Arginine Promotes Slow Myosin Heavy Chain Expression via Akirin2 and the AMP-Activated Protein Kinase Signaling Pathway in Porcine Skeletal Muscle Satellite Cells

Chen, Xiaoling; Guo, Yafei; Jia, Gang; Zhao, Hua; Liu, Guangmang; Huang, Zhiqing

doi:10.1021/acs.jafc.8b00775

Cited by 15 publications

(17 citation statements)

References 32 publications

(54 reference statements)

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“…Thus, we build the in vitro cell culture model that additional amino acids (Met, Leu, or Lys) adding into the culture medium at the selected concentrations (0.6 mM) can significantly promote milk synthesis and activation of the mTOR signaling. The in vitro cell culture models in some literatures are similar to ours (Chen et al, ; Dong et al, ; Guo et al, ; Li et al, ).…”

Section: Discussionsupporting

confidence: 74%

Amino acids stimulate glycyl‐tRNA synthetase nuclear localization for mammalian target of rapamycin expression in bovine mammary epithelial cells

Luo

Huang

et al. 2018

Journal Cellular Physiology

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Amino acids are required for the activation of mammalian target of rapamycin (mTOR) to increase cell growth, protein and lipid synthesis, and inhibit autophagy.However, the mechanism through which amino acids activate the mTOR signaling is still largely unknown. In our previous study, we discovered that glycyl-tRNA synthetase (GlyRS) is a key mediator of amino-acid-induced mTOR expression and activation in bovine mammary epithelial cells (BMECs). Here we show that amino acids stimulate GlyRS nuclear localization for mTOR expression in BMECs. Met stimulates GlyRS nuclear localization, and the nuclear GlyRS is cleaved into a C-terminus-containing truncated form. We prove that GlyRS has a bipartite nuclear leading sequences, and GlyRS is phosphorylated at Thr544 and Ser704 in the cytoplasm under the stimulation of amino acids (Met, Leu, and Lys). The nuclear GlyRS physically binds to nuclear factor kappa B1, triggers its phosphorylation, thereby enhancing mRNA expression of its target genes including mTOR, S6K1, and 4EBP1. We further demonstrate that GlyRS is required for the inhibition of autophagy by Met. Thus our work elucidates that amino acids trigger GlyRS phosphorylation and nuclear localization to enhance the mRNA expression of mTOR.amino acid, autophagy, glycyl-tRNA synthetase (GlyRS), mammalian target of rapamycin (mTOR), methionine, nuclear factor kappa B1 (NFκB1)

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Section: Discussionsupporting

confidence: 74%

Amino acids stimulate glycyl‐tRNA synthetase nuclear localization for mammalian target of rapamycin expression in bovine mammary epithelial cells

Luo

Huang

et al. 2018

Journal Cellular Physiology

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“…It was previously shown that NO contributes to slow MyHC transcription by AMPK activation in myotubes (Chen et al, 2018b), so we suggested that NO content restoration during rat hindlimb unloading would activate AMPK in rat soleus muscles. However, according to the results of our experiment L-arginine administration did not lead to AMPK activation.…”

Section: Discussionmentioning

confidence: 69%

NO-Dependent Mechanisms of Myosin Heavy Chain Transcription Regulation in Rat Soleus Muscle After 7-Days Hindlimb Unloading

et al. 2020

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It is known that nitric oxide (NO) may affect myosin heavy chain (MyHC) isoform mRNA transcription in skeletal muscles. The content of NO in soleus muscles decreases during rat hindlimb unloading as well as slow MyHC mRNA transcription. We aimed to detect which signaling pathways are involved in NO-dependent prevention of hindlimbsuspension (HS)-induced changes in MyHCs' expression pattern. Male Wistar rats were divided into four groups: cage control group (C), hindlimb suspended for 7 days (7HS), hindlimb suspended for 7 days with L-arginine administration (7HS+A) (500 mg/kg body mass), and hindlimb suspended for 7 days with both L-arginine (500 mg/kg) and NO-synthase inhibitor L-NAME administration (50 mg/kg) (7HS+A+N). L-arginine treatment during 7 days of rat HS prevented HS-induced NO content decrease and slow MyHC mRNA transcription decrease and attenuated fast MyHC IIb mRNA transcription increase; it also prevented NFATc1 nuclear content decrease, calsarcin-2 expression increase, and GSK-3β Ser 9 phosphorylation decrease. Moreover, L-arginine administration prevented the HS-induced myh7b and PGC1α mRNAs content decreases and slow-type genes repressor SOX6 mRNA transcription increase. All these slow fiber-type protective effects of L-arginine were blocked in HS+A+N group, indicating that these effects were NO-dependent. Thus, NO decrease prevention during HS restores calcineurin/NFATc1 and myh7b/SOX6 signaling.

