scholarly journals Phosphate increase during fatigue affects crossbridge kinetics in intact mouse muscle at physiological temperature

2017 ◽  
Vol 595 (13) ◽  
pp. 4317-4328 ◽  
Author(s):  
M. Nocella ◽  
G. Cecchi ◽  
B. Colombini
Keyword(s):  
Intact Mouse ◽  
Mouse Muscle ◽  
Physiological Temperature ◽  
Crossbridge Kinetics

scholarly journals TWIST1 and TWIST2 regulate glycogen storage and inflammatory genes in skeletal muscle

2015 ◽  
Vol 224 (3) ◽  
pp. 303-313 ◽  
Author(s):  
Jonathan M Mudry ◽  
Julie Massart ◽  
Ferenc L M Szekeres ◽  
Anna Krook
Keyword(s):  
Skeletal Muscle ◽  
Metabolic Diseases ◽  
Glycogen Synthesis ◽  
C2c12 Cells ◽  
Acid Oxidation ◽  
Diabetic Patients ◽  
Mrna Levels ◽  
Intact Mouse ◽  
Mouse Muscle ◽  
The Impact

TWIST proteins are important for development of embryonic skeletal muscle and play a role in the metabolism of tumor and white adipose tissue. The impact of TWIST on metabolism in skeletal muscle is incompletely studied. Our aim was to assess the impact of TWIST1 and TWIST2 overexpression on glucose and lipid metabolism. In intact mouse muscle, overexpression of Twist reduced total glycogen content without altering glucose uptake. Expression of TWIST1 or TWIST2 reducedPdk4mRNA, while increasing mRNA levels ofIl6,Tnfα, andIl1β. Phosphorylation of AKT was increased and protein abundance of acetyl CoA carboxylase (ACC) was decreased in skeletal muscle overexpressing TWIST1 or TWIST2. Glycogen synthesis and fatty acid oxidation remained stable in C2C12 cells overexpressing TWIST1 or TWIST2. Finally, skeletal muscle mRNA levels remain unaltered inob/obmice, type 2 diabetic patients, or in healthy subjects before and after 3 months of exercise training. Collectively, our results indicate that TWIST1 and TWIST2 are expressed in skeletal muscle. Overexpression of these proteins impacts proteins in metabolic pathways and mRNA level of cytokines. However, skeletal muscle levels of TWIST transcripts are unaltered in metabolic diseases.

scholarly journals Subcellular distribution of glycogen and decreased tetanic Ca2+in fatigued single intact mouse muscle fibres

2014 ◽  
Vol 592 (9) ◽  
pp. 2003-2012 ◽  
Author(s):  
Joachim Nielsen ◽  
Arthur J. Cheng ◽  
Niels Ørtenblad ◽  
Håkan Westerblad
Keyword(s):  
Subcellular Distribution ◽  
Muscle Fibres ◽  
Intact Mouse ◽  
Mouse Muscle

Interactions between intracellular calcium and phosphate in intact mouse muscle during fatigue

2011 ◽  
Vol 111 (2) ◽  
pp. 358-366 ◽  
Author(s):  
D. G. Allen ◽  
E. Clugston ◽  
Y. Petersen ◽  
I. V. Röder ◽  
B. Chapman ◽  
...  
Keyword(s):  
Tibialis Anterior Muscle ◽  
Complete Recovery ◽  
Force Transducer ◽  
Partial Recovery ◽  
Initial Value ◽  
Intact Mouse ◽  
Mouse Muscle ◽  
Intracellular Ca ◽  
Intracellular Phosphate ◽  
Distal Tendon

Fatigue was studied in intact tibialis anterior muscle of anesthetized mice. The distal tendon was detached and connected to a force transducer while blood flow continued normally. The muscle was stimulated with electrodes applied directly to the muscle surface and fatigued by repeated (1 per 4 s), brief (0.4 s), maximal (100-Hz stimulation frequency) tetani. Force declined monotonically to 49 ± 5% of the initial value with a half time of 36 ± 5 s and recovered to 86 ± 4% after 4 min. Intracellular phosphate concentration ([Pi]) was measured by 31P-NMR on perchloric acid extracts of muscles. [Pi] increased during fatigue from 7.6 ± 1.7 to 16.0 ± 1.6 mmol/kg muscle wet wt and returned to control during recovery. Intracellular Ca2+ was measured with cameleons whose plasmids had been transfected in the muscle 2 wk before the experiment. Yellow cameleon 2 was used to measure myoplasmic Ca2+, and D1ER was used to measure sarcoplasmic reticulum (SR) Ca2+. The myoplasmic Ca2+ during tetani declined steadily during the period of fatigue and showed complete recovery over 4 min. The SR Ca2+ also declined monotonically during fatigue and showed a partial recovery with rest. These results show that the initial phase of force decline is accompanied by a rise in [Pi] and a reduction in the tetanic myoplasmic Ca2+. We suggest that both changes contribute to the fatigue. A likely cause of the decline in tetanic myoplasmic Ca2+ is precipitation of CaPi in the SR.

