PSV-13 Understanding the role of zinc and manganese in proliferation and protein synthesis of primary bovine satellite cells

2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 308-308
Author(s):  
Anthony F Alberto ◽  
Laura A Smith ◽  
Caleb C Reichhardt ◽  
Stephanie L Hansen ◽  
Kara J Thornton
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Molecular Mechanisms ◽  
Muscle Growth ◽  
The Body ◽  
Trace Minerals ◽  
Trace Mineral ◽  
Bovine Skeletal Muscle ◽  
Free Media ◽  
And Control

Abstract Trace minerals are vital for the health and growth of livestock, supporting multiple biochemical processes in the body. There are several different signaling pathways that may be affected by trace minerals, ultimately altering growth of skeletal muscle. However, it is currently unknown how trace minerals specifically impact growth of skeletal muscle. As such, the objective of this study was to determine how zinc (Zn) and manganese (Mn) affect proliferation and protein synthesis of primary bovine satellite cell (BSC) cultures. Cultures were grown to 80% confluency and treated in 1% fetal bovine serum (control), 0.05, 0.10 or 0.25 µM of Mn, or 10, 20 or 40 µM of Zn to assess proliferation. Additionally, the above treatments were applied to fused BSC cultures in serum free media (control) to measure protein synthesis. The trace mineral concentrations chosen were based off known ranges of circulating concentrations of Zn or Mn. A series of contrasts were constructed to determine whether growth of BSC cultures was different between the treated and control cultures. Treatment with 10 µM Zn increased (P = 0.03) proliferation when compared to control cultures. However, treatment with Mn at the tested concentration did not (P > 0.12) result in proliferation rates that were different than the control cultures. Treatment with 10 µM Zn, 20 µM Zn, or 0.5 µM Mn increased (P < 0.05) protein synthesis compared to control cultures. These results indicate Zn is capable of increasing proliferation and both Zn and Mn increase protein synthesis of BSC cultures. Additional research is needed to couple trace mineral nutrition with knowledge of BSC biology to elucidate the molecular mechanisms by which trace minerals may function to support bovine skeletal muscle growth.

scholarly journals Molecular Mechanisms of Skeletal Muscle Hypertrophy

2020 ◽  
pp. 1-15
Author(s):  
Stefano Schiaffino ◽  
Carlo Reggiani ◽  
Takayuki Akimoto ◽  
Bert Blaauw
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Hypertrophy ◽  
Molecular Mechanisms ◽  
Muscle Growth ◽  
Transcriptional Level ◽  
Ribosomal Biogenesis ◽  
Skeletal Muscle Hypertrophy ◽  
Positive Regulators ◽  
Exercise Muscle

Skeletal muscle hypertrophy can be induced by hormones and growth factors acting directly as positive regulators of muscle growth or indirectly by neutralizing negative regulators, and by mechanical signals mediating the effect of resistance exercise. Muscle growth during hypertrophy is controlled at the translational level, through the stimulation of protein synthesis, and at the transcriptional level, through the activation of ribosomal RNAs and muscle-specific genes. mTORC1 has a central role in the regulation of both protein synthesis and ribosomal biogenesis. Several transcription factors and co-activators, including MEF2, SRF, PGC-1α4, and YAP promote the growth of the myofibers. Satellite cell proliferation and fusion is involved in some but not all muscle hypertrophy models.

scholarly journals PO-055 Changes of trace elements in skeletal muscle and serum of rats after exercise-induced injury

2018 ◽  
Vol 1 (3) ◽  
Author(s):  
Jingyun Liu ◽  
Qun Zuo
Keyword(s):  
Skeletal Muscle ◽  
Trace Elements ◽  
Nitric Acid ◽  
Vena Cava ◽  
The Body ◽  
Emission Spectrometry ◽  
Control Group ◽  
Exercise Induced ◽  
And Control ◽  
Cu And Zn

