Effects of contraction and insulin on protein synthesis, AMP-activated protein kinase and phosphorylation state of translation factors in rat skeletal muscle

@article{Miranda2007EffectsOC,
  title={Effects of contraction and insulin on protein synthesis, AMP-activated protein kinase and phosphorylation state of translation factors in rat skeletal muscle},
  author={Lisa Miranda Miranda and Sandrine Horman and Isabelle Y. De Potter and Louis Hue and Jorgen Jensen and Mark H. Rider},
  journal={Pfl{\"u}gers Archiv - European Journal of Physiology},
  year={2007},
  volume={455},
  pages={1129-1140}
}
In rat epitrochlearis skeletal muscle, contraction inhibited the basal and insulin-stimulated rates of protein synthesis by 75 and 70%, respectively, while increasing adenosine monophosphate-activated protein kinase (AMPK) activity. Insulin, on the other hand, stimulated protein synthesis (by 30%) and increased p70 ribosomal protein S6 kinase (p70S6K) Thr389, 40S ribosomal protein S6 (rpS6) Ser235/236, rpS6 Ser240/244 and eukaryotic initiation factor-4E-binding protein-1 (4E-BP1) Thr37/46… Expand
Mammalian target of rapamycin-independent S6K1 and 4E-BP1 phosphorylation during contraction in rat skeletal muscle.
TLDR
The results indicate mTOR-independent phosphorylation of S6K1 and 4E-BP1 and suggest MEK/ERK/RSK1-dependent phosphorylated of eIF4B during skeletal muscle contraction, which would keep the translation initiation machinery "primed" in an active state so that protein synthesis could quickly resume post-exercise. Expand
A novel PKB/Akt inhibitor, MK-2206, effectively inhibits insulin-stimulated glucose metabolism and protein synthesis in isolated rat skeletal muscle.
TLDR
A key role for PKB is found in mediating insulin-stimulated glucose uptake, glycogen synthesis and protein synthesis in skeletal muscle, and MK-2206, rather than Akti, would be the tool of choice for studying the role of PKB in insulin action in skeletal Muscle. Expand
Direct and indirect activation of eukaryotic elongation factor 2 kinase by AMP-activated protein kinase.
TLDR
This study provides new insights into the control of eEF2K by AMPK, with implications for linking metabolic stress to decreased protein synthesis to conserve energy reserves, a pathway that is of major importance in cancer cell survival. Expand
Lipid-induced mTOR activation in rat skeletal muscle reversed by exercise and 5'-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside.
TLDR
The data implicates reductions in mTOR complex activation with the reversal of lipid-induced skeletal muscle insulin resistance in response to exercise training or AICAR and identifies mTOR as a potential target for the treatment of insulin resistance. Expand
A Ca2+–calmodulin–eEF2K–eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions
TLDR
In fast‐twitch skeletal muscle, the inhibition of eEF2 activity by phosphorylation downstream of Ca2+–CaM–eEF2K signalling partially contributes to the suppression of protein synthesis during exercise/contractions. Expand
Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type.
TLDR
Data suggest that the depression of skeletal muscle protein synthesis with endurance-type exercise may be regulated at both initiation and elongation steps, with eEF2 phosphorylation contributing at all exercise intensities but 4EBP1 dephosphorylation contribute to a greater extent at high vs. low exercise intensITIES. Expand
AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase.
TLDR
The results suggest that GYS inactivation by AMPK activators in hepatocytes is due to GYS2 Ser7 phosphorylation, which lies in a favourable consensus forosphorylation by AM PK. Expand
Quantitative phosphoproteomics reveals novel phosphorylation events in insulin signaling regulated by protein phosphatase 1 regulatory subunit 12A.
TLDR
The results indicate that PPP1R12A indeed plays a role in skeletal muscle insulin signaling, providing novel insights into the biology of insulin action, and identify a large number of potential new substrates of serine/threonine protein phosphatase 1. Expand
Phosphorylation of translation factors in response to anoxia in turtles, Trachemys scripta elegans: role of the AMP-activated protein kinase and target of rapamycin signalling pathways
TLDR
The changes in phosphorylation state of translation factors suggest that organ-specific patterns of signalling and response are involved in achieving the anoxia-induced suppression of protein synthesis in turtles. Expand
Regulatory mechanisms of skeletal muscle protein turnover during exercise.
TLDR
Evidence is provided that upstream signaling to translation factors is mediated by signaling downstream of changes in intracellular Ca( 2+) and energy turnover, and a signaling cascade involving Ca(2+)/calmodulin-eEF2 kinase- eEF2 is implicated. Expand
...
1
2
3
4
...

