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  • 1.
    Aronson, D.
    et al.
    Research Division, Joslin Diabetes Center, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA.
    Wojtaszewski, J.
    Copenhagen Muscle Research Center, August Krogh Institute, University of Copenhagen, Copenhagen, Denmark.
    Thorell, A.
    Department of Surgery, Karolinska Hospital and Institute, Stockholm, Sweden.
    Nygren, J.
    Department of Surgery, Karolinska Hospital and Institute, Stockholm, Sweden.
    Zangen, A.
    Research Division, Joslin Diabetes Center, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA.
    Richter, E. A.
    Copenhagen Muscle Research Center, August Krogh Institute, University of Copenhagen, Copenhagen, Denmark.
    Ljungqvist, Olle
    Department of Surgery, Karolinska Hospital and Institute, Stockholm, Sweden.
    Fielding, R. A.
    Department of Health Sciences, Sargent Coll. All. Hlth. Professions, Boston University, Boston, MA , United States.
    Goodyear, L. J.
    Research Division, Joslin Diabetes Center, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA; Joslin Diabetes Center, One Joslin Place, Boston, MA, United States.
    Extracellular-regulated protein kinase cascades are activated in response to injury in human skeletal muscle1998In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 275, no 2, p. C555-C561Article in journal (Refereed)
    Abstract [en]

    The mitogen-activated protein (MAP) kinase signaling pathways are believed to act as critical signal transducers between stress stimuli and transcriptional responses in mammalian cells. However, it is not known whether these signaling cascades also participate in the response to injury in human tissues. To determine whether injury to the vastus lateralis muscle activates MAP kinase signaling in human subjects, two needle biopsies or open muscle biopsies were taken from the same incision site 30-60 min apart. The muscle biopsy procedures resulted in striking increases in dual phosphorylation of the extracellular-regulated kinases (ERK1 and ERK2) and in activity of the downstream substrate, the p90 ribosomal S6 kinase. Raf-1 kinase and MAP kinase kinase, upstream activators of ERK, were also markedly stimulated in all subjects. In addition, c-Jun NH2-terminal kinase and p38 kinase, components of two parallel MAP kinase pathways, were activated following muscle injury. The stimulation of the three MAP kinase cascades was present only in the immediate vicinity of the injury, a finding consistent with a local rather than systemic activation of these signaling cascades in response to injury. These data demonstrate that muscle injury induces the stimulation of the three MAP kinase cascades in human skeletal muscle, suggesting a physiological relevance of these protein kinases in the immediate response to tissue injury and possibly in the initiation of wound healing.

  • 2. Balagopal, P.
    et al.
    Ljungqvist, Olle
    Dept. of Surgery, Karolinska Institute and Hospital, Stockholm, Sweden.
    Nair, K. S.
    Endocrine Research Unit, Mayo Clinic and Foundation, Rochester, MN, United States.
    Skeletal muscle heavy-chain synthesis rate in healthy humans1997In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 272, no 1, p. 45-50Article in journal (Refereed)
    Abstract [en]

    Mixed muscle protein synthetic rate has been measured in humans. These measurements represent the average of synthetic rates of all muscle proteins with variable rates. We determined to what extent the synthesis rate of mixed muscle protein in humans reflects that of myosin heavy chain (MHC), the main contractile protein responsible for the conversion of ATP to mechanical energy as muscle contraction. Fractional synthetic rates of MHC and mixed muscle protein were measured from the increment of [C-13]leucine in these proteins in vastus lateralis biopsy samples taken at 5 and 10 h during a primed continuous infusion of L-[1-C-13]leucine in 10 young healthy subjects. Calculations were done by use of plasma [C-13]ketoisocaproate (KIC) and muscle tissue fluid [C-13]leucine as surrogate measures of leucyl-tRNA. Fractional synthetic rate of MHC with plasma KIC (0.0299 +/- 0.0043%/h) and tissue fluid leucine (0.0443 +/- 0.0056%/h) were only 72 +/- 3% of that of mixed muscle protein (0.0408 +/- 0.0032 and 0.0603 +/- 0.0059%/h, respectively, with KIC and tissue fluid leucine). Contribution of MHC (7 +/- 1 mg . kg(-1) . h(-1)) to synthetic rates of whole body mixed muscle protein (36 +/- 5 mg . kg(-1) . h(-1)) and whole body protein (127 +/- 4 mg . kg(-1) . h(-1)) is only 18 +/- 1 and 5 +/- 1%, respectively. This relatively low contribution of MHC to whole body and mixed muscle protein synthesis warrants direct measurement of synthesis rate of MHC in conditions involving abnormalities of muscle contractile function.

