Exercise and Mitochondrial Function: Importance and InferenceA Mini Review

2021 ◽  
Vol 21 ◽  
Author(s):  
Vaishali K. ◽  
Nitesh Kumar ◽  
Vanishree Rao ◽  
Rakesh Krishna Kovela ◽  
Mukesh Kumar Sinha
Keyword(s):  
Skeletal Muscle ◽  
Mitochondrial Function ◽  
Skeletal Muscles ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Present Review ◽  
Age Related ◽  
Exercise Induced ◽  
Mitochondrial Adaptations

: Skeletal muscles must generate and distribute energy properly in order to function perfectly. Mitochondria in skeletal muscle cells form vast networks to meet this need, and their functions may improve as a result of exercise. In the present review, we discussed exercise-induced mitochondrial adaptations, age-related mitochondrial decline, and a biomarker as a mitochondrial function indicator and exercise interference.

Does human serum impact differentiation and mitochondrial function of human LHCN-M2 skeletal muscle cells?

2021 ◽  
Author(s):  
Mark Turner ◽  
Amarjit Saini ◽  
Holly Brown ◽  
Sara Anisi ◽  
Claire Stewart ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Human Serum ◽  
Mitochondrial Function ◽  
Muscle Cells ◽  
Skeletal Muscle Cells

Age-related morphological changes in skeletal muscle cells of acid α-glucosidase knockout mice

2006 ◽  
Vol 33 (4) ◽  
pp. 505-513 ◽  
Author(s):  
Reinout P. Hesselink ◽  
Gert Schaart ◽  
Anton J.M. Wagenmakers ◽  
Maarten R. Drost ◽  
Ger J. van der Vusse
Keyword(s):  
Skeletal Muscle ◽  
Knockout Mice ◽  
Morphological Changes ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Age Related

Proteomic identification of secreted proteins from human skeletal muscle cells and expression in response to strength training

2011 ◽  
Vol 301 (5) ◽  
pp. E1013-E1021 ◽  
Author(s):  
Frode Norheim ◽  
Truls Raastad ◽  
Bernd Thiede ◽  
Arild C. Rustan ◽  
Christian A. Drevon ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Strength Training ◽  
Skeletal Muscles ◽  
Human Skeletal Muscle ◽  
Vastus Lateralis ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Secreted Proteins ◽  
Human Myotubes ◽  
Human Skeletal Muscle Cells

Regular physical activity protects against several types of diseases. This may involve altered secretion of signaling proteins from skeletal muscle. Our aim was to identify the most abundantly secreted proteins in cultures of human skeletal muscle cells and to monitor their expression in muscles of strength-training individuals. A total of 236 proteins were detected by proteome analysis in medium conditioned by cultured human myotubes, which was narrowed down to identification of 18 classically secreted proteins expressed in skeletal muscle, using the SignalP 3.0 and Human Genome Expression Profile databases together with a published mRNA-based reconstruction of the human skeletal muscle secretome. For 17 of the secreted proteins, expression was confirmed at the mRNA level in cultured human myotubes as well as in biopsies of human skeletal muscles. RT-PCR analyses showed that 15 of the secreted muscle proteins had significantly enhanced mRNA expression in m. vastus lateralis and/or m. trapezius after 11 wk of strength training among healthy volunteers. For example, secreted protein acidic and rich in cysteine, a secretory protein in the membrane fraction of skeletal muscle fibers, was increased 3- and 10-fold in m. vastus lateralis and m. trapezius, respectively. Identification of proteins secreted by skeletal muscle cells in vitro facilitated the discovery of novel responses in skeletal muscles of strength-training individuals.

scholarly journals Role of Angptl4/Fiaf in exercise-induced skeletal muscle AMPK activation

2018 ◽  
Vol 125 (3) ◽  
pp. 715-722 ◽  
Author(s):  
Hyukki Chang ◽  
Obin Kwon ◽  
Mi-Seon Shin ◽  
Gil Myoung Kang ◽  
Yea Hyun Leem ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscle Cells ◽  
Oxidative Capacity ◽  
Skeletal Muscle Cells ◽  
C2c12 Myotubes ◽  
Ampk Activation ◽  
Expression Levels ◽  
Exercise Induced ◽  
Amp Activated Protein Kinase

Angiopoietin-like protein 4 (Angptl4)/fasting-induced adipose factor (Fiaf) expression levels are increased by exercise in skeletal muscle. We have previously shown that Angptl4 regulates food intake and energy expenditure via modulation of hypothalamic AMP-activated protein kinase (AMPK) activity. AMPK is an important signaling molecule that integrates skeletal muscle metabolism during exercise. Therefore, we investigated the involvement of Angptl4 in exercise-induced AMPK activation in skeletal muscle. Angptl4 protein and mRNA expression levels were significantly increased in the gastrocnemius and soleus muscles of mice following a 50-min running bout. Treatment of C2C12 myotubes with Angptl4 increased phosphorylation of AMPK and acetyl-CoA carboxylase (ACC), which were markers of AMPK activation, and the mitochondrial maximum respiratory capacity. Treadmill exercise increased AMPK and ACC phosphorylation in the gastrocnemius of normal mice; this phosphorylation increase was attenuated in mice lacking Angptl4. Endurance to swimming and hanging was also reduced in Angptl4 knockout mice. Taken together, our current data demonstrate that exercise-induced upregulation of skeletal muscle Angptl4 is critical for AMPK activation and exercise tolerance. These findings unveil a new role for skeletal muscle Angptl4 in exercise physiology. NEW & NOTEWORTHY 1) Angiopoietin-like protein 4 (Angptl4) treatment activates AMP-activated protein kinase (AMPK) signaling in skeletal muscle cells. 2) Angptl4 increases the maximum mitochondrial oxidative capacity through AMPK activation in skeletal muscle cells. 3) Lack of Angptl4 mitigates exercise-induced skeletal muscle AMPK activation. 4) Angptl4-deficient mice show a lower endurance to exercise.

