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Insulin stimulation of glucose uptake fails to decrease palmitate oxidation in muscle if AMPK is activated.

W W Winder1, B F Holmes

  • 1Brigham Young University, Provo, Utah 84602, USA. william_winder@byu.edu

Journal of Applied Physiology (Bethesda, Md. : 1985)
|November 25, 2000
PubMed
Summary

AMP-activated protein kinase (AMPK) activation prevents high glucose uptake from inhibiting fatty acid oxidation in muscle. This finding is crucial for understanding metabolic regulation and potential therapeutic strategies.

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Area of Science:

  • Muscle metabolism
  • Cellular energy regulation
  • Biochemistry

Background:

  • Elevated insulin and glucose levels typically reduce fatty acid oxidation in muscle.
  • AMP-activated protein kinase (AMPK) is a key regulator of cellular energy homeostasis.

Purpose of the Study:

  • To investigate if AMPK activation can counteract the inhibitory effects of insulin and glucose on muscle fatty acid oxidation.

Main Methods:

  • Rat hindlimbs and isolated epitrochlearis muscles were perfused with varying concentrations of insulin and AICAR (an AMPK activator).
  • Measurements included glucose uptake, AMPK activity, acetyl-CoA carboxylase (ACC) activation, malonyl-CoA content, and palmitate oxidation rates.

Main Results:

  • Insulin increased glucose uptake and malonyl-CoA content, while attenuating AICAR-induced AMPK activation.

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  • AICAR activation of AMPK increased palmitate oxidation, independent of insulin levels or glucose uptake.
  • Malonyl-CoA levels were reduced by AICAR, mitigating its inhibitory effect on fatty acid oxidation.

    • Conclusions:

    • AMPK activation effectively prevents high glucose uptake and glycolytic flux from inhibiting fatty acid oxidation in fast-twitch muscle.
    • This suggests a critical role for AMPK in maintaining fatty acid oxidation under conditions of high glucose availability.