Mechanism of training-induced attenuation of postexercise ketosis

Beattie, M. A.; Winder, W. W.

doi:10.1152/ajpregu.1984.247.5.r780

Cited by 8 publications

(10 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Endurance-trained rats and humans have been reported to be more resistant to postexercise ketosis than untrained controls (Johnson, Walton, Krebs & Williamson, 1969;Johnson & Walton, 1971;Rennie, Jennett & Johnson, 1974;Winder, Hickson, Hagberg, Ehsani & McLane, 1979), though other studies (Grollman & Phillips, 1954;Passmore & Johnson, 1958;Johnson & Passmore, 1960;Askew, Dohm & Huston, 1975;Koeslag, Noakes & Sloan, 1980;Beattie & Winder, 1984) have shown that it is the athletes who develop the higher blood concentrations of ketone bodies during the recovery from a standard bout of exercise. The only factor which appears to distinguish these two groups of studies is diet.…”

Section: Introductionmentioning

confidence: 98%

Glycogen Metabolism and Post‐exercise Ketosis in Carbohydrate‐restricted Trained and Untrained Rats

Adams

Koeslag

1989

Exp Physiol

View full text Add to dashboard Cite

SUMMARYLiver and muscle glycogen, and blood 3-hydroxybutyrate concentrations were studied during and for 2 h after treadmill running for I h, in 144 carbohydrate-starved trained and untrained rats. The resting liver glycogen concentration of the trained animals was 227 + 8 (mean + S.E.M.),umol glucosyl units/g wet mass, compared with 162 + 12 ,umol/g in the untrained animals. The muscle glycogen levels were 42 + 1 and 28± 1 ,umol/g respectively. Exercise reduced muscle and liver glycogen concentrations by approximately the same absolute amounts in both animal groups, leaving the trained rats with nearly 3 times as much residual glycogen as the untrained animals. There was very little resynthesis of muscle glycogen recovery, but the trained animals replenished approximately 43 % of the liver glycogen used during exercise. The blood 3-hydroxybutyrate concentrations were negatively correlated with the simultaneous liver glycogen concentration of our experimental animals (r = -0 55; P < 000O1). It is concluded that trained animals primarily owe their resistance to post-exercise ketosis to their large stores of glycogen.

show abstract

Section: Introductionmentioning

confidence: 98%

Glycogen Metabolism and Post‐exercise Ketosis in Carbohydrate‐restricted Trained and Untrained Rats

Adams

Koeslag

1989

Exp Physiol

View full text Add to dashboard Cite

show abstract

“…, ; Askew et al . ; Beattie & Winder, ). This coincides with two‐ to threefold higher ex vivo rates of βHB and AcAc oxidation in gastrocnemius muscle homogenates presented with concentrations of both βHB and AcAc at 0.1 and 0.5 m m (Winder et al .…”

Section: Introductionmentioning

confidence: 99%

“…; Johnson & Walton, ; Rennie et al . ), or after a period of exercise training (Rennie & Johnson, ; Beattie & Winder, , ; Adams & Koeslag, , ; Ohmori et al . ).…”

Section: Introductionmentioning

confidence: 99%

Metabolism of ketone bodies during exercise and training: physiological basis for exogenous supplementation

Evans

Cogan

Egan

2016

The Journal of Physiology

299

304

View full text Add to dashboard Cite

Optimising training and performance through nutrition strategies is central to supporting elite sportspeople, much of which has focused on manipulating the relative intake of carbohydrate and fat and their contributions as fuels for energy provision. The ketone bodies, namely acetoacetate, acetone and β-hydroxybutyrate (βHB), are produced in the liver during conditions of reduced carbohydrate availability and serve as an alternative fuel source for peripheral tissues including brain, heart and skeletal muscle. Ketone bodies are oxidised as a fuel source during exercise, are markedly elevated during the post-exercise recovery period, and the ability to utilise ketone bodies is higher in exercise-trained skeletal muscle. The metabolic actions of ketone bodies can alter fuel selection through attenuating glucose utilisation in peripheral tissues, anti-lipolytic effects on adipose tissue, and attenuation of proteolysis in skeletal muscle. Moreover, ketone bodies can act as signalling metabolites, with βHB acting as an inhibitor of histone deacetylases, an important regulator of the adaptive response to exercise in skeletal muscle. Recent development of ketone esters facilitates acute ingestion of βHB that results in nutritional ketosis without necessitating restrictive dietary practices. Initial reports suggest this strategy alters the metabolic response to exercise and improves exercise performance, while other lines of evidence suggest roles in recovery from exercise. The present review focuses on the physiology of ketone bodies during and after exercise and in response to training, with specific interest in exploring the physiological basis for exogenous ketone supplementation and potential benefits for performance and recovery in athletes.

show abstract

“…In contrast, the decrease in malonyl-CoA during long-term, low-intensity exercise may occur by mechanisms other than phosphorylation of ACC. carnitine palmitoyltransferase-1; malonyl-coenzyme A; postexercise ketosis; 3-hydroxybutyrate POSTEXERCISE KETOSIS occurs after prolonged bouts of endurance exercise or after shorter bouts in fasted or carbohydrate-deficient states (2,3,7,13,14). In rats, the elevated 3-hydroxybutyrate levels seen during and after prolonged bouts of submaximal exercise are accompanied by a decline in liver malonyl-CoA (2,3,7).…”

mentioning

confidence: 99%

Liver AMP-activated protein kinase and acetyl-CoA carboxylase during and after exercise

Carlson

Winder

1999

Journal of Applied Physiology

Self Cite

View full text Add to dashboard Cite

Exercise induces a decline in liver malonyl-CoA, an inhibitor of carnitine palmitoyltransferase-1. The purpose of these experiments was to determine whether this decrease in malonyl-CoA is accompanied by an activation of AMP-activated protein kinase (AMPK) and inactivation of acetyl-CoA carboxylase (ACC). Rats were killed at rest, after 10 min of running at 32 m/min up a 15% grade or at 0, 15, or 60 min postexercise after 120 min of running at 16 m/min. There was no significant difference in AMPK and ACC activities after 120 min of exercise, although a trend toward a decrease in ACC and an increase in AMPK was noted 15 min postexercise. After 10 min at 32 m/min, however, maximal ACC activity decreased from 487 +/- 27 to 280 +/- 39 nmol. g-1. min-1, and the activation constant for citrate activation of ACC increased from 5.9 to 12.5 mM. AMPK activity increased from a resting value of 4.7 +/- 0.4 to 9.8 +/- 2.0 pmol. mg-1. min-1 after exercise. These data provide indirect evidence of phosphorylation and inactivation of liver ACC during heavy exercise. In contrast, the decrease in malonyl-CoA during long-term, low-intensity exercise may occur by mechanisms other than phosphorylation of ACC.

show abstract

Mechanism of training-induced attenuation of postexercise ketosis

Cited by 8 publications

References 0 publications

Glycogen Metabolism and Post‐exercise Ketosis in Carbohydrate‐restricted Trained and Untrained Rats

Glycogen Metabolism and Post‐exercise Ketosis in Carbohydrate‐restricted Trained and Untrained Rats

Metabolism of ketone bodies during exercise and training: physiological basis for exogenous supplementation

Liver AMP-activated protein kinase and acetyl-CoA carboxylase during and after exercise

Contact Info

Product

Resources

About