Branched-chain amino acids and arginine suppress MaFbx/atrogin-1 mRNA expression via mTOR pathway in C2C12 cell line

Herningtyas, Elizabeth Henny; Okimura, Yasuhiko; Handayaningsih, Anastasia Evi; Yamamoto, Daisuke; Maki, Taiki; Iida, Keiji; Takahashi, Yutaka; Kaji, Hidesuke; Chihara, Kazuo

doi:10.1016/j.bbagen.2008.06.004

Cited by 98 publications

(73 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result agrees with the recent study by Yamamoto et al [27] showing that BCAA significantly reduced the atrogin-1 mRNA level but not the MuRF1 mRNA level in dexamethasone induced muscle atrophy in rats. Herningtyas et al [4] reported that BCAAs and arginine decreased atrogin-1 and MuRF1 mRNA levels induced by starvation in C2C12 myocytes. Also, Maki et al [2] reported that oral BCAA administration suppressed atrogin-1 and MuRF1 protein expression during hindlimb suspension.…”

Section: Discussionmentioning

confidence: 99%

“…Muscle atrophy is characterized by a decrease in protein synthesis, an increase in protein degradation, or simultaneous changes in both processes and occurs in a variety of catabolic conditions such as prolonged disuse, denervation, aging, and cancer [3,4]. Among several methods such as hindlimb suspension, limb casting or surgical tenotomy, the hindlimb suspension model is the most effective and well-designed animal model for investigating muscle atrophy due to weightlessness [5,6].…”

Section: Introduction *mentioning

confidence: 99%

“…The main signaling pathway regulating protein synthesis is the IGF-1/Akt/mTOR pathway and the ability of BCAA to increase protein synthesis seems to rely on mTOR activation [21]. Furthermore, mTOR has an inhibitory effect due to BCAA on atrogin-1mRNA expression in C2C12 myocytes [4]. Sandri et al [22] reported that IGF-1 treatment or Akt overexpression inhibit FoxO and atrogin-1 expression in cultured myotubes undergoing atrophy.…”

mentioning

confidence: 99%

“…Among several experimental models inducing disuse muscle atrophy, the hindlimb suspension model is a well-designed animal model [5,6,19]. Atrogin-1 and MuRF1 are up-regulated up to 3 fold in hindlimb suspension, immobilization and denervation [4,17].…”

mentioning

confidence: 99%

See 3 more Smart Citations

Protective effect of branched chain amino acids on hindlimb suspension-induced muscle atrophy in growing rats

Jang¹,

Yun²,

Park³

et al. 2015

J. Exerc. Nutr, Biochem.

View full text Add to dashboard Cite

Protective effect of branched chain amino acids on hindlimb suspension-induced muscle atrophy in growing rats. JENB., Vol. 19, No. 3, pp.183-189, 2015 [Purpose] The effect of BCAA (branched chain amino acid) administration on muscle atrophy during growth phases is not well known. We investigated whether BCAA administration can prevent the muscle atrophy induced by hindlimb suspension in growing male rats. [Methods] Male Wistar rats were assigned to 1 of 2 groups (n = 7/group): hindlimb suspension and hindlimb suspension with oral BCAA administration (600 mg·kg -1 ·day -1

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introduction *mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Protective effect of branched chain amino acids on hindlimb suspension-induced muscle atrophy in growing rats

Jang¹,

Yun²,

Park³

et al. 2015

J. Exerc. Nutr, Biochem.

View full text Add to dashboard Cite

show abstract

“…The latter allows eIF4E to form an eIF4F complex with eIF4A and eIF4G, and this complex is associated with mRNA in the translation processes. Furthermore, it has been reported that activated mTOR inhibits the autophagy system 23) and the ubiquitinproteasome system 24) . From these findings, it is evident that leucine stimulates protein accretion in skeletal muscles.…”

Section: Regulation Of Protein Metabolism By Leucinementioning

confidence: 99%

Effects of protein and amino acid supplementation on muscle protein metabolism in relation to exercise

Shimomura

Kitaura

Shimomura

2012

JPFSM

View full text Add to dashboard Cite

Exercise promotes protein and amino acid breakdown in skeletal muscle. Proper nutrient intake in relation to exercise is thus important to maintain or build up skeletal muscle. It has been demonstrated that supplementation of branched-chain amino acids (BCAAs) before exercise has beneficial effects on skeletal muscle, such as decreasing exercise-induced muscle damage and soreness. Protein synthesis in skeletal muscle is enhanced after exercise, and proper timing of supplementation of protein and amino acids for effectively stimulating muscle protein synthesis is herein discussed. Treatment of elderly individuals with exercise and nutrient supplementation is also demonstrated to have efficacy against age-related sarcopenia.

show abstract

Leucine elicits myotube hypertrophy and enhances maximal contractile force in tissue engineered skeletal muscle in vitro

Martin

Turner

Farrington

et al. 2017

Journal Cellular Physiology

View full text Add to dashboard Cite

The amino acid leucine is thought to be important for skeletal muscle growth by virtue of its ability to acutely activate mTORC1 and enhance muscle protein synthesis, yet little data exist regarding its impact on skeletal muscle size and its ability to produce force. We utilized a tissue engineering approach in order to test whether supplementing culture medium with leucine could enhance mTORC1 signaling, myotube growth, and muscle function. Phosphorylation of the mTORC1 target proteins 4EBP‐1 and rpS6 and myotube hypertrophy appeared to occur in a dose dependent manner, with 5 and 20 mM of leucine inducing similar effects, which were greater than those seen with 1 mM. Maximal contractile force was also elevated with leucine supplementation; however, although this did not appear to be enhanced with increasing leucine doses, this effect was completely ablated by co‐incubation with the mTOR inhibitor rapamycin, showing that the augmented force production in the presence of leucine was mTOR sensitive. Finally, by using electrical stimulation to induce chronic (24 hr) contraction of engineered skeletal muscle constructs, we were able to show that the effects of leucine and muscle contraction are additive, since the two stimuli had cumulative effects on maximal contractile force production. These results extend our current knowledge of the efficacy of leucine as an anabolic nutritional aid showing for the first time that leucine supplementation may augment skeletal muscle functional capacity, and furthermore validates the use of engineered skeletal muscle for highly‐controlled investigations into nutritional regulation of muscle physiology.

show abstract

Branched-chain amino acids and arginine suppress MaFbx/atrogin-1 mRNA expression via mTOR pathway in C2C12 cell line

Cited by 98 publications

References 30 publications

Protective effect of branched chain amino acids on hindlimb suspension-induced muscle atrophy in growing rats

Protective effect of branched chain amino acids on hindlimb suspension-induced muscle atrophy in growing rats

Effects of protein and amino acid supplementation on muscle protein metabolism in relation to exercise

Leucine elicits myotube hypertrophy and enhances maximal contractile force in tissue engineered skeletal muscle in vitro

Contact Info

Product

Resources

About