An In Vivo Nuclear Magnetic Resonance Spectroscopic Study
M David, William A. Petit, Maren R. Laughlin, Robert G. Shulman, Judith King, Eugene J. Barrett
Abstract
M David, William A. Petit, Maren R. Laughlin, Robert G. Shulman, Judith King, Eugene J. Barrett
Abstract
Using 3C nuclear magnetic resonance spectroscopic methods we examined in vivo the synthesis of liver glycogen during the infusion of D-11-13Cjglucose and the turnover of labeled glycogen during subsequent infusion of D-11-13Cjglucose. In fasted rats the processes of glycogen synthesis and degradation were observed to occur simultaneously with the rate of synthesis > degradation leading to net glycogen synthesis. In fed rats, incorporation of infused D-[1-_3Cjglucose occurred briskly; however, over 2 h there was no net glycogen accumulated. Degradation of labeled glycogen was greater in the fed versus the fasted rats (P < 0.001), and the lack of net glycogen synthesis in fed rats was due to degradation and synthesis occurring at similar rates throughout the infusion period. There was no indication that suppression of phosphorylase a or subsequent activation of glycogen synthase was involved in modulation of the flux of tracer into liver glycogen. We conclude that in both fed and fasted rats, glycogen synthase and phosphorylase are active simultaneously and the levels of liver glycogen reached during refeeding are determined by the balance between ongoing synthetic and degrada
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Using 3C nuclear magnetic resonance spectroscopic methods we examined in vivo the synthesis of liver glycogen during the infusion of D-11-13Cjglucose and the turnover of labeled glycogen during subsequent infusion of D-11-13Cjglucose. In fasted rats the processes of glycogen synthesis and degradation were observed to occur simultaneously with the rate of synthesis > degradation leading to net glycogen synthesis. In fed rats, incorporation of infused D-[1-_3Cjglucose occurred briskly; however, over 2 h there was no net glycogen accumulated. Degradation of labeled glycogen was greater in the fed versus the fasted rats (P < 0.001), and the lack of net glycogen synthesis in fed rats was due to degradation and synthesis occurring at similar rates throughout the infusion period. There was no indication that suppression of phosphorylase a or subsequent activation of glycogen synthase was involved in modulation of the flux of tracer into liver glycogen. We conclude that in both fed and fasted rats, glycogen synthase and phosphorylase are active simultaneously and the levels of liver glycogen reached during refeeding are determined by the balance between ongoing synthetic and degrada
Key concepts: Glycogen, Glycogen phosphorylase, Glycogen branching enzyme, Glycogen synthase, Glycogenesis, Internal medicine, Glycogen debranching enzyme, Endocrinology