title: Enzyme adaptations of human skeletal muscle during bicycle short-sprint training and detraining.
abstract: The effect of sprint training and detraining on supramaximal performances was studied in relation to muscle enzyme adaptations in eight students trained four times a week for 9 weeks on a cycle ergometer. The subjects were tested for peak oxygen uptake (VO2peak), maximal aerobic power (MAP) and maximal short-term power output (Wmax) before and after training and after 7 weeks of detraining. During these periods, biopsies were taken from vastus lateralis muscle for the determination of creatine kinase (CK), adenylate kinase (AK), glycogen phosphorylase (PHOS), hexokinase (HK), phosphofructokinase (PFK), lactate dehydrogenase (LDH) and its isozymes, 3-hydroxy-acyl-CoA dehydrogenase (HAD) and citrate synthase (CS) activities. Training induced large improvements in Wmax (28%) with slight increases (3%) in VO2peak (P < 0.10). This was associated with a greater glycolytic potential as shown by higher activities for PHOS (9%), PFK (17%) and LDH (31%) after training, without changes in CK and oxidative markers (CS and HAD). Detraining induced significant decreases in VO2peak (4%), MAP (5%) and oxidative markers (10-16%), while Wmax and the anaerobic potential were maintained at a high level. This suggests a high level in supramaximal power output as a result of a muscle glycogenolytic and glycolytic adaptation. A long interruption in training has negligible effects on short-sprint ability and muscle anaerobic potential. On the other hand, a persistent training stimulus is required to maintain high aerobic capacity and muscle oxidative potential. This may contribute to a rapid return to competitive fitness for sprinters and power athletes.
authors.affiliation: Laboratoire de Physiologie, Faculté de Médecine Saint-Etienne, France.
authors.forename: M T
authors.initials: MT
authors.lastname: Linossier
authors.forename: D
authors.initials: D
authors.lastname: Dormois
authors.forename: C
authors.initials: C
authors.lastname: Perier
authors.forename: J
authors.initials: J
authors.lastname: Frey
authors.forename: A
authors.initials: A
authors.lastname: Geyssant
authors.forename: C
authors.initials: C
authors.lastname: Denis
mesh_terms: D000222:Adaptation, Physiological; D000263:Adenylate Kinase / Q000032:analysis / Q000378:metabolism; D000328:Adult; D015308:Anaerobic Threshold / Q000502:physiology; D002950:Citrate (si)-Synthase / Q000032:analysis / Q000378:metabolism; D003402:Creatine Kinase / Q000032:analysis / Q000378:metabolism; D004798:Enzymes / Q000032:analysis / Q000502:physiology*; D015444:Exercise / Q000502:physiology*; D005080:Exercise Test; D006593:Hexokinase / Q000032:analysis / Q000378:metabolism; D006801:Humans; D007770:L-Lactate Dehydrogenase / Q000032:analysis / Q000378:metabolism; D008297:Male; D018482:Muscle, Skeletal / Q000201:enzymology*; D010101:Oxygen Consumption / Q000502:physiology; D010732:Phosphofructokinase-1 / Q000032:analysis / Q000378:metabolism; D006005:Phosphorylases / Q000032:analysis / Q000378:metabolism
chemical_list: D004798:Enzymes; D007770:L-Lactate Dehydrogenase; D002950:Citrate (si)-Synthase; D006005:Phosphorylases; D006593:Hexokinase; D010732:Phosphofructokinase-1; D003402:Creatine Kinase; D000263:Adenylate Kinase