Effects of Corticosterone on Connectin Content and Protein Breakdown in Rat Skeletal Muscle

2000 ◽  
Vol 64 (12) ◽  
pp. 2686-2688 ◽  
Author(s):  
Kunioki HAYASHI ◽  
Osamu TADA ◽  
Kouji HIGUCHI ◽  
Akira OHTSUKA
Keyword(s):  
Skeletal Muscle ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle

scholarly journals Hypertrophy of Rat Skeletal Muscle Is Associated with Increased SIRT1/Akt/mTOR/S6 and Suppressed Sestrin2/SIRT3/FOXO1 Levels

2021 ◽  
Vol 22 (14) ◽  
pp. 7588
Author(s):  
Zoltan Gombos ◽  
Erika Koltai ◽  
Ferenc Torma ◽  
Peter Bakonyi ◽  
Attila Kolonics ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Hypertrophy ◽  
Male Rats ◽  
Cellular Interactions ◽  
Molecular Signaling ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle ◽  
Plantaris Muscle ◽  
Skeletal Muscle Hypertrophy ◽  
Intensive Investigation

Despite the intensive investigation of the molecular mechanism of skeletal muscle hypertrophy, the underlying signaling processes are not completely understood. Therefore, we used an overload model, in which the main synergist muscles (gastrocnemius, soleus) of the plantaris muscle were surgically removed, to cause a significant overload in the remaining plantaris muscle of 8-month-old Wistar male rats. SIRT1-associated pro-anabolic, pro-catabolic molecular signaling pathways, NAD and H2S levels of this overload-induced hypertrophy were studied. Fourteen days of overload resulted in a significant 43% (p < 0.01) increase in the mass of plantaris muscle compared to sham operated animals. Cystathionine-β-synthase (CBS) activities and bioavailable H2S levels were not modified by overload. On the other hand, overload-induced hypertrophy of skeletal muscle was associated with increased SIRT1 (p < 0.01), Akt (p < 0.01), mTOR, S6 (p < 0.01) and suppressed sestrin 2 levels (p < 0.01), which are mostly responsible for anabolic signaling. Decreased FOXO1 and SIRT3 signaling (p < 0.01) suggest downregulation of protein breakdown and mitophagy. Decreased levels of NAD+, sestrin2, OGG1 (p < 0.01) indicate that the redox milieu of skeletal muscle after 14 days of overloading is reduced. The present investigation revealed novel cellular interactions that regulate anabolic and catabolic processes in the hypertrophy of skeletal muscle.

Total and myofibrillar protein breakdown in different types of rat skeletal muscle: Effects of sepsis and regulation by insulin

Metabolism ◽  
1989 ◽  
Vol 38 (7) ◽  
pp. 634-640 ◽  
Author(s):  
Per-Olof Hasselgren ◽  
J.Howard James ◽  
Daniel W. Benson ◽  
Marianne Hall-Angerås ◽  
Ulf Angerås ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myofibrillar Protein ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle ◽  
Different Types

CL 316,243, a selective β3-adrenergic agonist, inhibits protein breakdown in rat skeletal muscle

2005 ◽  
Vol 451 (5) ◽  
pp. 617-624 ◽  
Author(s):  
Luiz Carlos C. Navegantes ◽  
Neusa M. Z. Resano ◽  
Amanda Martins Baviera ◽  
Renato H. Migliorini ◽  
Isis C. Kettelhut
Keyword(s):  
Skeletal Muscle ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle ◽  
Adrenergic Agonist ◽  
Cl 316,243

Interleukin-6 does not activate protein breakdown in rat skeletal muscle

1994 ◽  
Vol 76 (1) ◽  
pp. 1-4 ◽  
Author(s):  
Cèlia García-Martínez ◽  
Francisco J. López-Soriano ◽  
Josep M. Argilés
Keyword(s):  
Skeletal Muscle ◽  
Interleukin 6 ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle

scholarly journals Age- and activity-related changes in three proteinase enzymes of rat skeletal muscle

1985 ◽  
Vol 230 (3) ◽  
pp. 833-836 ◽  
Author(s):  
D F Goldspink ◽  
S E Lewis
Keyword(s):  
Skeletal Muscle ◽  
Old Age ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle ◽  
Foetal Life ◽  
Muscle Types ◽  
Specific Activities ◽  
Skeletal Muscle Types

The specific activities of three proteinases, cathepsins B, D and H, were measured in two skeletal-muscle types as a function of age (i.e. from large foetal life to old age), and in muscles immobilized at various lengths for 3 days. The activities of the lysosomal endopeptidases B and D, but not H, consistently changed in parallel with previously determined rates of protein breakdown, indicating a good and potentially useful correlation between the two.

scholarly journals Inhibition of protein breakdown by glutamine in perfused rat skeletal muscle

FEBS Letters ◽  
1988 ◽  
Vol 237 (1-2) ◽  
pp. 133-136 ◽  
Author(s):  
Peter A. MacLennan ◽  
Kenneth Smith ◽  
Brian Weryk ◽  
Peter W. Watt ◽  
Michael J. Rennie
Keyword(s):  
Skeletal Muscle ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle

scholarly journals Acute alterations in sodium flux in vitro lead to decreased myofibrillar protein breakdown in rat skeletal muscle

1987 ◽  
Vol 247 (1) ◽  
pp. 151-156 ◽  
Author(s):  
M N Goodman
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Myofibrillar Protein ◽  
Protein Breakdown ◽  
Rat Skeletal Muscle ◽  
Phospholipid Hydrolysis ◽  
Kinase C ◽  
Activate Protein Kinase ◽  
Ionophore Monensin

Myofibrillar protein breakdown was evaluated by measuring the release of N tau-methylhistidine by isolated rat skeletal muscles or perfused rat muscles in the presence of a variety of agents known to affect Na+ flux. Total cell proteolysis was evaluated simultaneously by measuring tyrosine release by muscles after the inhibition of protein synthesis with cycloheximide. Treatment of muscles with the Na+ ionophore monensin or inhibitors of Na+-K+ ATPase (ouabain, digoxin or vanadate) decreased N tau-methylhistidine release by muscles by 21-35%. A phorbol ester (phorbol 12-myristate 13-acetate) as well as a synthetic diacylglycerol known to activate protein kinase C and a Na+/H+ antiport also decreased N tau-methylhistidine release by muscles. Removal of extracellular Na+ blocked the ability of these agents to attenuate N tau-methylhistidine release by muscles, suggesting that their effectiveness required a change in Na+ flux. In contrast with N tau-methylhistidine release by muscles, these agents, except for monensin, did not effect the release of tyrosine, suggesting that they attenuate specifically the breakdown of myofibrillar proteins. Overall these results indicate a link between Na+ and the regulation of protein breakdown in rat skeletal muscle, whereby an influx of Na+ can result in a decrease in myofibrillar proteolysis. Left unresolved is whether phospholipid hydrolysis is involved in this scheme.

Sign in / Sign up

Export Citation Format

Share Document