scholarly journals Effect of Temperature on Crossbridge Force Changes during Fatigue and Recovery in Intact Mouse Muscle Fibers

PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e78918 ◽  
Author(s):  
Marta Nocella ◽  
Giovanni Cecchi ◽  
Maria Angela Bagni ◽  
Barbara Colombini
Keyword(s):  
Muscle Fibers ◽  
Effect Of Temperature ◽  
Intact Mouse ◽  
Mouse Muscle

Electron Microscopic Analysis of Myonecrosis Induced by a Pure Component Isolated From Rattlesnake Venom

1976 ◽  
Vol 34 ◽  
pp. 292-293
Author(s):  
Charlotte L. Ownby ◽  
David Cameron ◽  
Anthony T. Tu
Keyword(s):  
Gel Filtration ◽  
Microscopic Analysis ◽  
The United States ◽  
Exchange Chromatography ◽  
Pure Component ◽  
Electron Microscopic Level ◽  
Electron Microscopic ◽  
Mouse Muscle ◽  
Major Health Problem ◽  
Rattlesnake Venom

In the United States the major health problem resulting from snakebite poisoning is local tissue damage, i.e. hemorrhage and myonecrosis. Since commercial antivenin does not usually prevent such damage to tissue, a more effective treatment of snakebite-induced myonecrosis is needed. To aid in the development of such a treatment the pathogenesis of myonecrosis induced by a pure component of rattlesnake venom was studied at the electron microscopic level.The pure component, a small (4,300 mol. wt.), basic (isoelectric point of 9.6) protein, was isolated from crude prairie rattlesnake (Crotalus viridis viridis) venom by gel filtration (Sephadex G-50) followed by cation exchange chromatography (Sephadex C-25), and shown to be pure by electrophoresis. Selection of the myotoxic component was based on light microscopic observations of injected mouse muscle.

Mightier mouse muscle

Nature ◽  
1999 ◽  
Author(s):  
Sara Abdulla
Keyword(s):  
Mouse Muscle

scholarly journals Muscle unloading-induced metabolic remodeling is associated with acute alterations in PPARδ and UCP-3 expression

2008 ◽  
Vol 34 (2) ◽  
pp. 149-161 ◽  
Author(s):  
Dawn J. Mazzatti ◽  
Melissa A. Smith ◽  
Radu C. Oita ◽  
Fei-Ling Lim ◽  
Andrew J. White ◽  
...  
Keyword(s):  
Differential Expression ◽  
Fiber Type ◽  
Uncoupling Protein ◽  
Hindlimb Suspension ◽  
Metabolic Flexibility ◽  
Peroxisome Proliferator ◽  
Compensatory Response ◽  
Mouse Muscle ◽  
Metabolic Remodeling ◽  
Muscle Unloading

A number of physiological changes follow prolonged skeletal muscle unloading as occurs in spaceflight, bed rest, and hindlimb suspension (HLS) and also in aging. These include muscle atrophy, fiber type switching, and loss of the ability to switch between lipid and glucose usage, or metabolic inflexibility. The signaling and genomic events that precede these physiological manifestations have not been investigated in detail, particularly in regard to loss of metabolic flexibility. Here we used gene arrays to determine the effects of 24-h HLS on metabolic remodeling in mouse muscle. Acute unloading resulted in differential expression of a number of transcripts in soleus and gastrocnemius muscle, including many involved in lipid and glucose metabolism. These include the peroxisome proliferator-activated receptors (PPARs). In contrast to Ppar-α and Ppar-γ, which were downregulated by acute HLS, Ppar-δ was upregulated concomitant with increased expression of its downstream target, uncoupling protein-3 ( Ucp-3). However, differential expression of Ppar-δ was both acute and transient in nature, suggesting that regulation of PPARδ may represent an adaptive, compensatory response aimed at regulating fuel utilization and maintaining metabolic flexibility.

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