. Biol. Chem , vol.270 , pp. 27186-27191
    • Hawley, S.A.1    Selbert, M.A.2    Goldstein, E.G.3    Edelman, A.M.4    Carling, D.5    Hardie, D.G.6
  • 49
    • 20044370885 scopus 로고    scopus 로고
    • Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
    • Sakamoto, K., McCarthy, A., Smith, D., Green, K. A., Grahame, H. D., Ashworth, A., and Alessi, D. R. (2005) Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction. EMBO. J 24, 1810-1820.
    • (2005) EMBO. J , vol.24 , pp. 1810-1820
    • Sakamoto, K.1    McCarthy, A.2    Smith, D.3    Green, K.A.4    Grahame, H.D.5    Ashworth, A.6    Alessi, D.R.7
  • 50
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • Sanders, M. J., Grondin, P. O., Hegarty, B. D., Snowden, M. A., and Carling, D. (2007) Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade. Biochem. J. 403, 139-148.
    • (2007) Biochem. J , vol.403 , pp. 139-148
    • Sanders, M.J.1    Grondin, P.O.2    Hegarty, B.D.3    Snowden, M.A.4    Carling, D.5
  • 51
    • 0038583957 scopus 로고    scopus 로고
    • Yeast Pak1 kinase associates with and activates Snf1
    • Nath, N., McCartney, R. R., and Schmidt, M. C. (2003) Yeast Pak1 kinase associates with and activates Snf1. Mol. Cell. Biol. 23, 3909-3917.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 3909-3917
    • Nath, N.1    McCartney, R.R.2    Schmidt, M.C.3
  • 53
    • 0029915228 scopus 로고    scopus 로고
    • Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence
    • Edelman, A. M., Mitchelhill, K. I., Selbert, M. A., Anderson, K. A., Hook, S. S., Stapleton, D., Goldstein, E. G., Means, A. R., and Kemp, B. E. (1996) Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence. J. Biol. Chem. 271, 10806-10810.
    • (1996) J. Biol. Chem , vol.271 , pp. 10806-10810
    • Edelman, A.M.1    Mitchelhill, K.I.2    Selbert, M.A.3    Anderson, K.A.4    Hook, S.S.5    Stapleton, D.6    Goldstein, E.G.7    Means, A.R.8    Kemp, B.E.9
  • 54
    • 0033610891 scopus 로고    scopus 로고
    • Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin- dependent protein kinase kinase beta
    • Anderson, K. A., Means, R. L., Huang, Q. H., Kemp, B. E., Goldstein, E. G., Selbert, M. A., Edelman, A. M., Fremeau, R. T., and Means, A. R. (1998) Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin- dependent protein kinase kinase beta. J. Biol. Chem. 273, 31880-31889.
    • (1998) J. Biol. Chem , vol.273 , pp. 31880-31889
    • Anderson, K.A.1    Means, R.L.2    Huang, Q.H.3    Kemp, B.E.4    Goldstein, E.G.5    Selbert, M.A.6    Edelman, A.M.7    Fremeau, R.T.8    Means, A.R.9
  • 55
    • 0031178322 scopus 로고    scopus 로고
    • Molecular cloning of Ca2+/calmodulin-dependent protein kinase kinase beta
    • Kitani, T., Okuno, S., and Fujisawa, H. (1997) Molecular cloning of Ca2+/calmodulin-dependent protein kinase kinase beta. J. Biochem. (Tokyo). 122, 243-250.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 243-250
    • Kitani, T.1    Okuno, S.2    Fujisawa, H.3
  • 56
    • 0032032673 scopus 로고    scopus 로고
    • Localization of the mRNAs for two isoforms of Ca2+/calmodulin- dependent protein kinase kinases in the adult rat brain
    • Sakagami, H., Saito, S., Kitani, T., Okuno, S., Fujisawa, H., and Kondo, H. (1998) Localization of the mRNAs for two isoforms of Ca2+/calmodulin- dependent protein kinase kinases in the adult rat brain. Brain. Res. Mol. Brain. Res. 54, 311-315.
    • (1998) Brain. Res. Mol. Brain. Res , vol.54 , pp. 311-315
    • Sakagami, H.1    Saito, S.2    Kitani, T.3    Okuno, S.4    Fujisawa, H.5    Kondo, H.6
  • 57
    • 29144514756 scopus 로고    scopus 로고
    • Prominent expression and activity-dependent nuclear translocation of Ca2+/calmodulin- dependent protein kinase Idelta in hippocampal neurons
    • Sakagami, H., Kamata, A., Nishimura, H., Kasahara, J., Owada, Y., Takeuchi, Y., Watanabe, M., Fukunaga, K., and Kondo, H. (2005) Prominent expression and activity-dependent nuclear translocation of Ca2+/calmodulin- dependent protein kinase Idelta in hippocampal neurons. Eur. J. Neurosci. 22, 2697-2707.
    • (2005) Eur. J. Neurosci , vol.22 , pp. 2697-2707
    • Sakagami, H.1    Kamata, A.2    Nishimura, H.3    Kasahara, J.4    Owada, Y.5    Takeuchi, Y.6    Watanabe, M.7    Fukunaga, K.8    Kondo, H.9
  • 58
    • 0028978850 scopus 로고
    • Characterization of a Ca2+/calmodulin-dependent protein kinase cascade. Molecular cloning and expression of calcium/calmodulin-dependent protein kinase kinase
    • Tokumitsu, H., Enslen, H., and Soderling, T. R. (1995) Characterization of a Ca2+/calmodulin-dependent protein kinase cascade. Molecular cloning and expression of calcium/calmodulin-dependent protein kinase kinase. J. Biol. Chem. 270, 19320-19324.
