Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes

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Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes. / Vestergaard, H; Andersen, P H; Lund, S; Schmitz, O; Junker, S; Pedersen, O.

In: American Journal of Physiology (Consolidated), Vol. 266, No. 1 Pt 1, 01.1994, p. E92-101.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Vestergaard, H, Andersen, PH, Lund, S, Schmitz, O, Junker, S & Pedersen, O 1994, 'Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes', American Journal of Physiology (Consolidated), vol. 266, no. 1 Pt 1, pp. E92-101.

APA

Vestergaard, H., Andersen, P. H., Lund, S., Schmitz, O., Junker, S., & Pedersen, O. (1994). Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes. American Journal of Physiology (Consolidated), 266(1 Pt 1), E92-101.

Vancouver

Vestergaard H, Andersen PH, Lund S, Schmitz O, Junker S, Pedersen O. Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes. American Journal of Physiology (Consolidated). 1994 Jan;266(1 Pt 1):E92-101.

Author

Vestergaard, H ; Andersen, P H ; Lund, S ; Schmitz, O ; Junker, S ; Pedersen, O. / Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes. In: American Journal of Physiology (Consolidated). 1994 ; Vol. 266, No. 1 Pt 1. pp. E92-101.

Bibtex

@article{e094888b63264d019aee36c0d97e820c,
title = "Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes",
abstract = "Expression of muscle-specific glycogen synthase (GS) and phosphofructokinase (PFK) was analyzed in seven athletes and eight control subjects who were characterized using the euglycemic, hyperinsulinemic (2 mU.kg-1.min-1) clamp technique in combination with indirect calorimetry and biopsy sampling of vastus lateralis muscle. In the basal state, total GS activity and half-maximal GS activation by glucose 6-phosphate (G-6-P) were respectively 34% (P < 0.03) and 50% (P < 0.005) higher in athletes than in control subjects. In parallel, GS mRNA/microgram total RNA in athletes was 40% (P < 0.005) higher. No difference in GS immunoreactive protein abundance was found between the groups. PFK activity and protein levels were respectively 15% (P < 0.05) and 20% (P < 0.02) lower in athletes, whereas no differences was found in the level of PFK mRNA. After 4 h of hyperinsulinemia, total glucose disposal rate (P < 0.005) and both nonoxidative (P < 0.02) and oxidative (P < 0.03) glucose metabolism were significantly higher in athletes. In parallel, after hyperinsulinemia, the relative activation of GS by G-6-P was significantly higher in athletes, whereas total activity and gene expression of both GS and PFK were unaffected by insulin. We conclude that athletes have increased whole body insulin-stimulated nonoxidative glucose metabolism associated with both pretranslational (mRNA) and posttranslational (enzyme activity) upregulation of GS. However, the immunoreactive mass of GS is normal, emphasizing that posttranslational regulation of the GS protein activity is important for the increased glycogen synthesis rate of muscle in endurance-trained individuals.",
keywords = "Adult, Glucose, Glucose Clamp Technique, Glycogen Synthase, Humans, Hyperinsulinism, Lipid Metabolism, Male, Muscles, Phosphofructokinase-1, Protein Processing, Post-Translational, RNA, Messenger, Sports, Up-Regulation",
author = "H Vestergaard and Andersen, {P H} and S Lund and O Schmitz and S Junker and O Pedersen",
year = "1994",
month = jan,
language = "English",
volume = "266",
pages = "E92--101",
journal = "American Journal of Physiology - Cell Physiology",
issn = "0363-6143",
publisher = "American Physiological Society",
number = "1 Pt 1",

}

RIS

TY - JOUR

T1 - Pre- and posttranslational upregulation of muscle-specific glycogen synthase in athletes

AU - Vestergaard, H

AU - Andersen, P H

AU - Lund, S

AU - Schmitz, O

AU - Junker, S

AU - Pedersen, O

PY - 1994/1

Y1 - 1994/1

N2 - Expression of muscle-specific glycogen synthase (GS) and phosphofructokinase (PFK) was analyzed in seven athletes and eight control subjects who were characterized using the euglycemic, hyperinsulinemic (2 mU.kg-1.min-1) clamp technique in combination with indirect calorimetry and biopsy sampling of vastus lateralis muscle. In the basal state, total GS activity and half-maximal GS activation by glucose 6-phosphate (G-6-P) were respectively 34% (P < 0.03) and 50% (P < 0.005) higher in athletes than in control subjects. In parallel, GS mRNA/microgram total RNA in athletes was 40% (P < 0.005) higher. No difference in GS immunoreactive protein abundance was found between the groups. PFK activity and protein levels were respectively 15% (P < 0.05) and 20% (P < 0.02) lower in athletes, whereas no differences was found in the level of PFK mRNA. After 4 h of hyperinsulinemia, total glucose disposal rate (P < 0.005) and both nonoxidative (P < 0.02) and oxidative (P < 0.03) glucose metabolism were significantly higher in athletes. In parallel, after hyperinsulinemia, the relative activation of GS by G-6-P was significantly higher in athletes, whereas total activity and gene expression of both GS and PFK were unaffected by insulin. We conclude that athletes have increased whole body insulin-stimulated nonoxidative glucose metabolism associated with both pretranslational (mRNA) and posttranslational (enzyme activity) upregulation of GS. However, the immunoreactive mass of GS is normal, emphasizing that posttranslational regulation of the GS protein activity is important for the increased glycogen synthesis rate of muscle in endurance-trained individuals.

AB - Expression of muscle-specific glycogen synthase (GS) and phosphofructokinase (PFK) was analyzed in seven athletes and eight control subjects who were characterized using the euglycemic, hyperinsulinemic (2 mU.kg-1.min-1) clamp technique in combination with indirect calorimetry and biopsy sampling of vastus lateralis muscle. In the basal state, total GS activity and half-maximal GS activation by glucose 6-phosphate (G-6-P) were respectively 34% (P < 0.03) and 50% (P < 0.005) higher in athletes than in control subjects. In parallel, GS mRNA/microgram total RNA in athletes was 40% (P < 0.005) higher. No difference in GS immunoreactive protein abundance was found between the groups. PFK activity and protein levels were respectively 15% (P < 0.05) and 20% (P < 0.02) lower in athletes, whereas no differences was found in the level of PFK mRNA. After 4 h of hyperinsulinemia, total glucose disposal rate (P < 0.005) and both nonoxidative (P < 0.02) and oxidative (P < 0.03) glucose metabolism were significantly higher in athletes. In parallel, after hyperinsulinemia, the relative activation of GS by G-6-P was significantly higher in athletes, whereas total activity and gene expression of both GS and PFK were unaffected by insulin. We conclude that athletes have increased whole body insulin-stimulated nonoxidative glucose metabolism associated with both pretranslational (mRNA) and posttranslational (enzyme activity) upregulation of GS. However, the immunoreactive mass of GS is normal, emphasizing that posttranslational regulation of the GS protein activity is important for the increased glycogen synthesis rate of muscle in endurance-trained individuals.

KW - Adult

KW - Glucose

KW - Glucose Clamp Technique

KW - Glycogen Synthase

KW - Humans

KW - Hyperinsulinism

KW - Lipid Metabolism

KW - Male

KW - Muscles

KW - Phosphofructokinase-1

KW - Protein Processing, Post-Translational

KW - RNA, Messenger

KW - Sports

KW - Up-Regulation

M3 - Journal article

C2 - 8304448

VL - 266

SP - E92-101

JO - American Journal of Physiology - Cell Physiology

JF - American Journal of Physiology - Cell Physiology

SN - 0363-6143

IS - 1 Pt 1

ER -

ID: 150332793