title: Exercise and insulin cause GLUT-4 translocation in human skeletal muscle.
abstract: Studies in rodents have established that GLUT-4 translocation is the major mechanism by which insulin and exercise increase glucose uptake in skeletal muscle. In contrast, much less is known about the translocation phenomenon in human skeletal muscle. In the current study, nine healthy volunteers were studied on two different days. On one day, biopsies of vastus lateralis muscle were taken before and after a 2-h euglycemic-hyperinsulinemic clamp (0.8 mU. kg(-1). min(-1)). On another day, subjects exercised for 60 min at 70% of maximal oxygen consumption (VO(2 max)), a biopsy was obtained, and the same clamp and biopsy procedure was performed as that during the previous experiment. Compared with insulin treatment alone, glucose infusion rates were significantly increased during the postexercise clamp for the periods 0-30 min, 30-60 min, and 60-90 min, but not during the last 30 min of the clamp. Plasma membrane GLUT-4 content was significantly increased in response to physiological hyperinsulinemia (32% above rest), exercise (35%), and the combination of exercise plus insulin (44%). Phosphorylation of Akt, a putative signaling intermediary for GLUT-4 translocation, was increased in response to insulin (640% above rest), exercise (280%), and exercise plus insulin (1,000%). These data demonstrate that two normal physiological conditions, moderate intensity exercise and physiological hyperinsulinemia approximately 56 microU/ml, cause GLUT-4 translocation and Akt phosphorylation in human skeletal muscle.
authors.affiliation: Department of Surgery, Huddinge University Hospital, S-141 86 Huddinge,Sweden.
authors.forename: A
authors.initials: A
authors.lastname: Thorell
authors.forename: M F
authors.initials: MF
authors.lastname: Hirshman
authors.forename: J
authors.initials: J
authors.lastname: Nygren
authors.forename: L
authors.initials: L
authors.lastname: Jorfeldt
authors.forename: J F
authors.initials: JF
authors.lastname: Wojtaszewski
authors.forename: S D
authors.initials: SD
authors.lastname: Dufresne
authors.forename: E S
authors.initials: ES
authors.lastname: Horton
authors.forename: O
authors.initials: O
authors.lastname: Ljungqvist
authors.forename: L J
authors.initials: LJ
authors.lastname: Goodyear
mesh_terms: D000328:Adult; D001692:Biological Transport / Q000187:drug effects / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D015444:Exercise / Q000502:physiology*; D005260:Female; D005947:Glucose / Q000378:metabolism / Q000494:pharmacology; D051275:Glucose Transporter Type 4; D006003:Glycogen / Q000378:metabolism; D006801:Humans; D007328:Insulin / Q000378:metabolism / Q000494:pharmacology*; D019344:Lactic Acid / Q000378:metabolism; D008297:Male; D009004:Monosaccharide Transport Proteins / Q000378:metabolism*; D009124:Muscle Proteins; D018482:Muscle, Skeletal / Q000187:drug effects / Q000378:metabolism*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D051057:Proto-Oncogene Proteins c-akt
chemical_list: D051275:Glucose Transporter Type 4; D007328:Insulin; D009004:Monosaccharide Transport Proteins; D009124:Muscle Proteins; D011518:Proto-Oncogene Proteins; C495692:SLC2A4 protein, human; D019344:Lactic Acid; D006003:Glycogen; C494918:AKT1 protein, human; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt; D005947:Glucose