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

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.

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

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.

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

Glucose stimulates protein synthesis in skeletal muscle of neonatal pigs through an AMPK- and mTOR-independent process

2007 ◽  
Vol 293 (2) ◽  
pp. E595-E603 ◽  
Author(s):  
Asumthia S. Jeyapalan ◽  
Renan A. Orellana ◽  
Agus Suryawan ◽  
Pamela M. J. O'Connor ◽  
Hanh V. Nguyen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Protein Kinase ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Skeletal Muscle Protein ◽  
Neonatal Pigs ◽  
Skeletal Muscle Protein Synthesis ◽  
Fast Twitch

Skeletal muscle protein synthesis is elevated in neonates in part due to an enhanced response to the rise in insulin and amino acids after eating. In vitro studies suggest that glucose plays a role in protein synthesis regulation. To determine whether glucose, independently of insulin and amino acids, is involved in the postprandial rise in skeletal muscle protein synthesis, pancreatic-substrate clamps were performed in neonatal pigs. Insulin secretion was inhibited with somatostatin and insulin was infused to reproduce fasting or fed levels, while glucose and amino acids were clamped at fasting or fed levels. Fractional protein synthesis rates and translational control mechanisms were examined. Raising glucose alone increased protein synthesis in fast-twitch glycolytic muscles but not in other tissues. The response in muscle was associated with increased phosphorylation of protein kinase B (PKB) and enhanced formation of the active eIF4E·eIF4G complex but no change in phosphorylation of AMP-activated protein kinase (AMPK), tuberous sclerosis complex 2 (TSC2), mammalian target of rapamycin (mTOR), 4E-binding protein-1 (4E-BP1), ribosomal protein S6 kinase (S6K1), or eukaryotic elongation factor 2 (eEF2). Raising glucose, insulin, and amino acids increased protein synthesis in most tissues. The response in muscle was associated with phosphorylation of PKB, mTOR, S6K1, and 4E-BP1 and enhanced eIF4E·eIF4G formation. The results suggest that the postprandial rise in glucose, independently of insulin and amino acids, stimulates protein synthesis in neonates, and this response is specific to fast-twitch glycolytic muscle and occurs by AMPK- and mTOR-independent pathways.

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