• Corpus ID: 16970612

rate of palmitate oxidation in rat muscle Influence of malonyl-CoA and palmitate concentration on

@inproceedings{Merrill1998rateOP,
  title={rate of palmitate oxidation in rat muscle Influence of malonyl-CoA and palmitate concentration on},
  author={Gary F. Merrill and E J Kurth and Blake B. Rasmussen and William W. Winder},
  year={1998}
}
especially those papers emphasizing adaptive and integrative mechanisms. It is published 12 times a year (monthly) by publishes original papers that deal with diverse area of research in applied physiology, 
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SHOWING 1-10 OF 31 REFERENCES
5 Malonyl‐CoA—Regulator of Fatty Acid Oxidation in Muscle During Exercise
  • W. Winder
  • Biology
    Exercise and sport sciences reviews
  • 1998
TLDR
As muscle goes from a resting state to exercise, the following sequence of events occurs: the rise in AMP accompanying contraction allosterically activates AMPK and an AMPK kinase, which relieves inhibition of CPT-1 and allows an increased rate of fatty acid oxidation when fatty acids become available.
Malonyl-CoA regulation in skeletal muscle: its link to cell citrate and the glucose-fatty acid cycle.
TLDR
The results suggest that in the presence of glucose, insulin and acetoacetate acutely increase malonyl-CoA levels in the incubated soleus by increasing the cytosolic concentration of citrate, a novel mechanism that could complement the glucose-fatty acid cycle in determining how muscle chooses its fuels.
Hepatic malonyl-CoA levels of fed, fasted and diabetic rats as measured using a simple radioisotopic assay.
TLDR
Application of the radioisotopic method to the measurement of malonyl-CoA in livers from fed, fasted, and diabetic rats yielded values that were consistent with the recently postulated role of maloneyl- CoA in the regulation of hepatic ketone body production.
Time course of exercise-induced decline in malonyl-CoA in different muscle types.
TLDR
The rate of decline in malonyl-CoA in muscle during the course of a prolonged exercise bout may be an important signal for allowing increased fatty acid oxidation during long-term exercise.
Adaptation of muscle to exercise. Increase in levels of palmityl Coa synthetase, carnitine palmityltransferase, and palmityl Coa dehydrogenase, and in the capacity to oxidize fatty acids.
The capacity of gastrocnemius and quadriceps muscles to oxidize palmitate, oleate, linoleate, palmityl CoA, and palmityl carnitine doubled in rats subjected to a program of treadmill running. The
Impaired plasma FFA oxidation imposed by extreme CHO deficiency in contracting rat skeletal muscle.
The extent to which carbohydrate (CHO) availability affects free fatty acid (FFA) metabolism in contracting skeletal muscle is not well characterized. To study this question, rats were depleted of
Effect of fasting and refeeding on acetyl-CoA carboxylase in rat hindlimb muscle.
TLDR
Skeletal muscle ACC is controlled by different mechanisms than those observed in liver, and is found to respond to dietary manipulation similarly to liver.
Contraction-induced Changes in Acetyl-CoA Carboxylase and 5′-AMP-activated Kinase in Skeletal Muscle*
The concentration of malonyl-CoA, a negative regulator of fatty acid oxidation, diminishes acutely in contracting skeletal muscle. To determine how this occurs, the activity and properties of
The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis.
TLDR
Key developments of the last 20 years that have led to the current understanding of the physiology of the CPT system, the structure of theCPT isoforms, the chromosomal localization of their respective genes, and the identification of mutations in the human population are reviewed.
Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise.
TLDR
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.
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