Objective This study is to investigate the changes of trace elements (Cu, Fe, Zn, Se, Mg) in serum and skeletal muscle of rats after skeletal muscle injury induced by downhill running, and to find out the change regularity of trace elements in the body after exercise injury. To provide experimental basis for how to use trace elements supplements reasonably. Methods Fifty-four healthy male Sprague-Dawley rats aged 8 weeks were randomly divided into two groups: control group (C, N=6) and exercise group (E, N=48, include: 0 h group, 6 h group, 12 h group, 24 h group, 48 h group, 72 h group, 1- week group and 2- week group). The rats in exercise groups run down a 16°incline at 16m/min for 90 minutes. At the end of the exercise, the rats were killed at 0 h, 6 h, 12 h, 24 h, 48 h, 72 h, 1 week and 2 weeks, respectively. The serum was got from the inferior vena cava blood and diluted by 1% nitric acid. The muscle was got from the right side of the rat's sural which were digested by concentrated nitric acid and 30% hydrogen peroxide in 75℃water bath for 20mins. The content of trace elements in muscle and serum were measured by inductively coupled plasma atomic emission spectrometry (ICP-MS). All the data are analyzed and processed by SPSS22.0 statistical software. Results (1) The contents of trace elements in serum showed: Cu, Zn, Mg, Se decreased immediately after exercise, but the Cu still increased to reach a peak at 24h after decreasing, and after 2 weeks the content of Cu was slightly lower than pre-exercise level. However, the content of Zn did not elevate again, it continued declined to the lowest at 24h which was significantly lower than control group (P < 0.05). And after 2 weeks, Zn did not return to the pre-exercise level. The changes of Mg, Se in serum was not statistically significant. There is no difference between 0h and control groups in content of Fe, after that Fe decreased continually and appeared the least value at 24h, the differences between immediate group and control group were statistically significant (P < 0.05). Fe returned to the pre-exercise level after 2 weeks. (2) The contents of trace elements in muscle showed: Most of trace elements increased to the maximum level at 6 h, after that Mg, Fe, Cu decreased to the lowest value at 72 h which were significant lower than 0h group or 6h group (P < 0. 05). ALL the trace elements were lower than pre-exercise level. There was no statistical difference in the content of Se in muscle. Conclusions (1) The different changes of trace elements in skeletal muscle and serum after exercise injury may be due to the redistribution of trace elements caused by the body adaptability. (2) The most obviously changes of trace element in serum and muscle are Cu and Zn. Both of them did not return to the pre-exercise level after 2 weeks, it suggests that the supplement include Cu and Zn may play an important role in recovering after exercise-induced injury.

scholarly journals Regulation of Ribosome Biogenesis in Skeletal Muscle Hypertrophy

Physiology ◽  
2019 ◽  
Vol 34 (1) ◽  
pp. 30-42 ◽  
Author(s):  
Vandré Casagrande Figueiredo ◽  
John J. McCarthy
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Ribosome Biogenesis ◽  
Muscle Hypertrophy ◽  
Muscle Growth ◽  
Translational Efficiency ◽  
Resistance Exercise Training ◽  
Skeletal Muscle Growth ◽  
Skeletal Muscle Hypertrophy ◽  
Important Regulator

The ribosome is the enzymatic macromolecular machine responsible for protein synthesis. The rates of protein synthesis are primarily dependent on translational efficiency and capacity. Ribosome biogenesis has emerged as an important regulator of skeletal muscle growth and maintenance by altering the translational capacity of the cell. Here, we provide evidence to support a central role for ribosome biogenesis in skeletal muscle growth during postnatal development and in response to resistance exercise training. Furthermore, we discuss the cellular signaling pathways regulating ribosome biogenesis, discuss how myonuclear accretion affects translational capacity, and explore future areas of investigation within the field.

scholarly journals Skeletal-muscle growth and protein turnover

1975 ◽  
Vol 150 (2) ◽  
pp. 235-243 ◽  
Author(s):  
D J Millward ◽  
P J Garlick ◽  
R J C Stewart ◽  
D O Nnanyelugo ◽  
J C Waterlow
Keyword(s):  
Skeletal Muscle ◽  
Growth Rate ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Growth ◽  
Muscle Size ◽  
Synthesis Rate ◽  
Protein Breakdown ◽  
Breakdown Rate ◽  
Breakdown Rates