    • (1995) J. Biol. Chem , vol.270 , pp. 19320-19324
    • Tokumitsu, H.1    Enslen, H.2    Soderling, T.R.3
  • 59
    • 0029863222 scopus 로고    scopus 로고
    • Requirements for calcium and calmodulin in the calmodulin kinase activation cascade
    • Tokumitsu, H. and Soderling, T. R. (1996) Requirements for calcium and calmodulin in the calmodulin kinase activation cascade. J. Biol. Chem. 271, 5617-5622.
    • (1996) J. Biol. Chem , vol.271 , pp. 5617-5622
    • Tokumitsu, H.1    Soderling, T.R.2
  • 60
    • 0035923396 scopus 로고    scopus 로고
    • Differential regulatory mechanism of Ca2+/calmodulin-dependent protein kinase kinase isoforms
    • Tokumitsu, H., Iwabu, M., Ishikawa, Y., and Kobayashi, R. (2001) Differential regulatory mechanism of Ca2+/calmodulin-dependent protein kinase kinase isoforms. Biochemistry. 40, 13925-13932.
    • (2001) Biochemistry , vol.40 , pp. 13925-13932
    • Tokumitsu, H.1    Iwabu, M.2    Ishikawa, Y.3    Kobayashi, R.4
  • 61
    • 34248188085 scopus 로고    scopus 로고
    • CaMKK{alpha} Regulates Skeletal Muscle Glucose Uptake Independent of AMPK and Akt Activation
    • Witczak, C. A., Fujii, N., Hirshman, M. F., and Goodyear, L. J. (2007) CaMKK{alpha} Regulates Skeletal Muscle Glucose Uptake Independent of AMPK and Akt Activation. Diabetes. 56, 1403-1409.
    • (2007) Diabetes , vol.56 , pp. 1403-1409
    • Witczak, C.A.1    Fujii, N.2    Hirshman, M.F.3    Goodyear, L.J.4
  • 63
    • 40949146900 scopus 로고    scopus 로고
    • Normal hypertrophy accompanied by phosphoryation and activation of AMP-activated protein kinase alpha1 following overload in LKB1 knockout mice
    • McGee, S. L., Mustard, K. J., Hardie, D. G., and Baar, K. (2008) Normal hypertrophy accompanied by phosphoryation and activation of AMP-activated protein kinase alpha1 following overload in LKB1 knockout mice. J. Physiol. 586, 1731-1741.
    • (2008) J. Physiol , vol.586 , pp. 1731-1741
    • McGee, S.L.1    Mustard, K.J.2    Hardie, D.G.3    Baar, K.4
  • 64
    • 34248199965 scopus 로고    scopus 로고
    • Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase
    • Wu, Y., Song, P., Xu, J., Zhang, M., and Zou, M. H. (2007) Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase. J. Biol. Chem. 282, 9777-9788.
    • (2007) J. Biol. Chem , vol.282 , pp. 9777-9788
    • Wu, Y.1    Song, P.2    Xu, J.3    Zhang, M.4    Zou, M.H.5
  • 65
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • Momcilovic, M., Hong, S. P., and Carlson, M. (2006) Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro. J Biol. Chem. 281, 25336-25343.
    • (2006) J Biol. Chem , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 69
    • 1542314841 scopus 로고    scopus 로고
    • TAB3, a new binding partner of the protein kinase TAK1
    • Cheung, P. C., Nebreda, A. R., and Cohen, P. (2004) TAB3, a new binding partner of the protein kinase TAK1. Biochem. J. 378, 27-34.
    • (2004) Biochem. J , vol.378 , pp. 27-34
    • Cheung, P.C.1    Nebreda, A.R.2    Cohen, P.3
  • 70
    • 0034629146 scopus 로고    scopus 로고
    • TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop
    • Kishimoto, K., Matsumoto, K., and Ninomiya-Tsuji, J. (2000) TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop. J. Biol. Chem. 275, 7359-7364.
    • (2000) J. Biol. Chem , vol.275 , pp. 7359-7364
    • Kishimoto, K.1    Matsumoto, K.2    Ninomiya-Tsuji, J.3
  • 71
    • 0035968214 scopus 로고    scopus 로고
    • An evolutionarily conserved motif in the TAB1 C-terminal region is necessary for interaction with and activation of TAK1 MAPKKK
    • Ono, K., Ohtomo, T., Sato, S., Sugamata, Y., Suzuki, M., Hisamoto, N., Ninomiya-Tsuji, J., Tsuchiya, M., and Matsumoto, K. (2001) An evolutionarily conserved motif in the TAB1 C-terminal region is necessary for interaction with and activation of TAK1 MAPKKK. J. Biol. Chem. 276, 24396-24400.
    • (2001) J. Biol. Chem , vol.276 , pp. 24396-24400
    • Ono, K.1    Ohtomo, T.2    Sato, S.3    Sugamata, Y.4    Suzuki, M.5    Hisamoto, N.6    Ninomiya-Tsuji, J.7    Tsuchiya, M.8    Matsumoto, K.9
  • 72
    • 0034595826 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1
    • Sakurai, H., Miyoshi, H., Mizukami, J., and Sugita, T. (2000) Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1. FEBS Lett. 474, 141-145.
    • (2000) FEBS Lett , vol.474 , pp. 141-145
    • Sakurai, H.1    Miyoshi, H.2    Mizukami, J.3    Sugita, T.4
  • 74
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu, G., Kishida, S., Hiyama, A., Yamaguchi, K., Shibuya, H., Irie, K., Ninomiya-Tsuji, J., and Matsumoto, K. (2000) TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol. Cell. 5, 649-658.