  • 3.
    Ljungqvist, Olle
    et al.
    Örebro University, School of Medical Sciences. Departments of Surgery, Karolinska Hospital/Institute, Stockholm, Sweden.
    Boija, Per Olov
    Departments of Surgery, Karolinska Hospital/Institute, Stockholm, Sweden.
    Esahili, A. H.
    Departments of Surgery, Karolinska Hospital/Institute, Stockholm, Sweden.
    Larsson, Magnus
    Departments of Surgery, Karolinska Hospital/Institute, Stockholm, Sweden.
    Ware, James
    Departments of Surgery, Karolinska Hospital/Institute, Stockholm, Sweden.
    Food deprivation alters liver glycogen metabolism and endocrine responses to hemorrhage1990In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 259, no 5 Part 1, p. E692-E698Article in journal (Refereed)
    Abstract [en]

    Liver glycogen content, blood glucose, insulin, glucagon, and epinephrine were determined during 1 h hemorrhagic hypotension at 60 mmHg and 23 h thereafter in fed and two groups of 24-h food-deprived rats receiving either no infusion or 30% glucose intravenously during hemorrhage. Liver glycogen content was reduced by greater than 90% after 24-h food deprivation. Fed and food-deprived rats given glucose developed similar and substantial elevations of blood glucose during hemorrhage, whereas changes in blood glucose were modest in food-deprived rats given no infusion. In fed rats, liver glycogen was reduced by 60% during the 1-h bleed, but within 2 h after hemorrhage repletion of liver glycogen content commenced. By 6 h, approximately 75% of the glycogen lost during hemorrhage had been restored, and 23 h after hemorrhage liver glycogen content was six times greater compared with nonbled controls. Although glycogen levels increased after hemorrhage in food-deprived animals, the increase was negligible compared with that found in fed rats. Infusion of glucose during hemorrhage or adrenergic blockade after hemorrhage did not alter glycogen repletion in food-deprived rats. Posthemorrhage fed animals had high levels of insulin, glucagon, and epinephrine during hemorrhage, whereas insulin levels remained low in food-deprived rats despite exogenously induced hyperglycemia. It is concluded that rapid and substantial glycogen repletion can occur even immediately poststress. The conditions seem to be related to the nutritional state at the time of the insult.

  • 4.
    Ljungqvist, Olle
    et al.
    Department of Medicine, University of Vermont, Burlington, Vermont, VT, United States.
    Persson, M.
    Endocrine Research Unit, Division of Endocrinology and Metabolism, Mayo Clinic and Mayo Foundation, Rochester, MN, United States.
    Ford, G. C.
    Endocrine Research Unit, Division of Endocrinology and Metabolism, Mayo Clinic and Mayo Foundation, Rochester, MN, United States.
    Nair, K. S.
    Endocrine Research Unit, Division of Endocrinology and Metabolism, Mayo Clinic and Mayo Foundation, Rochester, MN, United States.
    Functional heterogeneity of leucine pools in human skeletal muscle1997In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 273, no 3 Pt 1, p. E564-E570Article in journal (Refereed)
    Abstract [en]

