PMID- 9429650
OWN - NLM
STAT- MEDLINE
DCOM- 19980311
LR  - 20220410
IS  - 0001-6772 (Print)
IS  - 0001-6772 (Linking)
VI  - 161
IP  - 4
DP  - 1997 Dec
TI  - Enzyme adaptations of human skeletal muscle during bicycle short-sprint training 
      and detraining.
PG  - 439-45
AB  - 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.
FAU - Linossier, M T
AU  - Linossier MT
AD  - Laboratoire de Physiologie, Faculte de Medecine Saint-Etienne, France.
FAU - Dormois, D
AU  - Dormois D
FAU - Perier, C
AU  - Perier C
FAU - Frey, J
AU  - Frey J
FAU - Geyssant, A
AU  - Geyssant A
FAU - Denis, C
AU  - Denis C
LA  - eng
PT  - Clinical Trial
PT  - Journal Article
PL  - England
TA  - Acta Physiol Scand
JT  - Acta physiologica Scandinavica
JID - 0370362
RN  - 0 (Enzymes)
RN  - EC 1.1.1.27 (L-Lactate Dehydrogenase)
RN  - EC 2.3.3.1 (Citrate (si)-Synthase)
RN  - EC 2.4.1.- (Phosphorylases)
RN  - EC 2.7.1.1 (Hexokinase)
RN  - EC 2.7.1.11 (Phosphofructokinase-1)
RN  - EC 2.7.3.2 (Creatine Kinase)
RN  - EC 2.7.4.3 (Adenylate Kinase)
SB  - IM
MH  - *Adaptation, Physiological
MH  - Adenylate Kinase/analysis/metabolism
MH  - Adult
MH  - Anaerobic Threshold/physiology
MH  - Citrate (si)-Synthase/analysis/metabolism
MH  - Creatine Kinase/analysis/metabolism
MH  - Enzymes/analysis/*physiology
MH  - Exercise/*physiology
MH  - Exercise Test
MH  - Hexokinase/analysis/metabolism
MH  - Humans
MH  - L-Lactate Dehydrogenase/analysis/metabolism
MH  - Male
MH  - Muscle, Skeletal/*enzymology
MH  - Oxygen Consumption/physiology
MH  - Phosphofructokinase-1/analysis/metabolism
MH  - Phosphorylases/analysis/metabolism
EDAT- 1998/01/16 00:00
MHDA- 1998/01/16 00:01
CRDT- 1998/01/16 00:00
PHST- 1998/01/16 00:00 [pubmed]
PHST- 1998/01/16 00:01 [medline]
PHST- 1998/01/16 00:00 [entrez]
AID - 10.1046/j.1365-201X.1997.00244.x [doi]
PST - ppublish
SO  - Acta Physiol Scand. 1997 Dec;161(4):439-45. doi: 
      10.1046/j.1365-201X.1997.00244.x.