Because of turnover, protein synthesis and breakdown can each be involved in the regulation of the growth of tissue protein. To investigate the regulation of skeletal-muscle-protein growth we measured rates of protein synthesis and breakdown in growing rats during development on a good diet, during development on a marginally low-protein diet and during rehabilitation on a good diet after a period of severe protein deficiency. Rates of protein synthesis were measured in vivo with a constant intravenous infusion of [14C]tyrosine. The growth rate of muscle protein was measured and the rate of breakdown calculated as breakdown rate=synthesis rate-growth rate. These measurements showed that during development on a good diet there was a fall with age in the rate of protein synthesis resulting from a fall in capacity (RNA concentration) and activity (synthesis rate per unit of RNA). There was a fall with age in the breakdown rate so that the rate was highest in the weaning rats, with a half-life of 3 days. There was a direct correlation between the fractional growth and breakdown rates. During rehabilitation on the good diet, rapid growth was also accompanied by high rates of protein breakdown. During growth on the inadequate diet protein synthesis rates were lesss than in controls, but growth occurred because of decreased rates of protein breakdown. This compression was not complete, however, since ultimate muscle size was only one-half that of controls. It is suggested that increased rates of protein breakdown are a necessary accompaniment to muscle growth and may result from the way in which myofibrils proliferate.

scholarly journals The mTORC1 signaling repressors REDD1/2 are rapidly induced and activation of p70S6K1 by leucine is defective in skeletal muscle of an immobilized rat hindlimb

2013 ◽  
Vol 304 (2) ◽  
pp. E229-E236 ◽  
Author(s):  
Andrew R. Kelleher ◽  
Scot R. Kimball ◽  
Michael D. Dennis ◽  
Rudolf J. Schilder ◽  
Leonard S. Jefferson
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Molecular Mechanisms ◽  
Bed Rest ◽  
Disuse Atrophy ◽  
Sprague Dawley ◽  
Ribosomal Protein S6 ◽  
Sprague Dawley Rats ◽  
Mtorc1 Signaling ◽  
Limb Immobilization

Limb immobilization, limb suspension, and bed rest cause substantial loss of skeletal muscle mass, a phenomenon termed disuse atrophy. To acquire new knowledge that will assist in the development of therapeutic strategies for minimizing disuse atrophy, the present study was undertaken with the aim of identifying molecular mechanisms that mediate control of protein synthesis and mechanistic target of rapamycin complex 1 (mTORC1) signaling. Male Sprague-Dawley rats were subjected to unilateral hindlimb immobilization for 1, 2, 3, or 7 days or served as nonimmobilized controls. Following an overnight fast, rats received either saline or l-leucine by oral gavage as a nutrient stimulus. Hindlimb skeletal muscles were extracted 30 min postgavage and analyzed for the rate of protein synthesis, mRNA expression, phosphorylation state of key proteins in the mTORC1 signaling pathway, and mTORC1 signaling repressors. In the basal state, mTORC1 signaling and protein synthesis were repressed within 24 h in the soleus of an immobilized compared with a nonimmobilized hindlimb. These responses were accompanied by a concomitant induction in expression of the mTORC1 repressors regulated in development and DNA damage responses (REDD) 1/2. The nutrient stimulus produced an elevation of similar magnitude in mTORC1 signaling in both the immobilized and nonimmobilized muscle. In contrast, phosphorylation of 70-kDa ribosomal protein S6 kinase 1 (p70S6K1) on Thr229 and Thr389 in response to the nutrient stimulus was severely blunted. Phosphorylation of Thr229 by PDK1 is a prerequisite for phosphorylation of Thr389 by mTORC1, suggesting that signaling through PDK1 is impaired in response to immobilization. In conclusion, the results show an immobilization-induced attenuation of mTORC1 signaling mediated by induction of REDD1/2 and defective p70S6K1 phosphorylation.