    • (2000) Mol. Cell , vol.5 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6    Ninomiya-Tsuji, J.7    Matsumoto, K.8
  • 75
    • 36849092777 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha augments matrix metalloproteinase-9 production in skeletal muscle cells through the activation of transforming growth factor-beta-activated kinase 1 (TAK1)-dependent signaling pathway
    • Srivastava, A. K., Qin, X., Wedhas, N., Arnush, M., Linkhart, T. A., Chadwick, R. B., and Kumar, A. (2007) Tumor necrosis factor-alpha augments matrix metalloproteinase-9 production in skeletal muscle cells through the activation of transforming growth factor-beta-activated kinase 1 (TAK1)-dependent signaling pathway. J. Biol. Chem. 282, 35113-35124.
    • (2007) J. Biol. Chem , vol.282 , pp. 35113-35124
    • Srivastava, A.K.1    Qin, X.2    Wedhas, N.3    Arnush, M.4    Linkhart, T.A.5    Chadwick, R.B.6    Kumar, A.7
  • 77
    • 10744230942 scopus 로고    scopus 로고
    • AICA riboside both activates AMP-activated protein kinase and competes with adenosine for the nucleoside transporter in the CA1 region of the rat hippocampus
    • Gadalla, A. E., Pearson, T., Currie, A. J., Dale, N., Hawley, S. A., Sheehan, M., Hirst, W., Michel, A. D., Randall, A., Hardie, D. G., and Frenguelli, B. G. (2004) AICA riboside both activates AMP-activated protein kinase and competes with adenosine for the nucleoside transporter in the CA1 region of the rat hippocampus. J. Neurochem. 88, 1272-1282.
    • (2004) J. Neurochem , vol.88 , pp. 1272-1282
    • Gadalla, A.E.1    Pearson, T.2    Currie, A.J.3    Dale, N.4    Hawley, S.A.5    Sheehan, M.6    Hirst, W.7    Michel, A.D.8    Randall, A.9    Hardie, D.G.10    Frenguelli, B.G.11
  • 78
    • 0021824214 scopus 로고
    • 5-Amino-4-imidazolecarboxamide riboside (Z-riboside) metabolism in eukaryotic cells
    • Sabina, R. L., Patterson, D., and Holmes, E. W. (1985) 5-Amino-4-imidazolecarboxamide riboside (Z-riboside) metabolism in eukaryotic cells. J. Biol. Chem. 260, 6107-6114.
    • (1985) J. Biol. Chem , vol.260 , pp. 6107-6114
    • Sabina, R.L.1    Patterson, D.2    Holmes, E.W.3
  • 79
    • 0034070567 scopus 로고    scopus 로고
    • Metabolic stress and altered glucose transport: Activation of AMP-activated protein kinase as a unifying coupling mechanism
    • Hayashi, T., Hirshman, M. F., Fujii, N., Habinowski, S. A., Witters, L. A., and Goodyear, L. J. (2000) Metabolic stress and altered glucose transport: activation of AMP-activated protein kinase as a unifying coupling mechanism. Diabetes. 49, 527-531.
    • (2000) Diabetes , vol.49 , pp. 527-531
    • Hayashi, T.1    Hirshman, M.F.2    Fujii, N.3    Habinowski, S.A.4    Witters, L.A.5    Goodyear, L.J.6
  • 80
    • 0031849916 scopus 로고    scopus 로고
    • Evidence for 5′ AMP-activated protein kinase mediation of the effect of muscle contraction on glucose transport
    • Hayashi, T., Hirshman, M. F., Kurth, E. J., Winder, W. W., and Goodyear, L. J. (1998) Evidence for 5′ AMP-activated protein kinase mediation of the effect of muscle contraction on glucose transport. Diabetes. 47, 1369-1373.
    • (1998) Diabetes , vol.47 , pp. 1369-1373
    • Hayashi, T.1    Hirshman, M.F.2    Kurth, E.J.3    Winder, W.W.4    Goodyear, L.J.5
  • 81
    • 28244466267 scopus 로고    scopus 로고
    • AMP-activated Protein Kinase {alpha}2 Activity Is Not Essential for Contraction-and Hyperosmolarity-induced Glucose Transport in Skeletal Muscle
    • Fujii, N., Hirshman, M. F., Kane, E. M., Ho, R. C., Peter, L. E., Seifert, M. M., and Goodyear, L. J. (2005) AMP-activated Protein Kinase {alpha}2 Activity Is Not Essential for Contraction-and Hyperosmolarity-induced Glucose Transport in Skeletal Muscle. J. Biol. Chem. 280, 39033-39041.
    • (2005) J. Biol. Chem , vol.280 , pp. 39033-39041
    • Fujii, N.1    Hirshman, M.F.2    Kane, E.M.3    Ho, R.C.4    Peter, L.E.5    Seifert, M.M.6    Goodyear, L.J.7
  • 82
    • 0037383091 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide 1-beta -D-ribofuranoside (AICAR) stimulates myocardial glycogenolysis by allosteric mechanisms
    • Longnus, S. L., Wambolt, R. B., Parsons, H. L., Brownsey, R. W., and Allard, M. F. (2003) 5-Aminoimidazole-4-carboxamide 1-beta -D-ribofuranoside (AICAR) stimulates myocardial glycogenolysis by allosteric mechanisms. Am. J. Physiol. Regul. Integr. Comp. Physiol. 284, R936-R944.