Factors Controlling Movement of Skeletal Muscles

Leonardo ◽  
2015 ◽  
Vol 48 (3) ◽  
pp. 270-271
Author(s):  
Miranda D. Grounds
Keyword(s):  
Skeletal Muscle ◽  
Extracellular Matrix ◽  
Cell Membrane ◽  
Skeletal Muscles ◽  
Muscle Cells ◽  
The Body ◽  
Skeletal Muscle Cells ◽  
3 Dimensional

The contraction of specialized skeletal muscle cells results in classic movements of bones and other parts of the body that are vital for life. There is exquisite control over the movement of diverse types of muscles. This paper indicates the way in which skeletal muscles (myofibres) are formed; then factors that contribute to generating the movement are outlined: these include the nerve, sarcomeres, cytoskeleton, cell membrane and the extracellular matrix. The factors controlling the movement of mature myofibres in 3-dimensional tissues in vivo are vastly more complex than for tissue cultured immature muscle cells in an artificial in vitro environment.

Testosterone and DHEA activate the glucose metabolism-related signaling pathway in skeletal muscle

2008 ◽  
Vol 294 (5) ◽  
pp. E961-E968 ◽  
Author(s):  
Koji Sato ◽  
Motoyuki Iemitsu ◽  
Katsuji Aizawa ◽  
Ryuichi Ajisaka
Keyword(s):  
Skeletal Muscle ◽  
Glucose Metabolism ◽  
Signaling Pathway ◽  
Skeletal Muscles ◽  
Glucose Transporter ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Glut 4 ◽  
Kinase C ◽  
Pkc Ζ

Circulating dehydroepiandrosterone (DHEA) is converted to testosterone or estrogen in the target tissues. Recently, we demonstrated that skeletal muscles are capable of locally synthesizing circulating DHEA to testosterone and estrogen. Furthermore, testosterone is converted to 5α-dihydrotestosterone (DHT) by 5α-reductase and exerts biophysiological actions through binding to androgen receptors. However, it remains unclear whether skeletal muscle can synthesize DHT from testosterone and/or DHEA and whether these hormones affect glucose metabolism-related signaling pathway in skeletal muscles. We hypothesized that locally synthesized DHT from testosterone and/or DHEA activates glucose transporter-4 (GLUT-4)-regulating pathway in skeletal muscles. The aim of the present study was to clarify whether DHT is synthesized from testosterone and/or DHEA in cultured skeletal muscle cells and whether these hormones affect the GLUT-4-related signaling pathway in skeletal muscles. In the present study, the expression of 5α-reductase mRNA was detected in rat cultured skeletal muscle cells, and the addition of testosterone or DHEA increased intramuscular DHT concentrations. Addition of testosterone or DHEA increased GLUT-4 protein expression and its translocation. Furthermore, Akt and protein kinase C-ζ/λ (PKC-ζ/λ) phosphorylations, which are critical in GLUT-4-regulated signaling pathways, were enhanced by testosterone or DHEA addition. Testosterone- and DHEA-induced increases in both GLUT-4 expression and Akt and PKC-ζ/λ phosphorylations were blocked by a DHT inhibitor. Finally, the activities of phosphofructokinase and hexokinase, main glycolytic enzymes, were enhanced by testosterone or DHEA addition. These findings suggest that skeletal muscle is capable of synthesizing DHT from testosterone, and that DHT activates the glucose metabolism-related signaling pathway in skeletal muscle cells.

Characterization of contraction-inducible CXC chemokines and their roles in C2C12 myocytes

2009 ◽  
Vol 297 (4) ◽  
pp. E866-E878 ◽  
Author(s):  
Taku Nedachi ◽  
Hiroyasu Hatakeyama ◽  
Tatsuyoshi Kono ◽  
Masaaki Sato ◽  
Makoto Kanzaki
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Contractile Activity ◽  
Electric Pulse ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Negative Feedback Regulation ◽  
Chemokine Production

Physical exercise triggers the release of several cytokines/chemokines from working skeletal muscles, but the underlying mechanism(s) by which skeletal muscles decipher and respond to highly complex contractile stimuli remains largely unknown. In an effort to investigate the regulatory mechanisms of the expressions of two contraction-inducible CXC chemokines, CXCL1/KC and CXCL5/LIX, in contracting skeletal muscle cells, we took advantage of our in vitro exercise model using highly developed contractile C2C12 myotubes, which acquire properties similar to those of in vivo skeletal muscle via manipulation of Ca2+ transients with electric pulse stimulation (EPS). Production of these CXC chemokines was immediately augmented by EPS-evoked contractile activity in a manner dependent on the activities of JNK and NF-κB, but not p38, ERK1/2, or calcineurin. Intriguingly, exposure of myotubes to cyclic mechanical stretch also induced expression of these CXC chemokines; however, a much longer period of stimulation (∼12 h) was required, despite rapid JNK phosphorylation. We also demonstrate herein that CXCL1/KC and CXCL5/LIX have the ability to raise intracellular Ca2+ concentrations via CXCR2-mediated activation of pertussis toxin-sensitive Gαi proteins in C2C12 myoblasts, an action at least partially responsible for their migration and differentiation. Although we revealed a possible negative feedback regulation of their own production in response to the contractile activity in differentiated myotubes, exogenous administration of these CXC chemokines did not acutely influence either insulin-induced Akt phosphorylation or GLUT4 translocation in C2C12 myotubes. Taken together, these data shed light on the fundamental characteristics of contraction-inducible CXC chemokine production and their potential roles in skeletal muscle cells.

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