References

SHOWING 1-10 OF 49 REFERENCES
AMP-activated Protein Kinase Suppresses Protein Synthesis in Rat Skeletal Muscle through Down-regulated Mammalian Target of Rapamycin (mTOR) Signaling*
TLDR
This is the first investigation to demonstrate changes in translation initiation and skeletal muscle protein synthesis in response to AMPK activation. Expand
Activation of AMP-Activated Protein Kinase Leads to the Phosphorylation of Elongation Factor 2 and an Inhibition of Protein Synthesis
TLDR
The activation of e EF2 kinase by AMPK, resulting in the phosphorylation and inactivation of eEF2, provides a novel mechanism for the inhibition of protein synthesis. Expand
Stimulation of the AMP-activated Protein Kinase Leads to Activation of Eukaryotic Elongation Factor 2 Kinase and to Its Phosphorylation at a Novel Site, Serine 398*
TLDR
It is shown that AMPK directly phosphorylates eEF2 kinase, and the major site of phosphorylation as Ser-398 in a regulatory domain of eEF1 kinase is identified, which may provide a key link between cellular energy status and the inhibition of protein synthesis, a major consumer of metabolic energy. Expand
Myocardial Ischemia and Increased Heart Work Modulate the Phosphorylation State of Eukaryotic Elongation Factor-2*
TLDR
Rapamycin did not mimic the effect of oxygen deprivation to inhibit protein synthesis in cardiomyocytes or lead to eEF2 phosphorylation in perfused hearts, suggesting that AMPK activation did not inhibit mTOR/p70 ribosomal protein S6 kinase (p70S6K) signaling. Expand
Control of Ser2448 Phosphorylation in the Mammalian Target of Rapamycin by Insulin and Skeletal Muscle Load*
TLDR
It is demonstrated that atrophy and hypertrophy of skeletal muscle are associated with decreases and increases in Ser2448 phosphorylation, suggesting that modulation of this site may have an important role in the control of protein synthesis. Expand
Effect of Contraction on Mitogen-activated Protein Kinase Signal Transduction in Skeletal Muscle
TLDR
Ex vivo muscle contraction stimulates extracellular signal-regulated kinase 1 and 2, and p38MAPK phosphorylation, and the first to show that contractile activity stimulates MAPKAP-K2 and MSK1, demonstrating that muscle contraction, separate from systemic influence, activates MAPK signaling. Expand
Control of p70 ribosomal protein S6 kinase and acetyl-CoA carboxylase by AMP-activated protein kinase and protein phosphatases in isolated hepatocytes.
TLDR
P70S6K adds to an increasing list of targets of AMPK in agreement with the inhibition of energy-consuming biosynthetic pathways, and blocks amino-acid-induced activation of ACC and p70S 6K by amino acids. Expand
Invited Review: Role of insulin in translational control of protein synthesis in skeletal muscle by amino acids or exercise.
TLDR
This review summarizes the results of a number of recent studies that have helped to establish the present understanding of the interactions of insulin, amino acids, and exercise in the regulation of protein synthesis in skeletal muscle. Expand
Contraction inhibits insulin-stimulated insulin receptor substrate-1/2-associated phosphoinositide 3-kinase activity, but not protein kinase B activation or glucose uptake, in rat muscle.
TLDR
In contracting skeletal muscle, insulin stimulates glucose uptake and activates PKB, but not p70(S6K), by a PI 3-kinase-dependent mechanism that is independent of changes in IRS-1- and IRS-2-associated PI 3 -kinase activity. Expand
Thr2446 Is a Novel Mammalian Target of Rapamycin (mTOR) Phosphorylation Site Regulated by Nutrient Status*
The mammalian target of rapamycin (mTOR) is a key regulator of protein translation. Signaling via mTOR is increased by growth factors but decreased during nutrient deprivation. Previous studies haveExpand
...
1
2
3
4
5
...