    • (2003) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.284
    • Longnus, S.L.1    Wambolt, R.B.2    Parsons, H.L.3    Brownsey, R.W.4    Allard, M.F.5
  • 84
    • 0034070567 scopus 로고    scopus 로고
    • Metabolic stress and altered glucose transport: Activation of AMP-activated protein kinase as a unifying coupling mechanism
    • Hayashi, T., Hirshman, M. F., Fujii, N., Habinowski, S. A., Witters, L. A., and Goodyear, L. J. (2000) Metabolic stress and altered glucose transport: Activation of AMP-activated protein kinase as a unifying coupling mechanism. Diabetes 49, 527-531.
    • (2000) Diabetes , vol.49 , pp. 527-531
    • Hayashi, T.1    Hirshman, M.F.2    Fujii, N.3    Habinowski, S.A.4    Witters, L.A.5    Goodyear, L.J.6
  • 88
    • 0034659785 scopus 로고    scopus 로고
    • Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain
    • Owen, M. R., Doran, E., and Halestrap, A. P. (2000) Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain. Biochem. J. 348 Pt 3, 607-614.
    • (2000) Biochem. J , vol.348 , Issue.PART 3 , pp. 607-614
    • Owen, M.R.1    Doran, E.2    Halestrap, A.P.3
  • 89
    • 0034614420 scopus 로고    scopus 로고
    • Dimethylbiguanide inhibits cell respiration via an indirect effect targeted on the respiratory chain complex I
    • El Mir, M. Y., Nogueira, V., Fontaine, E., Averet, N., Rigoulet, M., and Leverve, X. (2000) Dimethylbiguanide inhibits cell respiration via an indirect effect targeted on the respiratory chain complex I. J. Biol. Chem. 275, 223-228.
    • (2000) J. Biol. Chem , vol.275 , pp. 223-228
    • El Mir, M.Y.1    Nogueira, V.2    Fontaine, E.3    Averet, N.4    Rigoulet, M.5    Leverve, X.6
  • 90
    • 0036324142 scopus 로고    scopus 로고
    • The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • Hawley, S. A., Gadalla, A. E., Olsen, G. S., and Hardie, D. G. (2002) The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism. Diabetes 51, 2420-2425.
    • (2002) Diabetes , vol.51 , pp. 2420-2425
    • Hawley, S.A.1    Gadalla, A.E.2    Olsen, G.S.3    Hardie, D.G.4
  • 91
    • 0037067666 scopus 로고    scopus 로고
    • The Anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • Fryer, L. G., Parbu-Patel, A., and Carling, D. (2002) The Anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways. J. Biol. Chem. 277, 25226-25232.
    • (2002) J. Biol. Chem , vol.277 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 92
    • 33746434574 scopus 로고    scopus 로고
    • Total cellular calcium and magnesium content of cultured human peripheral blood mononuclear cells following exposure to antidiabetic drugs
    • Alon, I., Berman, S., Shteinshnaider, M., Efrati, S., Gorelik, O., Almoznino-Sarafian, D., Weissgarten, J., and Cohen, N. (2006) Total cellular calcium and magnesium content of cultured human peripheral blood mononuclear cells following exposure to antidiabetic drugs. Acta Diabetol. 43, 46-51.
    • (2006) Acta Diabetol , vol.43 , pp. 46-51
    • Alon, I.1    Berman, S.2    Shteinshnaider, M.3    Efrati, S.4    Gorelik, O.5    Almoznino-Sarafian, D.6    Weissgarten, J.7    Cohen, N.8
  • 93
    • 35048846963 scopus 로고    scopus 로고
    • Comparison of the antidiabetic effects of brain-derived neurotrophic factor and thiazolidinediones in obese diabetic mice
    • Yamanaka, M., Itakura, Y., Tsuchida, A., Nakagawa, T., Noguchi, H., and Taiji, M. (2007) Comparison of the antidiabetic effects of brain-derived neurotrophic factor and thiazolidinediones in obese diabetic mice. Diabetes Obes. Metab. 9, 879-888.
    • (2007) Diabetes Obes. Metab , vol.9 , pp. 879-888
    • Yamanaka, M.1    Itakura, Y.2    Tsuchida, A.3    Nakagawa, T.4    Noguchi, H.5    Taiji, M.6
  • 94
    • 0033123466 scopus 로고    scopus 로고
    • Rosiglitazone monotherapy improves glycaemic control in patients with type 2 diabetes: A twelve-week, randomized, placebo-controlled study
    • Patel, J., Anderson, R. J., and Rappaport, E. B. (1999) Rosiglitazone monotherapy improves glycaemic control in patients with type 2 diabetes: a twelve-week, randomized, placebo-controlled study. Diabetes Obes. Metab. 1, 165-172.
    • (1999) Diabetes Obes. Metab , vol.1 , pp. 165-172
    • Patel, J.1    Anderson, R.J.2    Rappaport, E.B.3
  • 97
    • 0037032414 scopus 로고    scopus 로고
    • Protein kinase inhibitors block the stimulation of the AMP-activated protein kinase by 5-amino-4-imidazolecarboxamide riboside
    • Fryer, L. G., Parbu-Patel, A., and Carling, D. (2002) Protein kinase inhibitors block the stimulation of the AMP-activated protein kinase by 5-amino-4-imidazolecarboxamide riboside. FEBS. Lett. 531, 189-192.
    • (2002) FEBS. Lett , vol.531 , pp. 189-192
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 102
    • 57349172504 scopus 로고    scopus 로고
    • Murphy, R. A. (1998) Muscle. 4, 269-316.
