PMID- 18557841
OWN - NLM
STAT- MEDLINE
DCOM- 20090805
LR  - 20131121
IS  - 1748-1716 (Electronic)
IS  - 1748-1708 (Linking)
VI  - 194
IP  - 4
DP  - 2008 Dec
TI  - Control of lipid oxidation during exercise: role of energy state and 
      mitochondrial factors.
PG  - 283-91
LID - 10.1111/j.1748-1716.2008.01879.x [doi]
AB  - Despite considerable progress during recent years our understanding of how lipid 
      oxidation (LOx) is controlled during exercise remains incomplete. This review 
      focuses on the role of mitochondria and energy state in the control of LOx. LOx 
      increases in parallel with increased energy demand up to an exercise intensity of 
      about 50-60% of VO(2max) after which the contribution of lipid decreases. The 
      switch from lipid to carbohydrate (CHO) is of energetic advantage due to the 
      increased ATP/O(2) yield. In the low-intensity domain (<50%VO(2max)) a moderate 
      reduction in energy state will stimulate both LOx and CHO oxidation and relative 
      fuel utilization is mainly controlled by substrate availability and the capacity 
      of the metabolic pathways. In the high-intensity domain (>60%VO(2max)) there is a 
      pronounced decrease in energy state, which will stimulate glycolysis in excess of 
      the substrate requirements of the oxidative processes. This will lead to 
      acidosis, reduced levels of free Coenzyme A (CoASH) and reduced levels of free 
      carnitine. Acidosis and reduced carnitine may limit the carnitine-mediated 
      transfer of long-chain fatty acids (LCFA) into mitochondria and may thus explain 
      the observed reduction in LOx during high-intensity exercise. Another potential 
      mechanism, suggested in this review, is that Acyl-CoA synthetase (ACS), an 
      initial step in LCFA catabolism, functions as a regulator of LOx. ACS activity is 
      suggested to be under control of CoASH and energy state. Furthermore, evidence 
      exists that additional control points exist beyond mitochondrial FA influx. The 
      nature and site of this control remain to be investigated.
FAU - Sahlin, K
AU  - Sahlin K
AD  - GIH, The Swedish School of Sport and Health Sciences, Astrands Laboratory, 
      Stockholm, Sweden. kent.sahlin@gih.se
FAU - Harris, R C
AU  - Harris RC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20080709
PL  - England
TA  - Acta Physiol (Oxf)
JT  - Acta physiologica (Oxford, England)
JID - 101262545
RN  - 0 (Adenine Nucleotides)
RN  - EC 2.3.1.21 (Carnitine O-Palmitoyltransferase)
RN  - SAA04E81UX (Coenzyme A)
SB  - IM
MH  - Adenine Nucleotides/metabolism
MH  - Carnitine O-Palmitoyltransferase/physiology
MH  - Coenzyme A/physiology
MH  - Energy Metabolism/physiology
MH  - Exercise/*physiology
MH  - Humans
MH  - Lipid Metabolism/*physiology
MH  - Mitochondria, Muscle/*metabolism
MH  - Muscle, Skeletal/metabolism
MH  - Oxidation-Reduction
RF  - 50
EDAT- 2008/06/19 09:00
MHDA- 2009/08/06 09:00
CRDT- 2008/06/19 09:00
PHST- 2008/06/19 09:00 [pubmed]
PHST- 2009/08/06 09:00 [medline]
PHST- 2008/06/19 09:00 [entrez]
AID - APS1879 [pii]
AID - 10.1111/j.1748-1716.2008.01879.x [doi]
PST - ppublish
SO  - Acta Physiol (Oxf). 2008 Dec;194(4):283-91. doi: 
      10.1111/j.1748-1716.2008.01879.x. Epub 2008 Jul 9.