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PPARbeta Activation Induces Rapid Changes of Both AMPK Subunit Expression and AMPK Activation in Mouse Skeletal Muscle



PPARbeta Activation Induces Rapid Changes of Both AMPK Subunit Expression and AMPK Activation in Mouse Skeletal Muscle







AMP-activated protein kinases (AMPK) are heterotrimeric, αβ, serine/threonine kinases. The 3-AMPK subunit is particularly interesting in muscle physiology because 1) it is specifically expressed in skeletal muscle, 2) α2β23 is the AMPK heterotrimer activated during exercise in humans, and 3) it is down-regulated in humans after a training period. However, mechanisms underlying this decrease of 3-AMPK expression remained unknown. We investigated whether the expression of AMPK subunits and particularly that of 3-AMPK are regulated by the PPARβ pathway. We report that PPARβ activation with GW742 induces a rapid (2 h) and sustained down-regulation of 3-AMPK expression both in mouse skeletal muscles and in culture myotubes. Concomitantly, phosphorylation levels of both AMPK and acetyl-coenzyme A carboxylase are rapidly modified. The 3-AMPK down-regulation is also observed in muscles from young and adult transgenic mice with muscle-specific overexpression of peroxisome proliferator-activated receptor β (PPARβ). We showed that 3-AMPK down-regulation is a rapid physiological muscle response observed in mouse after running exercise or fasting, two situations leading to PPARβ activation. Finally, using C2C12, we demonstrated that dose and time-dependent down-regulation of 3-AMPK expression upon GW742 treatment, is due to decrease 3-AMPK promoter activity.

Accession: 036191659

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