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• W1981671891 endingPage "4916" @default.
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• W1981671891 abstract "Previous work suggests that normal GLUT4 content is sufficient for increases in muscle glucose uptake (MGU) during hyperinsulinemia, because glucose phosphorylation is the more formidable barrier to insulin-stimulated MGU. It was hypothesized that a partial ablation of GLUT4 would not impair insulin-stimulated MGU when glucose phosphorylation capacity is normal but would do so when glucose phosphorylation capacity is increased. Thus, chow-fed C57BL/6J mice with a GLUT4 partial knockout (GLUT4+/–), hexokinase II overexpression (HKTg), or both (HKTg + GLUT4+/–) and wild-type littermates were studied. Carotid artery and jugular vein catheters were implanted for sampling and infusions at 4 months of age. After a 5-d recovery, 5-h fasted mice (n = 8–11/group) underwent a 120-min saline infusion or insulin clamp (4 mU/kg·min insulin with glucose maintained at 165 mg/dl) and received a 2-deoxy[3H]glucose bolus to provide an index of MGU (Rg) for the soleus, gastrocnemius, and superficial vastus lateralis. Basal Rg from all muscles studied from saline-infused mice were not changed by any of the genetic modifications. HKTg mice had augmented insulin-stimulated Rg in all muscles studied compared with remaining genotypes. Insulin-stimulated Rg was not impaired in any of the muscles studied from GLUT4+/– mice. However, the enhanced insulin-stimulated Rg created by HK overexpression was ablated in HKTg + GLUT4+/– mice. Thus, a 50% reduction of normal GLUT4 content in the presence of normal HK activity does not impair insulin-stimulated MGU. However, when the glucose phosphorylation barrier is lowered by HK overexpression, GLUT4 availability becomes a limitation to insulin-stimulated MGU." @default.
• W1981671891 created "2016-06-24" @default.
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• W1981671891 date "2004-11-01" @default.
• W1981671891 modified "2023-10-12" @default.
• W1981671891 title "Regulation of Insulin-Stimulated Muscle Glucose Uptake in the Conscious Mouse: Role of Glucose Transport Is Dependent on Glucose Phosphorylation Capacity" @default.
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• W1981671891 doi "https://doi.org/10.1210/en.2004-0465" @default.
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