Isoproterenol induces a ribosomal modification in the heart and the skeletal muscle of hamsters

1985 ◽  
Vol 5 (1) ◽  
pp. 13-19
Author(s):  
Josette Noël ◽  
Léa Brakier-Gingras
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Magnesium Concentration ◽  
Translation System ◽  
Synthesis Activity ◽  
And Control

The protein synthesis activity of heart, skeletal muscle and liver polysomes from isoprotenerol-treated and control hamsters has been compared in an in vitro non-inititating translation system. Heart and skeletal muscle polysomes from treated hamsters were less active than controls and required a higher magnesium concentration for optimal protein synthesis. These results suggest that there is a conformational modification in heart and skeletal muscle ribosomes from isoprotenerol-treated hamsters. No such change was observed with ribosomes from the liver of isoproterenol-treated hamsters.

scholarly journals Molecular Mechanisms, Therapeutic Targets and Pharmacological Interventions: An Update

2021 ◽  
Author(s):  
Mohit Kwatra ◽  
Sahabuddin Ahmed ◽  
Samir Ranjan Panda ◽  
Vegi Ganga Modi Naidu ◽  
Nitika Gupta
Keyword(s):  
Skeletal Muscle ◽  
Energy Expenditure ◽  
Muscle Mass ◽  
Molecular Mechanisms ◽  
Human Subjects ◽  
Therapeutic Targets ◽  
The Body ◽  
Sirtuin 1 ◽  
Pharmacological Interventions ◽  
Ubiquitin Proteasome

Muscles are the enriched reservoir of proteins in the body. During any workout or exercise, the demand in the form of energy is essentially required by the muscle. Energy expenditure of skeletal muscle is more dependent on the type of demand. There is particular homeostasis within the body that avoid surplus energy expenditure and this prevents any muscle loss. Muscle atrophy is termed as the loss of skeletal muscle mass due to immobility, malnutrition, medications, aging, cancer cachexia, variety of injuries or diseases that impact the musculoskeletal or nervous system. Hence, atrophy within the skeletal muscle initiates further cause fatigue, pain, muscle weakness, and disability in human subjects. Therefore, starvation and reduced muscle mass further initiate numerous signaling pathways including inflammatory, antioxidant signaling, mitochondria bio-energetic failure, AMP-activated protein kinase (AMPK), Sirtuin 1(SIRT1), BDNF/TrkB/PKC, Autophagy, ubiquitin-proteasome systems, etc. Here, in this chapter, we will mention molecular mechanisms involved in therapeutic targets and available Pharmacological Interventions with the latest updates.

scholarly journals p21-Activated Kinase 1 Is Permissive for the Skeletal Muscle Hypertrophy Induced by Myostatin Inhibition

2021 ◽  
Vol 12 ◽  
Author(s):  
Caroline Barbé ◽  
Audrey Loumaye ◽  
Pascale Lause ◽  
Olli Ritvos ◽  
Jean-Paul Thissen
Keyword(s):  
Skeletal Muscle ◽  
Muscle Mass ◽  
Skeletal Muscle Mass ◽  
Muscle Hypertrophy ◽  
Molecular Mechanisms ◽  
Muscle Development ◽  
The Body ◽  
Negative Regulator ◽  
Skeletal Muscle Hypertrophy ◽  
Myostatin Inhibition

Skeletal muscle, the most abundant tissue in the body, plays vital roles in locomotion and metabolism. Understanding the cellular processes that govern regulation of muscle mass and function represents an essential step in the development of therapeutic strategies for muscular disorders. Myostatin, a member of the TGF-β family, has been identified as a negative regulator of muscle development. Indeed, its inhibition induces an extensive skeletal muscle hypertrophy requiring the activation of Smad 1/5/8 and the Insulin/IGF-I signaling pathway, but whether other molecular mechanisms are involved in this process remains to be determined. Using transcriptomic data from various Myostatin inhibition models, we identified Pak1 as a potential mediator of Myostatin action on skeletal muscle mass. Our results show that muscle PAK1 levels are systematically increased in response to Myostatin inhibition, parallel to skeletal muscle mass, regardless of the Myostatin inhibition model. Using Pak1 knockout mice, we investigated the role of Pak1 in the skeletal muscle hypertrophy induced by different approaches of Myostatin inhibition. Our findings show that Pak1 deletion does not impede the skeletal muscle hypertrophy magnitude in response to Myostatin inhibition. Therefore, Pak1 is permissive for the skeletal muscle mass increase caused by Myostatin inhibition.

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