    • Murphy, R. A. (1998) Muscle. 4, 269-316.
  • 104
    • 0035891533 scopus 로고    scopus 로고
    • Detection of reactive oxygen and reactive nitrogen species in skeletal muscle
    • Murrant, C. L. and Reid, M. B. (2001) Detection of reactive oxygen and reactive nitrogen species in skeletal muscle. Microsc. Res. Tech. 55, 236-248.
    • (2001) Microsc. Res. Tech , vol.55 , pp. 236-248
    • Murrant, C.L.1    Reid, M.B.2
  • 105
    • 33746810466 scopus 로고    scopus 로고
    • Role of reactive oxygen species in contraction-mediated glucose transport in mouse skeletal muscle
    • Sandstrom, M. E., Zhang, S. J., Bruton, J., Silva, J. P., Reid, M. B., Westerblad, H., and Katz, A. (2006) Role of reactive oxygen species in contraction-mediated glucose transport in mouse skeletal muscle. J. Physiol. 575, 251-262.
    • (2006) J. Physiol , vol.575 , pp. 251-262
    • Sandstrom, M.E.1    Zhang, S.J.2    Bruton, J.3    Silva, J.P.4    Reid, M.B.5    Westerblad, H.6    Katz, A.7
  • 107
    • 84925549112 scopus 로고    scopus 로고
    • The paradigm of IL-6: From basic science to medicine. Arthritis. Res. 4 Suppl. 3:S233-42. Epub; 2002
    • May 9
    • Naka, T., Nishimoto, N., and Kishimoto, T. (2002) The paradigm of IL-6: from basic science to medicine. Arthritis. Res. 4 Suppl. 3:S233-42. Epub; 2002 May 9., S233-S242.
    • (2002)
    • Naka, T.1    Nishimoto, N.2    Kishimoto, T.3
  • 108
    • 0035651023 scopus 로고    scopus 로고
    • Transcriptional activation of the IL-6 gene in human contracting skeletal muscle: Influence of muscle glycogen content
    • Keller, C., Steensberg, A., Pilegaard, H., Osada, T., Saltin, B., Pedersen, B. K., and Neufer, P. D. (2001) Transcriptional activation of the IL-6 gene in human contracting skeletal muscle: influence of muscle glycogen content. FASEB J. 15, 2748-2750.
    • (2001) FASEB J , vol.15 , pp. 2748-2750
    • Keller, C.1    Steensberg, A.2    Pilegaard, H.3    Osada, T.4    Saltin, B.5    Pedersen, B.K.6    Neufer, P.D.7
  • 109
    • 0642364997 scopus 로고    scopus 로고
    • Immunohistochemical detection of interleukin-6 in human skeletal muscle fibers following exercise
    • Penkowa, M., Keller, C., Keller, P., Jauffred, S., and Pedersen, B. K. (2003) Immunohistochemical detection of interleukin-6 in human skeletal muscle fibers following exercise. FASEB J. 17, 2166-2168.
    • (2003) FASEB J , vol.17 , pp. 2166-2168
    • Penkowa, M.1    Keller, C.2    Keller, P.3    Jauffred, S.4    Pedersen, B.K.5
  • 112
    • 0037404462 scopus 로고    scopus 로고
    • Changes in [Ca2+]i induced by several glucose transport-enhancing stimuli in rat epitrochlearis muscle
    • Terada, S., Muraoka, I., and Tabata, I. (2003) Changes in [Ca2+]i induced by several glucose transport-enhancing stimuli in rat epitrochlearis muscle. J. Appl. Physiol. 94, 1813-1820.
    • (2003) J. Appl. Physiol , vol.94 , pp. 1813-1820
    • Terada, S.1    Muraoka, I.2    Tabata, I.3
  • 113
    • 0031978984 scopus 로고    scopus 로고
    • Exercise, glucose transport, and insulin sensitivity
    • Goodyear, L. J. and Kahn, B. B. (1998) Exercise, glucose transport, and insulin sensitivity. Annu. Rev. Med. 49:235-61, 235-261.
    • (1998) Annu. Rev. Med , vol.49 , Issue.235-261 , pp. 235-261
    • Goodyear, L.J.1    Kahn, B.B.2
  • 114
    • 0031417390 scopus 로고    scopus 로고
    • Exercise regulation of glucose transport in skeletal muscle
    • Hayashi, T., Wojtaszewski, J. F., and Goodyear, L. J. (1997) Exercise regulation of glucose transport in skeletal muscle. Am. J. Physiol. 273, E1039-51.
    • (1997) Am. J. Physiol , vol.273
    • Hayashi, T.1    Wojtaszewski, J.F.2    Goodyear, L.J.3
  • 115
    • 33947596679 scopus 로고    scopus 로고
    • The GLUT4 Glucose Transporter
    • Huang, S. and Czech, M. P. (2007) The GLUT4 Glucose Transporter. Cell Metab. 5, 237-252.
    • (2007) Cell Metab , vol.5 , pp. 237-252
    • Huang, S.1    Czech, M.P.2
  • 116
    • 0032697037 scopus 로고    scopus 로고
    • Exercise modulates postreceptor insulin signaling and glucose transport in muscle-specific insulin receptor knockout mice
    • Wojtaszewski, J. F., Higaki, Y., Hirshman, M. F., Michael, M. D., Dufresne, S. D., Kahn, C. R., and Goodyear, L. J. (1999) Exercise modulates postreceptor insulin signaling and glucose transport in muscle-specific insulin receptor knockout mice. J. Clin. Invest. 104, 1257-1264.