    Current models to measure muscle protein synthesis in humans assume a homogeneous intracellular amino acid pool. This assumption was tested by measuring the isotopic enrichment of leucine and its transamination product alpha-ketoisocaproate (KIC) in plasma and muscle tissue fluid and comparing them with that of leucyl-tRNA during a continuous infusion of L-[1-13C]leucine in 12 healthy subjects. Six subjects were studied twice while drinking a carbohydrate (0.42 kcal/kg) drink every 20 min for 11 h or the same volume of water. Six others took an isocaloric mixed meal providing 14 mg protein/kg every 20 min and water. Enrichment of plasma and tissue fluid KIC and plasma leucine was consistently higher than that of leucyl-tRNA and tissue fluid leucine (P < 0.01), whereas the enrichment of leucyl-tRNA was equivalent to that of tissue fluid leucine in all experiments. Furthermore, the ratio of enrichment of leucyl-tRNA to that of plasma leucine and KIC decreased after the mixed meal, whereas that of leucyl-tRNA to tissue fluid leucine remained constant. The enrichment of KIC was closer (approximately 17% lower) to that of plasma leucine than that of leucyl-tRNA (approximately 43% higher), indicating that the transamination pool derived more leucine from extracellular sources than the acylation pool. We conclude that the use of plasma KIC enrichment as a surrogate measure of leucyl-tRNA enrichment substantially underestimates muscle protein synthetic rates in humans, whereas tissue fluid leucine enrichment is a valid surrogate measure. In addition, the differences in enrichment of leucyl-tRNA and KIC support a regulated cytoplasmic trafficking of leucine in muscle cells.

  • 5.
    Ljungqvist, Olle
    et al.
    Örebro University, School of Medical Sciences. Department of Medicine, University of Vermont, Burlington VT, United States; Department of Surgery, Karolinska Institute, Karolinska Hospital, Stockholm, Sweden.
    Persson, Mai
    Endocrine Research Unit, Div. of Endocrinology and Metabolism, Mayo Clinic and Mayo Foundation, Rochester MN, United States.
    Ford, Godfrey Charles
    Endocrine Research Unit, Div. of Endocrinology and Metabolism, Mayo Clinic and Mayo Foundation, Rochester MN, United States.
    Nair, Sreekumaran
    Endocrine Research Unit, Div. of Endocrinology and Metabolism, Mayo Clinic and Mayo Foundation, Rochester MN, United States; Mayo Clinic, Rochester MN, United States.
    Functional heterogeneity of intracellular leucine pools in human skeletal muscle1997In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 273, no 3, p. E564-E570Article in journal (Refereed)
    Abstract [en]

    Current models to measure muscle protein synthesis in humans assume a homogeneous intracellular amino acid pool. This assumption was tested by measuring the isotopic enrichment of leucine and its transamination product alpha-ketoisocaproate (KIC) in plasma and muscle tissue fluid and comparing them with that of leucyl-tRNA during a continuous infusion of L-[1-13C]leucine in 12 healthy subjects. Six subjects were studied twice while drinking a carbohydrate (0.42 kcal/kg) drink every 20 min for 11 h or the same volume of water. Six others took an isocaloric mixed meal providing 14 mg protein/kg every 20 min and water. Enrichment of plasma and tissue fluid KIC and plasma leucine was consistently higher than that of leucyl-tRNA and tissue fluid leucine (P < 0.01), whereas the enrichment of leucyl-tRNA was equivalent to that of tissue fluid leucine in all experiments. Furthermore, the ratio of enrichment of leucyl-tRNA to that of plasma leucine and KIC decreased after the mixed meal, whereas that of leucyl-tRNA to tissue fluid leucine remained constant. The enrichment of KIC was closer (approximately 17% lower) to that of plasma leucine than that of leucyl-tRNA (approximately 43% higher), indicating that the transamination pool derived more leucine from extracellular sources than the acylation pool. We conclude that the use of plasma KIC enrichment as a surrogate measure of leucyl-tRNA enrichment substantially underestimates muscle protein synthetic rates in humans, whereas tissue fluid leucine enrichment is a valid surrogate measure. In addition, the differences in enrichment of leucyl-tRNA and KIC support a regulated cytoplasmic trafficking of leucine in muscle cells.

