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Kruk. В., Szczypaczewska M., Opaszowski В., Kaciuba Uściłko H., Nazar K. Thermoregulatory and metabolic responses to repeated bouts of prolonged cycle-ergometer exercise in man. Acta Physiol. Pol., Changes in body temperature, oxygen uptake (VO₂ ), heart rate (HR), sweating rate and plasma osmolality were examined in 10 human subjects, performing four successive 30 min exercise-bouts of the same intensity (50% VO₂ max) separated by 30 min rest periods. In spite of the rest intervals and replacement of body fluid loss there was a progressive increase in VO₂ . HR, rectal (Tre) and mean body (Tb) temperatures in consecutive exercise bouts. The thermoregulatory efficiency showed an increasing tendency, and a delay in the sweating response at the beginning of each exercise was shortened. It is concluded that a drift in metabolic and temperature responses to exercise, reported throughout a long-term continuous work, occurs also in the euhydrated subjects performing a prolonged intermittent exercise. It is not caused by an impaired thermoregulation during exercise but rather by insufficient restitution of metabolic processes during rest intervals.
The study was designed to determine metabolic and hormonal responses to acute modification of body carbohydrate stores by exercise and subsequent meals and to find out whether the responses depend on the training status of subjects. Nine sedentary students and 10 endurance athletes took part in four experimental sessions. During control session, after overnight fast oxygen uptake and CO2 production were measured and blood glucose, free fatty acids (FFA), insulin (I), leptin (L), growth hormone (GH), testosterone (T), catecholamines, ACTH and cortisol were determined. The remaining sessions were preceded by 1.5 h exercise at 70% HRmax in the evening followed by 12-16 hrs fast till morning when subjects ate either high-carbohydrate (H-CHO) or low-carbohydrate (L-CHO) meal or fasted. Respiratory gases and blood samples were collected before and 2 hours after meal. In glycogen depleted subjects respiratory quotient (RQ), I, norepinephrine (NE) and L decreased, whilst other variables were unaltered. Changes in I and NE were greater in athletes than in sedentary subjects. After H-CHO RQ, blood glucose, I and NE increased and FFA, GH and T decreased. The latter effect was greater in athletes than in untrained subjects. After L-CHO, RQ was at the fasting level and FFA increased only in sedentary group. In both groups I increased and GH and T decreased. Neither meal affected L concentration. In conclusion, hormonal and metabolic changes observed after depleting carbohydrate stores resemble those occurring during starvation. Composition of the ingested meal affects postprandial metabolism, which additionally depends on the subjects’ training status.
The aim of this study was to compare the effects of TNF-α, IL-1β and IFN-γ on the activation of protein kinase B (PKB), p70S6k, mitogen-activated protein kinase (MAPK) and p90rsk, and on IGF-I-stimulated glucose uptake and protein synthesis in mouse C2C12 myotubes. 100 nmol/l IGF-I stimulated glucose uptake in C2C12 myotubes by 198.1% and 10 ng/ml TNF-α abolished this effect. Glucose uptake in cells differentiated in the presence of 10 ng/ml IFN-γ increased by 167.2% but did not undergo significant further modification upon the addition of IGF-I. IGF-I increased the rate of protein synthesis by 249.8%. Neither TNF-α nor IFN-γ influenced basal protein synthesis, but both cytokines prevented the IGF-I effect. 10 ng/ml IL-1β did not modify either the basal or IGF-I-dependent glucose uptake and protein synthesis. With the exception of TNF-α causing an 18% decrease in the level of PKB protein, the cellular levels of PKB, p70S6k, p42MAPK, p44MAPK and p90rsk were not affected by the cytokines. IGF-I caused the phosphorylation of PKB (an approximate 8-fold increase above the basal value after 40 min of IGF-I treatment), p42MAPK (a 2.81-fold increase after 50 min), and the activation of p70S6k and p90rsk, manifesting as gel mobility retardation. In cells differentiated in the presence of TNF-α or IFN-γ, this IGF-I-mediated PKB and p70S6k phosphorylation was significantly diminished, and the increase in p42MAPK and p90rsk phosphorylation was prevented. The basal p42MAPK phosphorylation in C2C12 cells treated with IFN-γ was high and comparable with the activation of this kinase by IGF-I. Pretreatment of myogenic cells with IL-1β did not modify the IGF-I-stimulated phosphorylation of PKB, p70S6k, p42MAPK and p90rsk. In conclusion: i) TNF-α and IFN-γ, but not IL-1β, if present in the extracellular environment during C2C12 myoblast differentiation, prevent the stimulatory action of IGF-I on protein synthesis. ii) TNF-α- and IFN-γ-induced IGF-I resistance of protein synthesis could be associated with the decreased phosphorylation of PKB and p70S6k. iii) The activation of glucose uptake in C2C12 myogenic cells treated with IFN-γ is PKB independent. iv) The similar effects of TNF-α and IFN-γ on the signalling and action of IGF-I on protein synthesis in myogenic cells could suggest the involvement of both of these cytokines in protein loss in skeletal muscle.
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