|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Centre of Inflammation and Metabolism, Rigshospitalet, Copenhagen, Denmark; Department of Infectious Diseases, Rigshospitalet, Copenhagen, Denmark; The Copenhagen Muscle Research Centre, Rigshospitalet, Copenhagen, Denmark
2 Centre of Inflammation and Metabolism, Rigshospitalet, Copenhagen, Denmark; Section of Neuroprotection, The Panum Institute University of Copenhagen, Copenhagen, Denmark
3 Institute for Molecular Biology and Physiology, The August Krogh Building, University of Copenhagen, Copenhagen Muscle Research, Rigshospitalet, Centre of Inflammation and Metabolism, Copenhagen, Denmark
4 The Copenhagen Muscle Research Centre, Rigshospitalet, Copenhagen, Denmark
5 Centre of Inflammation and Metabolism, Rigshospitalet, Copenhagen, Denmark; Copenhagen Muscle Research Centre, Institute for Molecular Biology and Physiology, The August Krogh Building, University of Copenhagen, Copenhagen, Denmark
* To whom correspondence should be addressed. E-mail: plomgaard{at}dadlnet.dk.
The metabolic profile of rodent muscle is generally reflected in the MHC fiber type composition. The present study was conducted to test the hypothesis that metabolic gene expression is not tightly coupled with MHC fiber type composition for all genes in human skeletal muscle. Triceps brachii, vastus lateralis quadriceps and soleus muscle biopsies were obtained from normally physically active healthy young male volunteers, because these muscles are characterized by different fiber type compositions. As expected, CS and HAD activity was more than 2 fold higher in soleus and vastus than in triceps. Contrary, PFK and total LDH activity was approximately 3 and 2 fold higher in triceps than in both soleus and vastus. Expression of metabolic genes was assessed by determining the mRNA content of a broad range of metabolic genes. The triceps muscle had 2-5 fold higher MHC IIa, phosphofructokinase and lactate dehydrogenase A mRNA content and 2-4 fold lower MHC I, LPL, CD36, HSL and LDH B and HKII mRNA than vastus lateralis or soleus. Interestingly, such mRNA differences were not evident for any of the genes encoding mitochondrial oxidative proteins: HAD, CPTI, CS,
KGDH and Cytc nor for the transcriptional regulators: PGC-1
, FoxO1 or PPAR
. Thus, the mRNA expression of genes encoding mitochondrial proteins and transcriptional regulators does not seem to be fiber type specific as the genes encoding glycolytic and lipid metabolism genes, which suggests that basal mRNA regulation of genes encoding mitochondrial proteins does not match the wide differences in mitochondrial content of these muscles.
This article has been cited by other articles:
![]() |
L. Leick, J. F. P. Wojtaszewski, S. T. Johansen, K. Kiilerich, G. Comes, Y. Hellsten, J. Hidalgo, and H. Pilegaard PGC-1{alpha} is not mandatory for exercise- and training-induced adaptive gene responses in mouse skeletal muscle Am J Physiol Endocrinol Metab, February 1, 2008; 294(2): E463 - E474. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Kiilerich, J. B. Birk, R. Damsgaard, J. F. P. Wojtaszewski, and H. Pilegaard Regulation of PDH in human arm and leg muscles at rest and during intense exercise Am J Physiol Endocrinol Metab, January 1, 2008; 294(1): E36 - E42. [Abstract] [Full Text] [PDF] |
||||
![]() |
O. H. Mortensen, P. Plomgaard, C. P. Fischer, A. K. Hansen, H. Pilegaard, and B. K. Pedersen PGC-1beta is downregulated by training in human skeletal muscle: no effect of training twice every second day vs. once daily on expression of the PGC-1 family J Appl Physiol, November 1, 2007; 103(5): 1536 - 1542. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Visit Other APS Journals Online |