  • 6.
    McNurlan, Margaret A.
    et al.
    Rowett Research Institute, Aberdeen, United Kingdom..
    Essén, Pia
    Thorell, Anders
    Calder, A. Graham
    Andersson, S. E.
    Ljungqvist, Olle
    Örebro University, School of Medical Sciences.
    Sandgren, Anna
    Grant, Ian
    Tjäder, Inga
    Ballmer, Peter E.
    Wernerman, Jan
    Garlick, Peter J.
    Response of protein synthesis in human skeletal muscle to insulin: an investigation with L[2H5]phenylalanine1994In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 67, no Part 1, p. E102-E108Article in journal (Refereed)
    Abstract [en]

    The role of insulin in the regulation of muscle protein synthesis in adult humans has been investigated with intravenous infusion of insulin at levels comparable with those observed after normal feeding. Glucose was also infused to maintain euglycemia. Muscle protein synthesis was measured in six healthy subjects before and during insulin and glucose infusion from the incorporation of L-[H-2(5)]phenylalanine into the protein of vastus lateralis sampled by percutaneous biopsy. L-[H-2(5)]phenylalanine was given as a single injection of a flooding amount (45 mg/kg). The relatively low levels of enrichment of phenylalanine in protein (0.005 atom%) were measured by modified gas chromatography-mass spectrometry and verified by comparison with incorporation of L-[2,6-H-3]phenylalanine. Similarity of enrichment in tissue-free and plasma pools (flooding) and linear incorporation over the period of measurement were also verified. The fractional rate of muscle protein synthesis in the group of postabsorptive subjects was 1.65 +/- 0.11% (SE)/day. The rate was unaltered by insulin and glucose infusion, 1.66 +/- 0.16%/day.

  • 7.
    Nygren, Jonas O.
    et al.
    Department of Surgery, Karolinska Hospital, Stockholm, Sweden.
    Thorell, Anders
    Department of Surgery, Karolinska Hospital, Stockholm, Sweden; Huddinge Univ. Hospital, Huddinge, Sweden.
    Soop, Mattias
    Department of Surgery, Karolinska Hospital, Stockholm, Sweden.
    Efendic, Suad
    Dept. Endocrinology and Diabetes, Karolinska Hospital, Stockholm, Sweden.
    Brismar, Kerstin E.
    Dept. Endocrinology and Diabetes, Karolinska Hospital, Stockholm, Sweden.
    Karpe, Fredrik
    Gustaf V Research Institute, Karolinska Hospital, Stockholm, Sweden.
    Nair, K. Sreekumaran
    Endocrine Research Unit, Mayo Clinic, Rochester MN, United States.
    Ljungqvist, Olle
    Örebro University, School of Medical Sciences. Department of Surgery, Karolinska Hospital, Stockholm, Sweden; .
    Perioperative insulin and glucose infusion maintains normal insulin sensitivity after surgery1998In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 275, no 1 Part 1, p. E140-E148Article in journal (Refereed)
    Abstract [en]

    Elective surgery was performed after overnight fasting, a routine that may affect the metabolic response to surgery. We investigated the effects of insulin and glucose infusions before and during surgery on postoperative substrate utilization and insulin sensitivity. Seven patients were given insulin and glucose infusions 3 h before and during surgery (insulin group), and a control group of six patients underwent surgery after fasting overnight. Insulin sensitivity and glucose kinetics (D-[6,6-2H2]glucose) were measured before and immediately after surgery using a hyperinsulinemic, normoglycemic clamp. Glucose infusion rates and whole body glucose disposal decreased after surgery in the control group (-40 and -29%, respectively), whereas no significant change was found in the insulingroup (+16 and +25%). Endogenous glucose production remained unchanged in both groups. Postoperative changes in cortisol, glucagon, fat oxidation, and free fatty acids were attenuated in the insulin group (vs. control). We conclude that perioperative insulin and glucose infusions minimize the endocrine stress response and normalize postoperative insulin sensitivity and substrate utilization.

