scholarly journals High CO2 Downregulates Skeletal Muscle Protein Anabolism via AMP-activated Protein Kinase α2–mediated Depressed Ribosomal Biogenesis

2020 ◽  
Vol 62 (1) ◽  
pp. 74-86 ◽  
Author(s):  
Tanner C. Korponay ◽  
Joseph Balnis ◽  
Catherine E. Vincent ◽  
Diane V. Singer ◽  
Amit Chopra ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscle Protein ◽  
Ribosomal Biogenesis ◽  
Skeletal Muscle Protein ◽  
High Co2 ◽  
Amp Activated Protein Kinase

ATP (Mg2+) induced inhibition of cyclic AMP reactivity with a skeletal muscle protein kinase

1972 ◽  
Vol 47 (4) ◽  
pp. 653-661 ◽  
Author(s):  
Mari K. Haddox ◽  
Nancy E. Newton ◽  
Diane K. Hartle ◽  
Nelson D. Goldberg
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Muscle Protein ◽  
Skeletal Muscle Protein

Reversal of chronic alterations of skeletal muscle protein kinase C from fat-fed rats by BRL-49653

1997 ◽  
Vol 273 (5) ◽  
pp. E915-E921 ◽  
Author(s):  
Carsten Schmitz-Peiffer ◽  
Nicholas D. Oakes ◽  
Carol L. Browne ◽  
Edward W. Kraegen ◽  
Trevor J. Biden
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Muscle Protein ◽  
Skeletal Muscle Protein ◽  
Insulin Sensitizer ◽  
Muscle Insulin Resistance ◽  
Skeletal Muscle Insulin Resistance ◽  
Kinase C

We have recently shown that the reduction in insulin sensitivity of rats fed a high-fat diet is associated with the translocation of the novel protein kinase Cε(nPKCε) from cytosolic to particulate fractions in red skeletal muscle and also the downregulation of cytosolic nPKCθ. Here we have further investigated the link between insulin resistance and PKC by assessing the effects of the thiazolidinedione insulin-sensitizer BRL-49653 on PKC isoenzymes in muscle. BRL-49653 increased the recovery of nPKC isoenzymes in cytosolic fractions of red muscle from fat-fed rats, reducing their apparent activation and/or downregulation, whereas PKC in control rats was unaffected. Because BRL-49653 also improves insulin-stimulated glucose uptake in fat-fed rats and reduces muscle lipid storage, especially diglyceride content, these results strengthen the association between lipid availability, nPKC activation, and skeletal muscle insulin resistance and support the hypothesis that chronic activation of nPKC isoenzymes is involved in the generation of muscle insulin resistance in fat-fed rats.

scholarly journals Measurement of Cyclic 3',5'-Adenosine Monophosphate by the Activation of Skeletal Muscle Protein Kinase

1971 ◽  
Vol 246 (7) ◽  
pp. 1996-2003 ◽  
Author(s):  
William B. Wastila ◽  
James T. Stull ◽  
Steven E. Mayer ◽  
Donal A. Walsh
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscle Protein ◽  
Adenosine Monophosphate ◽  
Skeletal Muscle Protein

Stimulatory effect of the 2-palmitamidoethyl ester of adenosine 5'-phosphate on the activity of rabbit skeletal muscle protein kinase

1981 ◽  
Vol 46 (3) ◽  
pp. 792-797
Author(s):  
Sixtus Hynie ◽  
Jiří Smrt
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Drug Concentration ◽  
Narrow Range ◽  
Muscle Protein ◽  
Rabbit Skeletal Muscle ◽  
Skeletal Muscle Protein ◽  
High Drug ◽  
High Drug Concentration

2-Palmitamidoethyl ester of adenosine 5'-phosphate (PEA-AMP) stimulates the rabbit skeletal muscle protein kinase in relatively narrow range of high drug concentration. Mechanism of this effect seems to be analogous to that of cyclic AMP.

