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1 Department of Human Biology and Nutritional Sciences, University of Guelph, Guelph N1G 2W1; and 2 Department of Medicine and Kinesiology, McMaster University. Hamilton, Ontario, Canada L8N 3Z5
The de novo biosynthesis of
glycogen is catalyzed by glycogenin, a self-glucosylating protein
primer. To date, the role of glycogenin in regulating glycogen
metabolism and the attainment of maximal glycogen levels in skeletal
muscle are unknown. We measured glycogenin activity after enzymatic
removal of glucose by
-amylase, an indirect measure of glycogenin
amount. Seven male subjects performed an exercise and dietary protocol
that resulted in one high-carbohydrate leg (HL) and one
low-carbohydrate leg (LL) before testing. Resting muscle biopsies were
obtained and analyzed for total glycogen, proglycogen (PG),
macroglycogen (MG), and glycogenin activity. Results showed differences
(P < 0.05) between HL and LL for total glycogen (438.0 ± 69.5 vs. 305.7 ± 57.4 mmol glucosyl units/kg dry wt) and PG
(311.4 ± 38.1 vs. 227.3 ± 33.1 mmol glucosyl units/kg dry wt). A
positive correlation between total muscle glycogen content and
glycogenin activity (r = 0.84, P < 0.001) was
observed. Similar positive correlations (P < 0.05) were also
evident between both PG and MG concentration and glycogenin activity
(PG, r = 0.82; MG, r = 0.84). It can be concluded that
glycogenin does display activity in human skeletal muscle and is
proportional to glycogen concentration. Thus it must be considered as a
potential regulator of glycogen synthesis in human skeletal muscle.
glycogen metabolism; proglycogen; macroglycogen; carbohydrate loading; carbohydrate synthesis
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