Effect of adrenodemedullation on decline in muscle malonyl-CoA during exercise

Winder, W. W.; Braiden, R. W.; Cartmill, D. C.; Hutber, C. A.; Jones, J. P.

doi:10.1152/jappl.1993.74.5.2548

Cited by 11 publications

(5 citation statements)

References 14 publications

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“…The current study is consistent with results obtained from adrenodemedullated exercising rats (29). To determine the role of epinephrine in causing the decrease in malonyl-CoA in muscle during exercise, rats were adrenodemedullated or sham operated and then subjected to treadmill running.…”

Section: Discussionsupporting

confidence: 87%

Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A

Winder

Wilson

et al. 1997

Journal of Applied Physiology

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192

127

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This study was designed to compare functional effects of phosphorylation of muscle acetyl-CoA carboxylase (ACC) by adenosine 3',5'-cyclic monophosphate-dependent protein kinase (PKA) and by AMP-activated protein kinase (AMPK). Muscle ACC (272 kDa) was phosphorylated and then subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography. Functional effects of phosphorylation were determined by measuring ACC activity at different concentrations of each of the substrates and of citrate, an activator of the enzyme. The maximal velocity (Vmax) and the Michaelis constants (Km) for ATP, acetyl-CoA, and bicarbonate were unaffected by phosphorylation by PKA. Phosphorylation by AMPK increased the Km for ATP and acetyl-CoA. Sequential phosphorylation by PKA and AMPK, first without label and second with label, appeared to reduce the extent of label incorporation, regardless of the order. The activation constant (Ka) for citrate activation was increased to the same extent by AMPK phosphorylation, regardless of previous or subsequent phosphorylation by PKA. Thus muscle ACC can be phosphorylated by PKA but with no apparent functional effects on the enzyme. AMPK appears to be the more important regulator of muscle ACC.

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Section: Discussionsupporting

confidence: 87%

Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A

Winder

Wilson

et al. 1997

Journal of Applied Physiology

Self Cite

192

127

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“…This decrease in malonyl-CoA is associated with an increase in AMPK activity and a decrease in ACC activity (22,47,77). It appears that this intracellular signaling cascade is contraction dependent, because nerve stimulation results in the same intracellular changes (10,22,71), denervation increases malonyl-CoA content (54), and adrenodemedullated rats running on a treadmill still have a decrease in muscle malonyl-CoA (76).…”

Section: Effects Of Exercise On Muscle Fatty Acid Oxidationmentioning

confidence: 99%

Regulation of Fatty Acid Oxidation in Skeletal Muscle

Rasmussen¹,

1999

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Researchers using animals are beginning to elucidate the control of fatty acid metabolism in muscle at the molecular and enzymatic level. This review examines the physiological data that has been collected from human subjects in the context of the proposed control mechanisms. A number of factors, including the availability of free fatty acids and the abundance of fatty acid transporters, may influence the rate of muscle fatty acid oxidation. However, the predominant point of control appears to be the rate at which fatty acyl-coenzyme A is transported into the mitochondria by the carnitine palmitoyl transferase system. In turn, evidence suggests that the intracellular concentration of malonyl-coenzyme A in muscle is an important regulator of carnitine palmitoyl transferase-I activity. Malonyl-coenzyme A is increased by glucose, which is likely the mechanism whereby glucose intake suppresses the transfer of fatty acids into the mitochondria for subsequent oxidation. In contrast, malonyl-coenzyme A levels decrease during exercise, which enables increased fatty acid oxidation. However, for any given carnitine palmitoyl transferase-I activity, there may be an effect of free fatty acid availability on fatty acid oxidation, particularly at low levels of free fatty acids. Nonetheless, the rate of glucose or glycogen metabolism is probably the primary regulator of the balance between glucose and fatty acid oxidation in muscle.

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“…This phenomenon might offer a mechanistic explanation for the depressive effect of carbohydrates on muscle fat oxidation (73). Submaximal physical exercise evokes a significant decline in the muscular content of malonyl CoA (68,306,307), which allows for an increased flux of fatty acyl units through the f3-oxidative pathway by relieving the inhibition of carnitine acyltransferase I. Enhanced supply of fatty acids to skeletal muscle mitochondria is also thought to be instrumental in mitigating the inhibitory effect of malonyl CoA on fatty acid oxidation, because increased levels of fatty acyl CoA render carnitine acyltransferase I less sensitive to malonyl CoA [ Fig.…”

Section: Skeletal Muscle Cellsmentioning

confidence: 99%

Lipid Metabolism in Muscle

Vusse

Reneman

1996

Comprehensive Physiology

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The sections in this article are: Supply and Cellular Uptake of Upids in Skeletal Muscles Albumin‐Bound Fatty Acids Fatty Acids in Circulating Lipoproteins Skeletal Muscle Fatty Acid Uptake Fatty Acid Metabolism in the Skeletal Muscle Cell Activation and Oxidation of Fatty Acids Intramuscular Triacylglycerols Supply and Utilization of Upids During Exercise Albumin‐Bound Fatty Acids in Plasma during Exercise Circulating Lipoprotein‐Triacylglycerols as a Potential Source of Fatty Acids during Exercise Contribution of Intramuscular Triacylglycerols to Fatty Acid Oxidation during Exercise Relative Contribution of Various Sources of Lipids to Overall Fatty Acid Utilization during Exercise Gender Differences in Lipid Utilization during Exercise Effect of Training on Skeletal Muscle Lipid Utilization Advantages of Enhanced Lipid Utilization by Trained Muscles during Exercise Possible Causes of Increased Lipid Consumption by Trained Muscles during Exercise Utilization of Plasma‐Borne Fatty Acids by Trained Muscles Circulating Lipoproteins as an Additional Source of Lipids for Trained Muscles Utilization of Intramuscular Triacylglycerols in Endurance‐Trained Muscles Regulation of Fatty Acid Release from Intramuscular Triacylglycerols in Trained Muscles Effect of Diet on Muscle Lipid Metabolism High‐Carbohydrate vs. High‐Fat Diets in Relation to Physical Performance Shift from Carbohydrate to Lipid Utilization by High‐Fat Diet Source of Lipid for Muscles during High‐Fat Diet Feeding Possible Mechanisms Underlying Increased Muscular Lipid Utilization during High‐Fat Feeding Interrelationship Between Muscular Carbohydrate and Lipid Metabolism The Glucose–Fatty Acid, or Randle, Cycle The Existence of the Randle Cycle in Skeletal Muscle Possible Mechanisms Underlying the Glucose‐Fatty Acid Cycle in Skeletal Muscle A Role for Malonyl CoA in Fuel Selection in Skeletal Muscle Cells Defects in the Skeletal Muscle Fatty Acid Oxidative Pathway Concluding Remarks

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Effect of adrenodemedullation on decline in muscle malonyl-CoA during exercise

Cited by 11 publications

References 14 publications

Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A

Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A

Regulation of Fatty Acid Oxidation in Skeletal Muscle

Lipid Metabolism in Muscle

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