Effect of adenosine nucleolipids on the activity of rabbit skeletal muscle protein kinase

1980 ◽  
Vol 45 (11) ◽  
pp. 3210-3216 ◽  
Author(s):  
Sixtus Hynie ◽  
Jiří Smrt
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscle Protein ◽  
Inhibitory Effect ◽  
Rabbit Skeletal Muscle ◽  
Phosphate Esters ◽  
Skeletal Muscle Protein ◽  
Inhibitory Effects ◽  
Enzyme Stimulation ◽  
Hydroxy Compounds

The inhibitory effects of adenosine 5'-phosphate esters with lipoid hydroxy compounds on rabbit skeletal muscle protein kinase are in comparison with adenosine or adenosine 5'-monophosphate relatively weak. The inhibitory effect is in some cases preceded by the enzyme stimulation which can reach up to 70-80% of the stimulation by cyclic AMP. While the inhibitory effect seems to be caused by the adenosine moiety of the compound, the nature of the stimulatory effect is not yet elucidated.

scholarly journals Leucine supplementation stimulates protein synthesis and reduces degradation signal activation in muscle of newborn pigs during acute endotoxemia

2016 ◽  
Vol 311 (4) ◽  
pp. E791-E801 ◽  
Author(s):  
Adriana D. Hernandez-García ◽  
Daniel A. Columbus ◽  
Rodrigo Manjarín ◽  
Hanh V. Nguyen ◽  
Agus Suryawan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Protein Kinase ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Ring Finger ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Leucine Supplementation ◽  
Amp Activated Protein Kinase

Sepsis disrupts skeletal muscle proteostasis and mitigates the anabolic response to leucine (Leu) in muscle of mature animals. We have shown that Leu stimulates muscle protein synthesis (PS) in healthy neonatal piglets. To determine if supplemental Leu can stimulate PS and reduce protein degradation (PD) signaling in neonatal muscle during endotoxemia, overnight-fasted neonatal pigs were infused for 8 h with LPS or saline while plasma amino acids, glucose, and insulin were maintained at fasting levels during pancreatic-substrate clamps. Leu or saline was infused during the last hour. Markers of PS and PD were determined in skeletal muscle. Compared with controls, Leu increased PS in longissimus dorsi (LD), gastrocnemius, and soleus muscles. LPS decreased PS in these three muscles by 36%, 28%, and 38%, but Leu antagonized that reduction by increasing PS by 84%, 81%, and 83%, respectively, when supplemented to LPS. Leu increased eukaryotic translation initiation factor (eIF)3b-raptor interactions, eIF4E-binding protein-1, and S6 kinase 1 phosphorylation as well as eIF4E·eIF4G complex formation in LD, gastrocnemius, and soleus muscles of control and LPS-treated pigs. In LD muscle, LPS increased the light chain (LC)3-II-to-LC3 ratio and muscle-specific RING finger (MuRF-1) abundance but not atrogin-1 abundance or AMP-activated protein kinase-α phosphorylation. Leu supplementation to LPS-treated pigs reduced the LC3-II-to-LC3 ratio, MuRF-1 abundance, and AMP-activated protein kinase-α phosphorylation compared with LPS alone. In conclusion, parenteral Leu supplementation attenuates the LPS-induced reduction in PS by stimulating mammalian target of rapamycin complex 1-dependent translation and may reduce PD by attenuating autophagy-lysosome and MuRF-1 signaling in neonatal skeletal muscle.

Novel aspects of skeletal muscle protein kinase and protein phosphatase regulation by Ca2+

1980 ◽  
Vol 18 ◽  
pp. 121-144 ◽  
Author(s):  
L.M.G. Heilmeyer ◽  
U. Gröschel-Stewart ◽  
U. Jahnke ◽  
M.W. Kilimann ◽  
K.P. Kohse ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Muscle Protein ◽  
Skeletal Muscle Protein ◽  
Phosphatase Regulation
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