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Rhonda J. Wilson, Jenny E. Gusba, Deborah L. Robinson and Terry E. Graham
Am J Physiol Endocrinol Metab 292:1815-1822, 2007. First published Feb 20, 2007; doi:10.1152/ajpendo.00598.2006 You might find this additional information useful... This article cites 31 articles, 15 of which you can access free at: This article has been citedby 2 other HighWire hosted articles: Glycogenin-1 Deficiency and Inactivated Priming of Glycogen Synthesis A. R. Moslemi, C. Lindberg, J. Nilsson, H. Tajsharghi, B. Andersson and A. Oldfors N. Engl. J. Med., April 1, 2010; 362 (13): 1203-1210. [Abstract] [Full Text] [PDF] Characterization of the acute temporal changes in excisional murine cutaneous wound inflammation by screening of thewound-edge transcriptome S. Roy, S. Khanna, C. Rink, S. Biswas and C. K. Sen Physiol Genomics, July 1, 2008; 34 (2): 162-184. [Abstract] [Full Text] [PDF]
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AJP - Endocrinology and Metabolism publishes results of original studies about endocrine and metabolic systems on any level of organization. It is published 12 times a year (monthly) by the American Physiological Society, 9650 Rockville Pike, Bethesda MD20814-3991. Copyright © 2005 by the American Physiological Society. ISSN: 0193-1849, ESSN: 1522-1555. Visit our website at

Am J Physiol Endocrinol Metab 292: E1815–E1822, 2007. First published February 20, 2007; doi:10.1152/ajpendo.00598.2006.

Glycogenin protein and mRNA expression in response to changing glycogen concentration in exercise and recovery
Rhonda J.Wilson, Jenny E. Gusba, Deborah L. Robinson, and Terry E. Graham
Department of Human Health and Nutritional Sciences, University of Guelph, Guelph, Ontario, Canada
Submitted 9 November 2006; accepted in final form 16 February 2007

Wilson RJ, Gusba JE, Robinson DL, Graham TE. Glycogenin protein and mRNA expression in response to changing glycogen concentration in exercise and recovery. Am J PhysiolEndocrinol Metab 292: E1815–E1822, 2007. First published February 20, 2007; doi:10.1152/ajpendo.00598.2006.—Glycogenin (GN-1) is essential for the formation of a glycogen granule; however, rarely has it been studied when glycogen concentration changes in exercise and recovery. It is unclear whether GN-1 is degraded or is liberated and exists as apoprotein (apo)-GN-1 (unglycosylated). To examinethis, we measured GN-1 protein and mRNA level at rest, at exhaustion (EXH), and during 5 h of recovery in which the rate of glycogen restoration was influenced by carbohydrate (CHO) provision. Ten males cycled ˙ (65% VO2 max) to volitional EXH (117.8 4.2 min) on two separate occasions. Subjects were administered carbohydrate (CHO; 1 g kg 1 h 1 Gatorlode) or water [placebo (PL)] during 5 h ofrecovery. Muscle biopsies were taken at rest, at EXH, and following 30, 60, 120, and 300 min of recovery. At EXH, total glycogen concentration was reduced (P 0.05). However, GN-1 protein and mRNA content did not change. By 5 h of recovery, glycogen was resynthesized to 60% of rest in the CHO trial and remained unchanged in the PL trial. GN-1 protein and mRNA level did not increase during recovery ineither trial. We observed modest amounts of apo-GN-1 at EXH, suggesting complete degradation of some granules. These data suggest that GN-1 is conserved, possibly as very small, or nascent, granules when glycogen concentration is low. This would provide the ability to rapidly restore glycogen during early recovery. skeletal muscle; carbohydrate; exhaustion; resynthesis; recovery
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