    • (1999) J. Clin. Invest , vol.104 , pp. 1257-1264
    • Wojtaszewski, J.F.1    Higaki, Y.2    Hirshman, M.F.3    Michael, M.D.4    Dufresne, S.D.5    Kahn, C.R.6    Goodyear, L.J.7
  • 117
    • 0028914037 scopus 로고
    • Wortmannin inhibits insulin-stimulated but not contraction-stimulated glucose transport activity in skeletal muscle
    • Lee, A. D., Hansen, P. A., and Holloszy, J. O. (1995) Wortmannin inhibits insulin-stimulated but not contraction-stimulated glucose transport activity in skeletal muscle. FEBS Lett. 361, 51-54.
    • (1995) FEBS Lett , vol.361 , pp. 51-54
    • Lee, A.D.1    Hansen, P.A.2    Holloszy, J.O.3
  • 118
    • 0028947991 scopus 로고
    • The effects of wortmannin on rat skeletal muscle. Dissociation of signaling pathways for insulin- and contraction-activated hexose transport
    • Yeh, J. I., Gulve, E. A., Rameh, L., and Birnbaum, M. J. (1995) The effects of wortmannin on rat skeletal muscle. Dissociation of signaling pathways for insulin- and contraction-activated hexose transport. J. Biol. Chem. 270, 2107-2111.
    • (1995) J. Biol. Chem , vol.270 , pp. 2107-2111
    • Yeh, J.I.1    Gulve, E.A.2    Rameh, L.3    Birnbaum, M.J.4
  • 119
    • 0345832116 scopus 로고    scopus 로고
    • Knockout of the alpha2 but not alpha1 5′-AMP-activated protein kinase isoform abolishes 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranosidebut not contraction-induced glucose uptake in skeletal muscle
    • Jorgensen, S. B., Viollet, B., Andreelli, F., Frosig, C., Birk, J. B., Schjerling, P., Vaulont, S., Richter, E. A., and Wojtaszewski, J. F. (2004) Knockout of the alpha2 but not alpha1 5′-AMP-activated protein kinase isoform abolishes 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranosidebut not contraction-induced glucose uptake in skeletal muscle. J. Biol. Chem. 279, 1070-1079.
    • (2004) J. Biol. Chem , vol.279 , pp. 1070-1079
    • Jorgensen, S.B.1    Viollet, B.2    Andreelli, F.3    Frosig, C.4    Birk, J.B.5    Schjerling, P.6    Vaulont, S.7    Richter, E.A.8    Wojtaszewski, J.F.9
  • 120
    • 0031425839 scopus 로고    scopus 로고
    • AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle
    • Merrill, G. F., Kurth, E. J., Hardie, D. G., and Winder, W. W. (1997) AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle. Am. J. Physiol. 273, E1107-E1112.
    • (1997) Am. J. Physiol , vol.273
    • Merrill, G.F.1    Kurth, E.J.2    Hardie, D.G.3    Winder, W.W.4
  • 122
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation
    • Sano, H., Kane, S., Sano, E., Miinea, C. P., Asara, J. M., Lane, W. S., Garner, C. W., and Lienhard, G. E. (2003) Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation. J. Biol. Chem. 278, 14599-14602.
    • (2003) J. Biol. Chem , vol.278 , pp. 14599-14602
    • Sano, H.1    Kane, S.2    Sano, E.3    Miinea, C.P.4    Asara, J.M.5    Lane, W.S.6    Garner, C.W.7    Lienhard, G.E.8
  • 125
    • 33845998942 scopus 로고    scopus 로고
    • AS160 regulates insulin- and contraction-stimulated glucose uptake in mouse skeletal muscle
    • Kramer, H. F., Witczak, C. A., Taylor, E. B., Fujii, N., Hirshman, M. F., and Goodyear, L. J. (2006) AS160 regulates insulin- and contraction-stimulated glucose uptake in mouse skeletal muscle. J. Biol. Chem. 281, 31478-85.
    • (2006) J. Biol. Chem , vol.281 , pp. 31478-31485
    • Kramer, H.F.1    Witczak, C.A.2    Taylor, E.B.3    Fujii, N.4    Hirshman, M.F.5    Goodyear, L.J.6
  • 127
    • 38749110036 scopus 로고    scopus 로고
    • Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators
    • Chen, S., Murphy, J., Toth, R., Campbell, D. G., Morrice, N. A., and MacKintosh, C. (2008) Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators. Biochem. J. 409, 449-459.
    • (2008) Biochem. J , vol.409 , pp. 449-459
    • Chen, S.1    Murphy, J.2    Toth, R.3    Campbell, D.G.4    Morrice, N.A.5    MacKintosh, C.6
  • 128
    • 0036079974 scopus 로고    scopus 로고
    • Glycogen and its metabolism
    • Roach, P. J. (2002) Glycogen and its metabolism. Curr. Mol. Med. 2, 101-120.
    • (2002) Curr. Mol. Med , vol.2 , pp. 101-120
    • Roach, P.J.1
  • 129
    • 2942702303 scopus 로고    scopus 로고
    • Regulation of glycogen synthase activity and phosphorylation by exercise
    • Nielsen, J. N. and Wojtaszewski, J. F. (2004) Regulation of glycogen synthase activity and phosphorylation by exercise. Proc. Nutr. Soc. 63, 233-237.
    • (2004) Proc. Nutr. Soc , vol.63 , pp. 233-237
    • Nielsen, J.N.1    Wojtaszewski, J.F.2
  • 130
    • 0024335432 scopus 로고
    • The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase
    • Carling, D. and Hardie, D. G. (1989) The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase. Biochim. Biophys. Acta. 1012, 81-86.
