|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Noll Physiological Research Center, The Pennsylvania State University, Univesity Park, PA, USA; Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, PA, USA
2 Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, PA, USA
3 Noll Physiological Research Center, The Pennsylvania State University, Univesity Park, PA, USA
* To whom correspondence should be addressed. E-mail: nxk171{at}psu.edu.
The focus of the study described herein was to examine the relative expression levels of mRNAs and proteins relevant to the regulation of translational initation, and hence protein synthesis, in the time course following an acute bout of resistance exercise in male Sprague Dawley rats. Significant increases in the relative abundance of the mRNAs coding for the epsilon (33%) and gamma (26%) subunits of eukaryotic initiation factor (eIF) 2B were observed 48 hrs after the exercise bout. Furthermore, the mRNA coding for the delta subunit of eIF2B was also significantly increased, both 24 hr (46%) and 48 hr (44%) post-exercise. There was a relative decrease in three eIF2B
kinase mRNAs, namely sequences coding for glycogen synthase kinase 3
(49%), casein kinase I (48%), and casein kinase II (42%) 48 hr into the recovery period. Additionally, there was a significant decrease in expression of the mRNAs coding for eIF2
(28% 24 hr post-exercise) and one of its regulatory kinases, double-stranded RNA-activated protein kinase (PKR) (33% 48 hr post-exercise). Finally, an increase in eIF2B total protein (124%) was observed within 3 hr post-exercise. These results suggest that there may be rapid translational regulation of mRNAs coding for species relevant to translational initiation following an acute bout of resistance exercise. Furthermore, transcription of these mRNAs is altered further into the recovery period, and this might play a role in protein synthetic capacity upon subsequent bouts of resistance exercise.
This article has been cited by other articles:
![]() |
C. M. Dieli-Conwright, T. M. Spektor, J. C. Rice, F. R. Sattler, and E. T. Schroeder Influence of hormone replacement therapy on eccentric exercise induced myogenic gene expression in postmenopausal women J Appl Physiol, November 1, 2009; 107(5): 1381 - 1388. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. M. Dieli-Conwright, T. M. Spektor, J. C. Rice, and E. T. Schroeder Hormone therapy attenuates exercise-induced skeletal muscle damage in postmenopausal women J Appl Physiol, September 1, 2009; 107(3): 853 - 858. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. J. Drummond, C. S. Fry, E. L. Glynn, H. C. Dreyer, S. Dhanani, K. L. Timmerman, E. Volpi, and B. B. Rasmussen Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis J. Physiol., April 1, 2009; 587(7): 1535 - 1546. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. D. Fluckey, M. Knox, L. Smith, E. E. Dupont-Versteegden, D. Gaddy, P. A. Tesch, and C. A. Peterson Insulin-facilitated increase of muscle protein synthesis after resistance exercise involves a MAP kinase pathway Am J Physiol Endocrinol Metab, June 1, 2006; 290(6): E1205 - E1211. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Kubica, D. R. Bolster, P. A. Farrell, S. R. Kimball, and L. S. Jefferson Resistance Exercise Increases Muscle Protein Synthesis and Translation of Eukaryotic Initiation Factor 2B{epsilon} mRNA in a Mammalian Target of Rapamycin-dependent Manner J. Biol. Chem., March 4, 2005; 280(9): 7570 - 7580. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. K. Reiter, S. J. Crozier, S. R. Kimball, and L. S. Jefferson Meal Feeding Alters Translational Control of Gene Expression in Rat Liver J. Nutr., March 1, 2005; 135(3): 367 - 375. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Visit Other APS Journals Online |