Chronic activation of AMP kinase results in NRF-1 activation and mitochondrial biogenesis.
@article{Bergeron2001ChronicAO, title={Chronic activation of AMP kinase results in NRF-1 activation and mitochondrial biogenesis.}, author={Raynald Bergeron and J. M. Ren and Kevin S. Cadman and Irene K. Moore and Pascal Perret and Marc Pypaert and Lawrence H. Young and Clay F. Semenkovich and Gerald I. Shulman}, journal={American journal of physiology. Endocrinology and metabolism}, year={2001}, volume={281 6}, pages={ E1340-6 } }
The underlying mechanism by which skeletal muscle adapts to exercise training or chronic energy deprivation is largely unknown. To examine this question, rats were fed for 9 wk either with or without beta-guanadinopropionic acid (beta-GPA; 1% enriched diet), a creatine analog that is known to induce muscle adaptations similar to those induced by exercise training. Muscle phosphocreatine, ATP, and ATP/AMP ratios were all markedly decreased and led to the activation of AMP-activated protein…
519 Citations
Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle
- BiologyThe Proceedings of the Nutrition Society
- 2004
The evidence indicates that the decrease in the levels of high-energy phosphates, leading to activation of AMP kinase (AMPK), and the increase in cytosolic Ca2+, which activates Ca2+/calmodulin-dependent protein Kinase (CAMK), are signals that initiate these adaptative responses.
Aging-Associated Reductions in AMP-Activated Protein Kinase Activity and Mitochondrial Biogenesis
- Biology, MedicineCell metabolism
- 2007
Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT 4 levels in muscle
- Biology
- 2004
The evidence indicates that the decrease in the levels of highenergy phosphates, leading to activation of AMP kinase (AMPK), and the increase in cytosolic Ca, which activates Ca/calmodulin-dependent protein Kinase (CAMK), are signals that initiate these adaptative responses.
Upregulation of Mitochondrial Uncoupling Protein-2 by the AMP-Activated Protein Kinase in Endothelial Cells Attenuates Oxidative Stress in Diabetes
- Biology, MedicineDiabetes
- 2008
It is concluded that AMPK activation increases UCP-2, resulting in the inhibition of both O2·− and prostacyclin synthase nitration in diabetes.
AMP-activated protein kinase-independent inhibition of hepatic mitochondrial oxidative phosphorylation by AICA riboside.
- Biology, ChemistryThe Biochemical journal
- 2007
It is concluded that AICA riboside inhibits cellular respiration by an AMPK-independent mechanism that likely results from the combined intracellular P(i) depletion and ZMP accumulation.
Normal hypertrophy accompanied by phosphoryation and activation of AMP‐activated protein kinase α1 following overload in LKB1 knockout mice
- BiologyThe Journal of physiology
- 2008
The data suggest that the α1 isoform of AMPK is preferentially activated in skeletal muscle following overload in the absence of metabolic adaptations, suggesting that this isoform might be important in the regulation of growth but not metabolism.
Chronic AMPK stimulation attenuates adaptive signaling in dystrophic skeletal muscle.
- Biology, MedicineAmerican journal of physiology. Cell physiology
- 2012
The data demonstrate that prior pharmacological conditioning is a salient determinant in how dystrophic muscle adapts to subsequent complementary, acute physiological stress stimuli and provide insight into possible therapeutic applications of synthetic agonists in neuromuscular diseases, such as during chronic administration to Duchenne muscular dystrophy patients.
Effects of chronic AICAR treatment on fiber composition, enzyme activity, UCP3, and PGC-1 in rat muscles.
- BiologyJournal of applied physiology
- 2003
The results seem to imply that the chronic activation of AMPK alters such muscle histochemical and metabolic characteristics, as well as the glycolytic and oxidative enzyme activities but not the antioxidant enzyme activities.
Exercise increases nuclear AMPK α2 in human skeletal muscle
- Biology
- 2003
The results suggest that nuclear translocation of AMPK might mediate the effects of exercise on skeletal muscle gene and protein expression.
5’ Adenosine Monophosphate-Activated Protein Kinase, Metabolism and Exercise
- BiologySports medicine
- 2004
This review discusses the putative roles of AMPK in acute and chronic exercise responses, and suggests avenues for future AMPK research in exercise physiology and biochemistry.
References
SHOWING 1-10 OF 50 REFERENCES
Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle.
- BiologyJournal of applied physiology
- 2000
The results suggest that chronic AMPK activation may mediate the effects of muscle contraction on some, but not all, biochemical adaptations of muscle to endurance exercise training.
Evidence for 5′AMP-Activated Protein Kinase Mediation of the Effect of Muscle Contraction on Glucose Transport
- Biology, MedicineDiabetes
- 1998
Data suggest that AICAR and contraction stimulate glucose transport by a similar insulin-independent signaling mechanism and are consistent with the hypothesis that AMPK is involved in exercise-stimulated glucose uptake.
Differential effects of creatine depletion on the regulation of enzyme activities and on creatine-stimulated mitochondrial respiration in skeletal muscle, heart, and brain.
- BiologyBiochimica et biophysica acta
- 1996
AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation.
- BiologyAmerican journal of physiology. Endocrinology and metabolism
- 2000
Observations support the concept that inhibition of ACC is an important component in stimulating fatty acid oxidation in response to exercise and that there is coordinated regulation of nNOSmu to protect the muscle from ischemia/metabolic stress.
AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle.
- Biology, Computer ScienceAmerican journal of physiology. Endocrinology and metabolism
- 1997
Evidence is provided that decreases in muscle content of malonyl-CoA can increase the rate of fatty acid oxidation, and perfusion with medium containing AICAR was found to activate AMPK in skeletal muscle, inactivate ACC, and decrease malony l-coA.
Adaptation of muscle to creatine depletion: effect on GLUT-4 glucose transporter expression.
- BiologyThe American journal of physiology
- 1993
Results provide evidence that chronic creatine depletion increases GLUT-4 expression by pretranslational mechanisms and support the hypothesis that the levels of mitochondrial enzymes, hexokinase, andglucose transport activity maximally stimulated by insulin was increased in parallel with GLut-4 protein concentration in the epitrochlearis.
Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise.
- Biology, Computer ScienceThe American journal of physiology
- 1996
The activation of the AMP-activated protein kinase with consequent phosphorylation and inactivation of ACC may be one of the primary events in the control of malonyl-CoA and hence fatty acid oxidation during exercise.
Dual regulation of the AMP‐activated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle
- BiologyThe EMBO journal
- 1998
The novel regulation of AMPK described here provides a mechanism by which energy supply can meet energy demand following the utilization of the immediate energy reserve provided by the creatine kinase–phosphocreatine system.
Respiratory Uncoupling Induces δ-Aminolevulinate Synthase Expression through a Nuclear Respiratory Factor-1-dependent Mechanism in HeLa Cells*
- BiologyThe Journal of Biological Chemistry
- 1999
The data suggest that the transcription factor NRF-1 plays a key role in cellular adaptation to energy demands by translating physiological signals into an increased capacity for generating energy.
Exercise induces isoform-specific increase in 5'AMP-activated protein kinase activity in human skeletal muscle.
- Biology, MedicineBiochemical and biophysical research communications
- 2000
Exercise at a higher intensity for only 20 min leads to increases in AMPK alpha2 activity but not alpha1 activity, suggesting that the alpha2-containing AMPK complex, rather than alpha1, may be involved in the metabolic responses to exercise in human skeletal muscle.