    • (1989) Biochim. Biophys. Acta , vol.1012 , pp. 81-86
    • Carling, D.1    Hardie, D.G.2
  • 133
    • 33748443452 scopus 로고    scopus 로고
    • Muscle-specific overexpression of wild type and R225Q mutant AMP-activated protein kinase gamma3-subunit differentially regulates glycogen accumulation
    • Yu, H., Hirshman, M. F., Fujii, N., Pomerleau, J. M., Peter, L. E., and Goodyear, L. J. (2006) Muscle-specific overexpression of wild type and R225Q mutant AMP-activated protein kinase gamma3-subunit differentially regulates glycogen accumulation. Am. J. Physiol. Endocrinol. Metab. 291, E557-E565.
    • (2006) Am. J. Physiol. Endocrinol. Metab , vol.291
    • Yu, H.1    Hirshman, M.F.2    Fujii, N.3    Pomerleau, J.M.4    Peter, L.E.5    Goodyear, L.J.6
  • 134
    • 0037326943 scopus 로고    scopus 로고
    • Selective suppression of AMP-activated protein kinase in skeletal muscle: Update on 'lazy mice'
    • Mu, J., Barton, E. R., and Birnbaum, M. J. (2003) Selective suppression of AMP-activated protein kinase in skeletal muscle: update on 'lazy mice'. Biochem. Soc. Trans. 31, 236-241.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 236-241
    • Mu, J.1    Barton, E.R.2    Birnbaum, M.J.3
  • 135
    • 0347716759 scopus 로고    scopus 로고
    • Rheb fills a GAP between TSC and TOR
    • Manning, B. D. and Cantley, L. C. (2003) Rheb fills a GAP between TSC and TOR. Trends. Biochem. Sci. 28, 573-576.
    • (2003) Trends. Biochem. Sci , vol.28 , pp. 573-576
    • Manning, B.D.1    Cantley, L.C.2
  • 137
    • 34548450714 scopus 로고    scopus 로고
    • AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes
    • Nakashima, K. and Yakabe, Y. (2007) AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes. Biosci. Biotechnol. Biochem. 71, 1650-1656.
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 1650-1656
    • Nakashima, K.1    Yakabe, Y.2
  • 138
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated Protein Kinase Suppresses Protein Synthesis in Rat Skeletal Muscle through Down-regulated Mammalian Target of Rapamycin (mTOR) Signaling
    • Bolster, D. R., Crozier, S. J., Kimball, S. R., and Jefferson, L. S. (2002) AMP-activated Protein Kinase Suppresses Protein Synthesis in Rat Skeletal Muscle through Down-regulated Mammalian Target of Rapamycin (mTOR) Signaling. J. Biol. Chem. 277, 23977-23980.
    • (2002) J. Biol. Chem , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 139
    • 0037143449 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis
    • Horman, S., Browne, G., Krause, U., Patel, J., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C., and Rider, M. (2002) Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. Curr. Biol. 12, 1419-1423.
    • (2002) Curr. Biol , vol.12 , pp. 1419-1423
    • Horman, S.1    Browne, G.2    Krause, U.3    Patel, J.4    Vertommen, D.5    Bertrand, L.6    Lavoinne, A.7    Hue, L.8    Proud, C.9    Rider, M.10
  • 140
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., Zhu, T., and Guan, K. L. (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 141
    • 33745206561 scopus 로고    scopus 로고
    • Impaired overload-induced muscle growth is associated with diminished translational signalling in aged rat fast-twitch skeletal muscle
    • Thomson, D. M. and Gordon, S. E. (2006) Impaired overload-induced muscle growth is associated with diminished translational signalling in aged rat fast-twitch skeletal muscle. J. Physiol. 574, 291-305.
    • (2006) J. Physiol , vol.574 , pp. 291-305
    • Thomson, D.M.1    Gordon, S.E.2
  • 142
    • 12344309493 scopus 로고    scopus 로고
    • Diminished overload-induced hypertrophy in aged fast-twitch skeletal muscle is associated with AMPK hyperphosphorylation
    • Thomson, D. M. and Gordon, S. E. (2005) Diminished overload-induced hypertrophy in aged fast-twitch skeletal muscle is associated with AMPK hyperphosphorylation. J. Appl. Physiol. 98, 557-564.
    • (2005) J. Appl. Physiol , vol.98 , pp. 557-564
    • Thomson, D.M.1    Gordon, S.E.2
  • 143
    • 38649089494 scopus 로고    scopus 로고
    • Calcium-dependent proteolytic system and muscle dysfunctions: A possible role of calpains in sarcopenia
    • Dargelos, E., Poussard, S., Brule, C., Daury, L., and Cottin, P. (2008) Calcium-dependent proteolytic system and muscle dysfunctions: a possible role of calpains in sarcopenia. Biochimie. 90, 359-368.
    • (2008) Biochimie , vol.90 , pp. 359-368
    • Dargelos, E.1    Poussard, S.2    Brule, C.3    Daury, L.4    Cottin, P.5
  • 145
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • Lecker, S. H., Goldberg, A. L., and Mitch, W. E. (2006) Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. J. Am. Soc. Nephrol. 17, 1807-1819.
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 146
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • Lecker, S. H., Solomon, V., Mitch, W. E., and Goldberg, A. L. (1999) Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J. Nutr. 129, 227S-237S.