  • 8.
    Soop, M.
    et al.
    Department of Surgery, Karolinska Hospital, Stockholm, Sweden.
    Nygren, J.
    Centre of Gastrointestinal Disease, Karolinska Institutet at Ersta Hospital, Stockholm, Sweden.
    Myrenfors, P.
    Department of Anesthesia, Karolinska Hospital, Stockholm, Sweden.
    Thorell, A.
    Centre of Gastrointestinal Disease, Karolinska Institutet at Ersta Hospital, Stockholm, Sweden.
    Ljungqvist, Olle
    Centre of Gastrointestinal Disease, Karolinska Institutet at Ersta Hospital, Stockholm, Sweden.
    Preoperative oral carbohydrate treatment attenuates immediate postoperative insulin resistance2001In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 280, no 4, p. E576-E583Article in journal (Refereed)
  • 9.
    Thorell, Anders
    et al.
    Department of Surgery, Huddinge University Hospital, Huddinge, Sweden.
    Hirshman, Michael F.
    Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston MA, United States.
    Nygren, Jonas O.
    Department of Surgery, Karolinska Hospital, Karolinska Institute, Stockholm, Sweden.
    Jorfeldt, Lennart Sven
    Department of Thorac. Clinical Physiology, Karolinska Hospital, Karolinska Institute, Stockholm, Sweden.
    Wojtaszewski, Jörgen F. P.
    Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston MA, United States;.
    Dufresne, Scott D.
    Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston MA, United States.
    Horton, Edward S.
    Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston MA, United States.
    Ljungqvist, Olle
    Örebro University, School of Medical Sciences. Department of Surgery, Huddinge University Hospital, Huddinge, Sweden.
    Goodyear, Laurie J.
    Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston MA, United States; Metabolism Section, Joslin Diabetes Center, Boston MA, United States.
    Exerciseand insulin cause GLUT-4 translocation in human skeletal muscle1999In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 277, no 4, p. E733-E741Article in journal (Refereed)
    Abstract [en]

    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 translocationphenomenon 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(2max)), 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 inresponse 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 ~56 μU/ml, cause GLUT-4 translocation and Akt phosphorylation in human skeletal muscle.

  • 10.
    Thorell, Anders
    et al.
    Departments of Surgery, Huddinge University Hospital, Stockholm, Sweden; Department of Surgery, Huddinge University Hospital, Huddinge, Sweden.
    Nygren, Jonas
    Departments of Surgery, Karolinska University Hospital, Karolinska Institute, Stockholm, Sweden.
    Hirshman, Michael F.
    Joslin Diabetes Center, Harvard Medical School, Boston MA, United States.
    Nair, K. Sreekumaran
    Div. of Endocrinology and Metabolism, Mayo Clinic, Rochester MN, United States.
    Hayashi, Tatsuya
    Joslin Diabetes Center, Harvard Medical School, Boston MA, United States.
    Horton, Edward S.
    Joslin Diabetes Center, Harvard Medical School, Boston MA, United States.
    Goodyear, Laurie J.
    Div. of Endocrinology and Metabolism, Mayo Clinic, Rochester MN , United States.
    Ljungqvist, Olle
    Örebro University, School of Medical Sciences. Departments of Surgery, Huddinge University Hospital, Stockholm, Sweden.
    Surgery-induced insulin resistance in human patients relations to glucoseutilization and transport1999In: American Journal of Physiology, ISSN 0002-9513, E-ISSN 2163-5773, Vol. 276, no 4, p. E754-E761Article in journal (Refereed)
    Abstract [en]

    To investigate the underlying molecular mechanisms for surgery-induced insulin resistance in skeletal muscle, six otherwise healthy patients undergoing total hip replacement were studied before, during, and after surgery. Patients were studied under basal conditions and during physiological hyperinsulinemia (60 microU/ml). Biopsies of vastus lateralis muscle were used to measure GLUT-4 translocation, glucose transport, and glycogen synthase activities. Surgery reduced insulin-stimulated glucose disposal (P < 0.05) without altering the insulin-stimulated increase in glucose oxidation or suppression of endogenous glucose production. Preoperatively, insulin infusion increased plasma membrane GLUT-4 in all six subjects (P < 0.05), whereas insulin-stimulated GLUT-4 translocation only occurred in three patientspostoperatively (not significant). Moreover, nonoxidative glucose disposal rates and basal levels of glycogen synthase activities in muscle were reduced postoperatively (P < 0.05). These findings demonstrate that peripheral insulin resistance develops immediately postoperatively and that this condition might be associated with perturbations in insulin-stimulated GLUT-4 translocation as well as nonoxidative glucose disposal, presumably at the level of glycogen synthesis.

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