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4-Aminoimidazole

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Grahame D Hardie – One of the best experts on this subject based on the ideXlab platform.

  • activation of glut1 by metabolic and osmotic stress potential involvement of amp activated protein kinase ampk
    Journal of Cell Science, 2002
    Co-Authors: Kay Barnes, Jean C Ingram, Omar Porras, Felipe L Barros, Emma R Hudson, Lee G D Fryer, Fabienne Foufelle, David Carling, Grahame D Hardie, Stephen A Baldwin

    Abstract:

    In the rat liver epithelial cell line Clone 9, the V max for
    glucose uptake is actuely increased by inhibition of oxidative phosphorylation
    and by osmotic stress. By using a membrane-impermeant photoaffinity labelling
    reagent together with an isoform-specific antibody, we have, for the first
    time, provided direct evidence for the involvement of the GLUT1 glucose
    transporter isoform in this response. Transport stimulation was found to be
    associated with enhanced accessibility of GLUT1 to its substrate and with
    photolabelling of formerly `cryptic9 exofacial substrate binding sites in
    GLUT1 molecules. The total amount of cell surface GLUT1 remained constant. The
    precise mechanism for this binding site `unmasking9 is unclear but appears to
    involve AMP-activated protein kinase: in the current study, osmotic and
    metabolic stresses were found to result in activation of the α1 isoform
    of AMP-activated protein kinase, and transport stimulation could be mimicked
    both by 5-aminoimidazole-4-carboxamide ribonucleoside and by infection of
    cells with a recombinant adenovirus encoding constitutively active
    AMP-activated protein kinase. The effect of 5-aminoimidazole-4-carboxamide
    ribonucleoside, as for metabolic stress, was on the V max rather
    than on the K m for transport and did not affect the cell-surface
    concentration of GLUT1. The relevant downstream target(s) of AMP-activated
    protein kinase have not yet been identified, but stimulation of transport by
    inhibition of oxidative phosphorylation or by 5-aminoimidazole-4-carboxamide
    ribonucleoside was not prevented by either inhibitors of conventional and
    novel protein kinase C isoforms or inhibitors of nitric oxide synthase. These
    enzymes, which have been implicated in stress-regulated pathways in other cell
    types, are therefore unlikely to play a role in transport regulation by stress
    in Clone 9 cells.

  • effect of fiber type and nutritional state on aicar and contraction stimulated glucose transport in rat muscle
    American Journal of Physiology-endocrinology and Metabolism, 2002
    Co-Authors: Jacob Ihlemann, Grahame D Hardie, Ylva Hellsten, Hans P M M Lauritzen, H Galbo, Thorkil Ploug

    Abstract:

    AMP-activated protein kinase (AMPK) may mediate the stimulatory effect of contraction and 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) on glucose transport in skeletal muscle. In muscles w…

  • 5 aminoimidazole 4 carboxamide ribonucleoside
    FEBS Journal, 1995
    Co-Authors: Julia M. Corton, John G. Gillespie, Simon A. Hawley, Grahame D Hardie

    Abstract:

    The AMP-activated protein kinase (AMPK) is believed to protect cells against environmental stress (e.g. heat shock) by switching off biosynthetic pathways, the key signal being elevation of AMP. Identification of novel targets for the kinase cascade would be facilitated by development of a specific agent for activating the kinase in intact cells. Incubation of rat hepatocytes with 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) results in accumulation of the monophosphorylated derivative (5-aminoimidaz-ole-4-carboxamide ribonucleoside; ZMP) within the cell. ZMP mimics both activating effects of AMP on AMPK, i.e. direct allosteric activation and promotion of phosphorylation by AMPK kinase. Unlike existing methods for activating AMPK in intact cells (e.g. fructose, heat shock), AICAR does not perturb the cellular contents of ATP, ADP or AMP. Incubation of hepatocytes with AICAR activates AMPK due to increased phosphorylation, causes phosphorylation and inactivation of a known target for AMPK (3-hydroxy-3-methylglutaryl-CoA reductase), and almost total cessation of two of the known target pathways, i.e. fatty acid and sterol synthesis. Incubation of isolated adipocytes with AICAR antagonizes isoprenaline-induced lipolysis. This provides direct evidence that the inhibition by AMPK of activation of hormone-sensitive lipase by cyclic-AMP-dependent protein kinase, previously demonstrated in cell-free assays, also operates in intact cells. AICAR should be a useful tool for identifying new target pathways and processes regulated by the protein kinase cascade.

Julia M. Corton – One of the best experts on this subject based on the ideXlab platform.