    • (1999) J. Nutr , vol.129
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 147
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart, C. M. (1997) Targeting of substrates to the 26S proteasome. FASEB J. 11, 1055-1066.
    • (1997) FASEB J , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 148
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian, T. N., Kisselev, A. F., and Goldberg, A. L. (1997) Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272, 1791-1798.
    • (1997) J. Biol. Chem , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 149
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev, A. F., Akopian, T. N., and Goldberg, A. L. (1998) Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biol. Chem. 273, 1982-1989.
    • (1998) J. Biol. Chem , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 150
    • 0020479562 scopus 로고
    • The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis
    • Haas, A. L. and Rose, I. A. (1982) The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J. Biol. Chem. 257, 10329-10337.
    • (1982) J. Biol. Chem , vol.257 , pp. 10329-10337
    • Haas, A.L.1    Rose, I.A.2
  • 151
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman, M. H., Rubin, D. M., Fried, V. A., and Finley, D. (1998) The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell Biol. 18, 3149-3162.
    • (1998) Mol. Cell Biol , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 153
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., and Glass, D. J. (2004) The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell. 14, 395-403.
    • (2004) Mol. Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6    Gonzalez, M.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 154
    • 34249703500 scopus 로고    scopus 로고
    • AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells
    • Krawiec, B. J., Nystrom, G. J., Frost, R. A., Jefferson, L. S., and Lang, C. H. (2007) AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells. Am. J. Physiol. Endocrinol. Metab. 292, E1555-E1567.
    • (2007) Am. J. Physiol. Endocrinol. Metab , vol.292
    • Krawiec, B.J.1    Nystrom, G.J.2    Frost, R.A.3    Jefferson, L.S.4    Lang, C.H.5
  • 156
    • 0031769951 scopus 로고    scopus 로고
    • Influence of malonyl-CoA and palmitate concentration on rate of palmitate oxidation in rat muscle
    • Merrill, G. F., Kurth, E. J., Rasmussen, B. B., and Winder, W. W. (1998) Influence of malonyl-CoA and palmitate concentration on rate of palmitate oxidation in rat muscle. J. Appl. Physiol. 85, 1909-1914.
    • (1998) J. Appl. Physiol , vol.85 , pp. 1909-1914
    • Merrill, G.F.1    Kurth, E.J.2    Rasmussen, B.B.3    Winder, W.W.4
  • 157
    • 0033666193 scopus 로고    scopus 로고
    • Insulin stimulation of glucose uptake fails to decrease palmitate oxidation inmuscle if AMPK is activated
    • Winder, W. W. and Holmes, B. F. (2000) Insulin stimulation of glucose uptake fails to decrease palmitate oxidation inmuscle if AMPK is activated. J. Appl. Physiol. 89, 2430-2437.
    • (2000) J. Appl. Physiol , vol.89 , pp. 2430-2437
    • Winder, W.W.1    Holmes, B.F.2
  • 158
    • 0036430469 scopus 로고    scopus 로고
    • Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise
    • Wojtaszewski, J. F., Mourtzakis, M., Hillig, T., Saltin, B., and Pilegaard, H. (2002) Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise. Biochem. Biophys. Res. Commun. 298, 309-316.
    • (2002) Biochem. Biophys. Res. Commun , vol.298 , pp. 309-316
    • Wojtaszewski, J.F.1    Mourtzakis, M.2    Hillig, T.3    Saltin, B.4    Pilegaard, H.5
  • 161
    • 21044443195 scopus 로고    scopus 로고
    • AMP kinase activation with AICAR further increases fatty acid oxidation and blunts triacylglycerol hydrolysis in contracting rat soleus muscle
    • Smith, A. C., Bruce, C. R., and Dyck, D. J. (2005) AMP kinase activation with AICAR further increases fatty acid oxidation and blunts triacylglycerol hydrolysis in contracting rat soleus muscle. J. Physiol. 565, 547-553.
    • (2005) J. Physiol , vol.565 , pp. 547-553
    • Smith, A.C.1    Bruce, C.R.2    Dyck, D.J.3
  • 162
    • 33644846005 scopus 로고    scopus 로고
    • Skeletal muscle lipid metabolism in exercise and insulin resistance
    • Kiens, B. (2006) Skeletal muscle lipid metabolism in exercise and insulin resistance. Physiol. Rev. 86, 205-243.
    • (2006) Physiol. Rev , vol.86 , pp. 205-243
    • Kiens, B.1
  • 163
    • 0024516569 scopus 로고
    • Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism
    • Garton, A. J., Campbell, D. G., Carling, D., Hardie, D. G., Colbran, R. J., and Yeaman, S. J. (1989) Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism. Eur. J. Biochem. 179, 249-254.
    • (1989) Eur. J. Biochem , vol.179 , pp. 249-254
    • Garton, A.J.1    Campbell, D.G.2    Carling, D.3    Hardie, D.G.4    Colbran, R.J.5    Yeaman, S.J.6
  • 165
    • 1642356600 scopus 로고    scopus 로고
    • Contractions induce phosphorylation of the AMPK site Ser565 in hormone-sensitive lipase in muscle
    • Donsmark, M., Langfort, J., Holm, C., Ploug, T., and Galbo, H. (2004) Contractions induce phosphorylation of the AMPK site Ser565 in hormone-sensitive lipase in muscle. Biochem. Biophys. Res. Commun. 316, 867-871.
    • (2004) Biochem. Biophys. Res. Commun , vol.316 , pp. 867-871
    • Donsmark, M.1    Langfort, J.2    Holm, C.3    Ploug, T.4    Galbo, H.5


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