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AMP-activated Protein Kinase

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William W. Winder – One of the best experts on this subject based on the ideXlab platform.

  • Effects of 3-phosphoglycerate and other metabolites on the activation of AMP-activated Protein Kinase by LKB1-STRAD-MO25.
    American journal of physiology. Endocrinology and metabolism, 2006
    Co-Authors: William J. Ellingson, David G. Chesser, William W. Winder

    Abstract:

    Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated Protein Kinase (AMPK) by an upstream Kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protei…

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  • Evidence against regulation of AMP-activated Protein Kinase and LKB1/STRAD/MO25 activity by creatine phosphate
    American journal of physiology. Endocrinology and metabolism, 2005
    Co-Authors: Eric B. Taylor, Cori L. Compton, Jeremy D. Lamb, William J. Ellingson, David G. Chesser, William W. Winder

    Abstract:

    Muscle contraction results in phosphorylation and activation of the AMP-activated Protein Kinase (AMPK) by an AMPK Kinase (AMPKK). LKB1/STRAD/MO25 (LKB1) is the major AMPKK in skeletal muscle; howe…

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  • Regulation of muscle GLUT4 enhancer factor and myocyte enhancer factor 2 by AMP-activated Protein Kinase.
    American journal of physiology. Endocrinology and metabolism, 2005
    Co-Authors: Burton F. Holmes, William W. Winder, Ann Louise Olson, David P. Sparling, G. Lynis Dohm

    Abstract:

    As the primary glucose transporter in skeletal muscle, GLUT4 is an important factor in the regulation of blood glucose. We previously reported that stimulation of AMP-activated Protein Kinase (AMPK…

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David Carling – One of the best experts on this subject based on the ideXlab platform.

  • Beyond energy homeostasis: the expanding role of AMP-activated Protein Kinase in regulating metabolism
    Cell Metabolism, 2015
    Co-Authors: David Carling, Benoit Viollet

    Abstract:

    The recent exciting advances in ourunderstanding of the regulation of the energy sensor AMP-activated Protein Kinase (AMPK), together with renewed appreciation of its importance in maintaining cellular function, brought together leading scientists at a recent FASEB-sponsored meeting inSeptember 2014. Here, we report some of the highlights of this conference.

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  • Insulin Antagonizes Ischemia-induced Thr 172 Phosphorylation of AMP-activated Protein Kinase -Subunits
    , 2006
    Co-Authors: Sandrine Horman, Didier Vertommen, Dietbert Neumann, David Carling, Richard J. Heath, Angela Woods, Louis Hue, Mark H. Rider

    Abstract:

    Previous studies showed that insulin antagonizes AMP-activated Protein Kinase activation by ischemia and that Protein Kinase B might be implicated. Here we investigated whether the direct phosphorylation of AMP-activated Protein Kinase by Protein Kinase B might participate in this effect. Protein Kinase B phosphorylated recombinant bacterially expressed AMP-activated Protein Kinase heterotrimers at Ser 485 of the 1-subunits. In perfused rat hearts, phosphorylation of the 1/2 AMP-activated Protein Kinase subunits on Ser 485 /Ser 491 was increased by insulin and insulin pretreatment decreased the phosphorylation of the-subunits at Thr 172 in a subsequent ischemic episode. It is proposed that the effect of insulin to antagonize AMP-activated Protein Kinase activation involves a hierarchical mechanism whereby Ser 485 /Ser 491 phosphorylation by Protein Kinase B reduces subsequent phosphorylation of Thr 172 by

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  • Insulin antagonizes ischemia-induced Thr172 phosphorylation of AMP-activated Protein Kinase alpha-subunits in heart via hierarchical phosphorylation of Ser485/491.
    The Journal of biological chemistry, 2005
    Co-Authors: Sandrine Horman, Didier Vertommen, Dietbert Neumann, David Carling, Richard J. Heath, Angela Woods, Uwe Schlattner, Véronique Mouton, Theo Wallimann, Louis Hue

    Abstract:

    Previous studies showed that insulin antagonizes AMP-activated Protein Kinase activation by ischemia and that Protein Kinase B might be implicated. Here we investigated whether the direct phosphorylation of AMP-activated Protein Kinase by Protein Kinase B might participate in this effect. Protein Kinase B phosphorylated recombinant bacterially expressed AMP-activated Protein Kinase heterotrimers at Ser(485) of the alpha1-subunits. In perfused rat hearts, phosphorylation of the alpha1/alpha2 AMP-activated Protein Kinase subunits on Ser(485)/Ser(491) was increased by insulin and insulin pretreatment decreased the phosphorylation of the alpha-subunits at Thr(172) in a subsequent ischemic episode. It is proposed that the effect of insulin to antagonize AMP-activated Protein Kinase activation involves a hierarchical mechanism whereby Ser(485)/Ser(491) phosphorylation by Protein Kinase B reduces subsequent phosphorylation of Thr(172) by LKB1 and the resulting activation of AMP-activated Protein Kinase.

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Bruce E Kemp – One of the best experts on this subject based on the ideXlab platform.

  • Structure and function of AMP-activated Protein Kinase.
    Acta physiologica (Oxford England), 2009
    Co-Authors: Jonathan S. Oakhill, John W. Scott, Bruce E Kemp

    Abstract:

    AMP-activated Protein Kinase (AMPK) regulates metabolism in response to energy demand and supply. AMPK is activated in response to rises in intracellular AMP or calcium-mediated signalling and is responsible for phosphorylating a wide variety of substrates. Recent structural studies have revealed the architecture of the abc subunit interactions as well as the AMP binding pockets on the c subunit. The a catalytic domain (1–280) is autoinhibited by a C-terminal tail (313–335), which is proposed to interact with the small lobe of the catalytic domain by homology modelling with the MARK2 Protein structure. Two direct activating drugs have been reported for AMPK, the thienopyridone compound A769662 and PTI, which may activate by distinct mechanisms.

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  • Low salt concentrations activate AMP-activated Protein Kinase in mouse macula densa cells
    American journal of physiology. Renal physiology, 2009
    Co-Authors: Natasha Cook, Bruce E Kemp, Frosa Katsis, Scott A Fraser, Marina Katerelos, Kurt Gleich, Peter F Mount, Gregory R. Steinberg, Vicki Levidiotis, David A. Power

    Abstract:

    The energy-sensing Kinase AMP-activated Protein Kinase (AMPK) is associated with the sodium-potassium-chloride cotransporter NKCC2 in the kidney and phosphorylates it on a regulatory site in vitro….

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  • AMP-activated Protein Kinase–the fat controller of the energy railroad.
    Canadian journal of physiology and pharmacology, 2006
    Co-Authors: Gregory R. Steinberg, S. Lance Macaulay, Mark A. Febbraio, Bruce E Kemp

    Abstract:

    AMP-activated Protein Kinase plays an important role in the regulation of lipid metabolism in response to metabolic stress and energy demand. It is also under endocrine control. AMPK acts at multiple steps and has a central role controlling fatty acid, triglyceride, and cholesterol synthesis, as well as the oxidation of fatty acids through direct phosphorylation effects and the control of gene transcription. As such, it can be considered to be the fat controller of the energy railroad. It is thought that AMPK may be a major mediator of the health benefits of exercise in mitigating the development of obesity and age-onset diseases.

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