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“…The isolation and identification of porcine skeletal muscle satellite cells were performed as described in our previous study (13) . Porcine skeletal muscle satellite cells were grown in Dulbecco's modified Eagle's medium/F12 supplemented with 15 % fetal bovine serum and with 100 U/ml penicillin and 100 μg/ml streptomycin at 37°C in a 5 % CO 2 atmosphere.…”

Section: Cell Culture and Treatmentsmentioning

confidence: 99%

“…Previous studies have suggested that Arg plays multiple physiological functions in animals, such as antioxidant activity, reproductive performance and fat deposition (8)(9)(10)(11) . A few recent studies have shown that Arg promotes more type I muscle fibres formation in mice and MyHC I expression in porcine skeletal muscle satellite cells (12)(13)(14) . However, no information has been reported about the effect of Arg on type I muscle fibre type formation in weaning piglets.…”

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confidence: 99%

Arginine promotes porcine type I muscle fibres formation through improvement of mitochondrial biogenesis

et al. 2019

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The present study aimed to investigate whether arginine (Arg) promotes porcine type I muscle fibres formation via improving mitochondrial biogenesis. In the in vivo study, a total of sixty Duroc × Landrace × Yorkshire weaning piglets with an average body weight of 6·55 (sd 0·36) kg were randomly divided into four treatments and fed with a basal diet or a basal diet supplemented with 0·5, 1·0 and 1·5 % l-Arg, respectively, in a 4-week trial. Results showed that dietary supplementation of 1·0 % Arg significantly enhanced the activity of succinate dehydrogenase, up-regulated the protein expression of myosin heavy chain I (MyHC I) and increased the mRNA levels of MyHC I, troponin I1, C1 and T1 (Tnni1, Tnnc1 and Tnnt1) in longissimus dorsi muscle compared with the control group. In addition, ATPase staining analysis indicated that 1·0 % Arg supplementation significantly increased the number of type I muscle fibres and significantly decreased the number of type II muscle fibres. Furthermore, 1·0 % Arg supplementation significantly up-regulated PPAR-γ coactivator-1α (PGC-1α), sirtuin 1 and cytochrome c (Cytc) protein expressions, increased PGC-1α, nuclear respiratory factor 1 (NRF1), mitochondria transcription factor B1 (TFB1M), Cytc and ATP synthase subunit C1 (ATP5G) mRNA levels and increased mitochondrial DNA content. In the in vitro study, mitochondrial complex I inhibitor rotenone (Rot) was used. We found that Rot annulled Arg-induced type I muscle fibres formation. Together, our results provide for the first time the evidence that Arg promotes porcine type I muscle fibres formation through improvement of mitochondrial biogenesis.

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Arginine Promotes Slow Myosin Heavy Chain Expression via Akirin2 and the AMP-Activated Protein Kinase Signaling Pathway in Porcine Skeletal Muscle Satellite Cells

Cited by 15 publications

References 32 publications

Amino acids stimulate glycyl‐tRNA synthetase nuclear localization for mammalian target of rapamycin expression in bovine mammary epithelial cells

Amino acids stimulate glycyl‐tRNA synthetase nuclear localization for mammalian target of rapamycin expression in bovine mammary epithelial cells

NO-Dependent Mechanisms of Myosin Heavy Chain Transcription Regulation in Rat Soleus Muscle After 7-Days Hindlimb Unloading

Arginine promotes porcine type I muscle fibres formation through improvement of mitochondrial biogenesis

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