Myostatin Increases Smad2 Phosphorylation and Atrogin-1 Expression in Chick Embryonic Myotubes

Saneyasu, Takaoki; Honda, Kazuhisa; Kamisoyama, Hiroshi

doi:10.2141/jpsa.0180092

Cited by 15 publications

(9 citation statements)

References 37 publications

(51 reference statements)

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“…In 1997, it was reported that skeletal muscle mass markedly increased in myostatin gene-knockout mice, which attracted attention as a factor regulating muscle mass (79). Myostatin binds to activin type IIB receptor and ALK4/ALK5 coreceptor, promotes phosphorylation of Smad2 and Smad3 proteins, and suppresses the expression of genes involved in skeletal muscle differentiation (80,81). Myostatin has also been reported to inhibit the PI3K/Akt signaling pathway (82).…”

Section: Myokines and Sarcopeniamentioning

confidence: 99%

Pathophysiology and mechanisms of primary sarcopenia (Review)

et al. 2021

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Aging causes skeletal muscle atrophy, and myofiber loss can be a critical component of this process. In 1989, Rosenberg emphasized the importance of the loss of skeletal muscle mass that occurs with aging and coined the term 'sarcopenia'. Since then, sarcopenia has attracted considerable attention due to the aging population in developed countries. The presence of sarcopenia is closely related to staggering, falls and even frailty in the elderly, which in turn leads to the need for nursing care. Sarcopenia is often associated with a poor prognosis in the elderly. Therefore, it is crucial to investigate the causes and pathogenesis of sarcopenia, and to develop and introduce interventional strategies in line with these causes and pathogenesis. Sarcopenia can be a primary component of physical frailty. The association between sarcopenia, frailty and locomotive syndrome is complex; however, sarcopenia is a muscle-specific concept that is relatively easy to approach in research. In the elderly, a lack of exercise, malnutrition and hormonal changes lead to neuromuscular junction insufficiency, impaired capillary blood flow, reduced repair and regeneration capacity due to a decrease in the number of muscle satellite cells, the infiltration of inflammatory cells and oxidative stress, resulting in muscle protein degradation exceeding synthesis. In addition, mitochondrial dysfunction causes metabolic abnormalities, such as insulin resistance, which may lead to quantitative and qualitative abnormalities in skeletal muscle, resulting in sarcopenia. The present review article focuses on age-related primary sarcopenia and outlines its pathogenesis and mechanisms.

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Section: Myokines and Sarcopeniamentioning

confidence: 99%

Pathophysiology and mechanisms of primary sarcopenia (Review)

et al. 2021

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“…Real-time PCR analysis was performed as previously described[ 31 , 32 , 33 ]. Total RNA was extracted from tissues using Sepazol-RNA I Super G (Nacalai Tesque, Inc., Kyoto, Japan).…”

Section: Methodsmentioning

confidence: 99%

Effects of Amino Acid Supplementation to a Low-Protein Diet on the Growth Performance and Protein Metabolism-related Factors in Broiler Chicks

El-far,

Kamiya,

Saneyasu

et al. 2024

J. Poult. Sci.

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A low-protein (LP) diet may alleviate the environmental impact of chicken meat production by reducing nitrogen excretion and ammonia emissions. Thus, this study investigated the effect of a 15% reduced protein diet with or without amino acid (AA) supplementation on the growth performance of broiler chicks from 10 to 35 days of age and the underlying mechanism for loss of skeletal muscle mass. Thirty-six male broiler chicks were allocated to three experimental groups based on body weight: control, LP, and essential AA-supplemented LP (LP+AA). The body weight gain, feed conversion ratio, and weight of breast muscles and legs significantly decreased only in the LP group at the end of the feeding period. Plasma uric acid levels were significantly lower in the LP+AA group than those of the other groups. In the LP group, mRNA levels of microtubule-associated protein 1 light chain 3 isoform B were significantly higher in the pectoralis major , whereas those of atrogin-1, muscle RING-finger protein-1, and myoblast determination protein 1 were significantly higher in the biceps femoris compared to those in the control group. There were no significant differences in insulin-like growth factor 1 mRNA levels in the liver or skeletal muscle between groups. These findings suggested that supplementation with essential AAs ameliorated the impaired effects of an LP diet on growth performance in broiler chicks, and that the transcriptional changes in proteolytic genes in skeletal muscles might be related to the impaired effects of the LP diet.

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“…Lysates of chicken embryonic myotubes prepared in a previous study (Saneyasu et al, 2019b) were used as the positive control. Bands were detected using Chemi-Lumi One Super (Nacalai Tesque, Inc., Kyoto, Japan), visualized with LumiCube (Liponics Inc., Tokyo, Japan), and quantified using the CS Analyzer software (ATTO Co., Tokyo, Japan).…”

Section: Western Blot Analysismentioning

confidence: 99%

“…C: Western blot analysis of Smad2/3. The lysates of chicken embryonic myotubes were prepared according to a previous study(Saneyasu et al, 2019b) and used as a positive control in the present study. CEM, chicken embryonic myotubes; Mstn, myostatin.…”

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confidence: 99%

Role of Hypothalamic Transforming Growth Factor-β (TGF-β)/Smad Signaling in Feeding Regulation in Chickens

et al. 2022

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Previous studies in mammalian obesity models have suggested that central transforming growth factor-β (TGF-β) controls the gene expression of appetite-regulating neuropeptides and peripheral energy metabolism. In the present study, we investigated the possible involvement of central TGF-β/Smad signaling in feeding regulation in chickens. Central administration of TGF-β1 resulted in phosphorylation of Smad2 in the hypothalamus of chicks and suppressed feed intake without changing the gene expression of hypothalamic appetite-regulating neuropeptides (neuropeptide Y, agouti-related protein, proopiomelanocortin, and corticotropin-releasing factor). However, neither fasting nor refeeding induced the phosphorylation of hypothalamic Smad2. These findings suggest that the activation of hypothalamic TGF-β/Smad signaling suppresses feed intake in chicks but it might not occur in response to feeding status.

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Myostatin Increases Smad2 Phosphorylation and Atrogin-1 Expression in Chick Embryonic Myotubes

Cited by 15 publications

References 37 publications

Pathophysiology and mechanisms of primary sarcopenia (Review)

Pathophysiology and mechanisms of primary sarcopenia (Review)

Effects of Amino Acid Supplementation to a Low-Protein Diet on the Growth Performance and Protein Metabolism-related Factors in Broiler Chicks

Role of Hypothalamic Transforming Growth Factor-β (TGF-β)/Smad Signaling in Feeding Regulation in Chickens

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