  • 5 aminoimidazole 4 carboxamide ribonucleoside a specific method for activating amp activated protein kinase in intact cells
    FEBS Journal, 1995
    Co-Authors: Julia M. Corton, John G. Gillespie, Simon A. Hawley, D G Hardie

    Abstract:

    : The AMP-activated protein kinase (AMPK) is believed to protect cells against environmental stress (e.g. heat shock) by switching off biosynthetic pathways, the key signal being elevation of AMP. Identification of novel targets for the kinase cascade would be facilitated by development of a specific agent for activating the kinase in intact cells. Incubation of rat hepatocytes with 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) results in accumulation of the monophosphorylated derivative (5-aminoimidazole-4-carboxamide ribonucleoside; ZMP) within the cell. ZMP mimics both activating effects of AMP on AMPK, i.e. direct allosteric activation and promotion of phosphorylation by AMPK kinase. Unlike existing methods for activating AMPK in intact cells (e.g. fructose, heat shock), AICAR does not perturb the cellular contents of ATP, ADP or AMP. Incubation of hepatocytes with AICAR activates AMPK due to increased phosphorylation, causes phosphorylation and inactivation of a known target for AMPK (3-hydroxy-3-methylglutaryl-CoA reductase), and almost total cessation of two of the known target pathways, i.e. fatty acid and sterol synthesis. Incubation of isolated adipocytes with AICAR antagonizes isoprenaline-induced lipolysis. This provides direct evidence that the inhibition by AMPK of activation of hormone-sensitive lipase by cyclic-AMP-dependent protein kinase, previously demonstrated in cell-free assays, also operates in intact cells. AICAR should be a useful tool for identifying new target pathways and processes regulated by the protein kinase cascade.

  • 5 aminoimidazole 4 carboxamide ribonucleoside
    FEBS Journal, 1995
    Co-Authors: Julia M. Corton, John G. Gillespie, Simon A. Hawley, Grahame D Hardie

    Abstract:

    The AMP-activated protein kinase (AMPK) is believed to protect cells against environmental stress (e.g. heat shock) by switching off biosynthetic pathways, the key signal being elevation of AMP. Identification of novel targets for the kinase cascade would be facilitated by development of a specific agent for activating the kinase in intact cells. Incubation of rat hepatocytes with 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) results in accumulation of the monophosphorylated derivative (5-aminoimidaz-ole-4-carboxamide ribonucleoside; ZMP) within the cell. ZMP mimics both activating effects of AMP on AMPK, i.e. direct allosteric activation and promotion of phosphorylation by AMPK kinase. Unlike existing methods for activating AMPK in intact cells (e.g. fructose, heat shock), AICAR does not perturb the cellular contents of ATP, ADP or AMP. Incubation of hepatocytes with AICAR activates AMPK due to increased phosphorylation, causes phosphorylation and inactivation of a known target for AMPK (3-hydroxy-3-methylglutaryl-CoA reductase), and almost total cessation of two of the known target pathways, i.e. fatty acid and sterol synthesis. Incubation of isolated adipocytes with AICAR antagonizes isoprenaline-induced lipolysis. This provides direct evidence that the inhibition by AMPK of activation of hormone-sensitive lipase by cyclic-AMP-dependent protein kinase, previously demonstrated in cell-free assays, also operates in intact cells. AICAR should be a useful tool for identifying new target pathways and processes regulated by the protein kinase cascade.

  • 5‐Aminoimidazole‐4‐Carboxamide Ribonucleoside
    FEBS Journal, 1995
    Co-Authors: Julia M. Corton, John G. Gillespie, Simon A. Hawley, D. Grahame Hardie

    Abstract:

    The AMP-activated protein kinase (AMPK) is believed to protect cells against environmental stress (e.g. heat shock) by switching off biosynthetic pathways, the key signal being elevation of AMP. Identification of novel targets for the kinase cascade would be facilitated by development of a specific agent for activating the kinase in intact cells. Incubation of rat hepatocytes with 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) results in accumulation of the monophosphorylated derivative (5-aminoimidaz-ole-4-carboxamide ribonucleoside; ZMP) within the cell. ZMP mimics both activating effects of AMP on AMPK, i.e. direct allosteric activation and promotion of phosphorylation by AMPK kinase. Unlike existing methods for activating AMPK in intact cells (e.g. fructose, heat shock), AICAR does not perturb the cellular contents of ATP, ADP or AMP. Incubation of hepatocytes with AICAR activates AMPK due to increased phosphorylation, causes phosphorylation and inactivation of a known target for AMPK (3-hydroxy-3-methylglutaryl-CoA reductase), and almost total cessation of two of the known target pathways, i.e. fatty acid and sterol synthesis. Incubation of isolated adipocytes with AICAR antagonizes isoprenaline-induced lipolysis. This provides direct evidence that the inhibition by AMPK of activation of hormone-sensitive lipase by cyclic-AMP-dependent protein kinase, previously demonstrated in cell-free assays, also operates in intact cells. AICAR should be a useful tool for identifying new target pathways and processes regulated by the protein kinase cascade.

Yuanhong Liu – One of the best experts on this subject based on the ideXlab platform.

  • Gold-Catalyzed Formal [3 + 2] Cycloaddition of Ynamides with 4,5-Dihydro-1,2,4-oxadiazoles: Synthesis of Functionalized 4-Aminoimidazoles
    Organic letters, 2017
    Co-Authors: Gaonan Wang, Ning Sun, Yuanhong Liu

    Abstract:

    A gold-catalyzed formal [3 + 2] cycloaddition of ynamides with 4,5-dihydro-1,2,4-oxadiazoles has been developed. The reaction provides a concise and regioselective access to highly functionalized 4-Aminoimidazoles likely via the formation of an α-imino gold carbene intermediate followed by cyclization. 4,5-Dihydro-1,2,4-oxadiazole was found to act as an efficient N-iminonitrene equivalent in these reactions.