Okubo M, Bogardus C, Lillioja S, Mott D M
Clinical Diabetes and Nutrition Section, National Institute of Diabetes and Digestive and Kidney Diseases, Phoenix, AZ 85016.
Metabolism. 1988 Dec;37(12):1171-6. doi: 10.1016/0026-0495(88)90196-5.
The influence of glucose-6-phosphate (glucose-6-P) on skeletal muscle glycogen synthase phosphatase was examined in normal glucose-tolerant Southwest American Indians. Phosphatase was stimulated with physiological concentrations of glucose-6-P and inhibited by ATP (5 mmol/L) and glycogen (0.1%). Phosphatase activity was measured before and after insulin infusion using the euglycemic clamp technique. Although glycogen synthase fractional activity increased in all subjects, this increase was not related to a change in phosphatase activity in the absence or presence of glucose-6-P. These results suggest that glycogen synthase phosphatase from human muscle can be regulated by physiological concentrations of glucose-6-P, ATP, and glycogen, and that insulin does not alter glucose-6-P stimulation of the enzyme in normal subjects.
在糖耐量正常的美国西南部印第安人中，研究了6-磷酸葡萄糖（glucose-6-P）对骨骼肌糖原合酶磷酸酶的影响。用生理浓度的6-磷酸葡萄糖刺激磷酸酶，并被ATP（5 mmol/L）和糖原（0.1%）抑制。使用正常血糖钳夹技术在输注胰岛素前后测量磷酸酶活性。尽管所有受试者的糖原合酶分数活性均增加，但这种增加与在有或没有6-磷酸葡萄糖存在的情况下磷酸酶活性的变化无关。这些结果表明，人肌肉中的糖原合酶磷酸酶可受6-磷酸葡萄糖、ATP和糖原的生理浓度调节，并且胰岛素不会改变正常受试者中该酶对6-磷酸葡萄糖的刺激作用。
