Akirin2 promotes slow myosin heavy chain expression by CaN/NFATc1 signaling in porcine skeletal muscle satellite cells

Chen, Xiaoling; Luo, Yi; Huang, Zhiqing; Liu, Guangmang; Zhao, Hua

doi:10.18632/oncotarget.15374

Cited by 6 publications

(6 citation statements)

References 33 publications

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“…29 Our previous studies demonstrated that Akirin2 promotes MyHC I expression. 8,9 Here, we showed that arginine upregulated Akirin2 expression. In addition, Akirin2 siRNA abolished arginine-induced MyHC I upregulation.…”

Section: ■ Discussionmentioning

confidence: 82%

“…It has been reported that Akirin2 promotes proliferation and differentiation of porcine skeletal muscle statellite cells . Our previous studies showed that Akirin2 regulates slow-twitch fiber expression by calcineurin (CaN)/nuclear factor of activated T cells c1 (NFATc1) signaling. , …”

Section: Introductionmentioning

confidence: 99%

“…7 Our previous studies showed that Akirin2 regulates slow-twitch fiber expression by calcineurin (CaN)/nuclear factor of activated T cells c1 (NFATc1) signaling. 8,9 The process of muscle fiber formation is controlled by some signaling pathways. The signaling molecule AMP-activated protein kinase (AMPK) is a heterotrimer that comprises a catalytic α and regulatory β and γ subunits.…”

Section: ■ Introductionmentioning

confidence: 99%

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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

Chen

Guo

Jia

et al. 2018

J. Agric. Food Chem.

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This study aimed to investigate the effect of arginine on the expression of slow myosin heavy chain (MyHC) I and its underlying mechanism in porcine skeletal muscle satellite cells. Our results showed that arginine upregulated the mRNA (1.54 ± 0.08; p < 0.01) and protein (2.01 ± 0.01; p < 0.001) levels of MyHC I. We also showed that arginine upregulated the expression of Akirin2 (1.35 ± 0.1; p < 0.05) and increased the NO content (1.56 ± 0.04; p < 0.001). Akirin2 siRNA abolished arginine-induced upregulation of MyHC I and the increase of the NO content. In addition, arginine significantly increased the phospho-AMP-activated protein kinase (AMPK)/AMPK level (1.33 ± 0.06; p < 0.05), the AMPK content (79.55 ± 0.13; p < 0.001), and the AMPKα2 mRNA level (2.03 ± 0.20; p < 0.01). AMPKα2 silencing or AMPK inhibitor Compound C abolished arginine-induced upregulation of MyHC I. Our results provide, for the first time, evidence for the involvement of Akirin2 and the AMPK signaling pathway in arginine-induced MyHC I expression in porcine skeletal muscle satellite cells.

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Section: ■ Discussionmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

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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

Chen

Guo

Jia

et al. 2018

J. Agric. Food Chem.

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“…Studies using satellite cells isolated from porcine muscles are also consistent with a role for Akirin2 in the proliferation and differentiation of these cells [53,77]. For example, siRNA knockdown of Akirin2 led to reductions in the mitotic marker phospho-histone H3 (PH3) and incorporation of EdU whilst overexpression of Akirin2 had the opposite effects [53].…”

Section: Akirin2mentioning

confidence: 68%

Akirin proteins in development and disease: critical roles and mechanisms of action

Bösch

Peek

Smolikove

et al. 2020

Cell. Mol. Life Sci.

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The Akirin genes, which encode small, nuclear proteins, were first characterized in 2008 in Drosophila and rodents. Early studies demonstrated important roles in immune responses and tumorigenesis, which subsequent work found to be highly conserved. More recently, a multiplicity of Akirin functions, and the associated molecular mechanisms involved, have been uncovered. Here, we comprehensively review what is known about invertebrate Akirin and its two vertebrate homologues Akirin1 and Akirin2, highlighting their role in regulating gene expression changes across a number of biological systems. We detail essential roles for Akirin family proteins in the development of the brain, limb, and muscle, in meiosis, and in tumorigenesis, emphasizing associated signaling pathways. We describe data supporting the hypothesis that Akirins act as a "bridge" between a variety of transcription factors and major chromatin remodeling complexes, and discuss several important questions remaining to be addressed. In little more than a decade, Akirin proteins have gone from being completely unknown to being increasingly recognized as evolutionarily conserved mediators of gene expression programs essential for the formation and function of animals.Terms of use and reuse: academic research for non-commercial purposes, see here for full terms. https://www.springer.com/aamterms-v1

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“…The proportion of oxidized myofibers can be increased by the addition of nutrients to animal diets [ 9 ]. There is much research investigating the modification of skeletal muscle satellite cell (SMSC) proliferation and differentiation to increase the formation of myofibers, to improve the quality of skeletal muscles [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

Effects of sheep slaughter age on myogenic characteristics in skeletal muscle satellite cells

Han

Su³

et al. 2022

Anim Biosci

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Objective:The objective of this study was to investigate the effects of sheep slaughter age on myogenic characteristics in skeletal muscle satellite cells (SMSCs).Methods: Primary SMSCs were isolated from hind leg biceps femoris muscles of Wurank lambs (slaughtered at three months, Mth-3) and adults (slaughtered at fifteen months, Mth-15). SMSCs were selected by morphological observation and fluorescence staining. Myogenic Regulatory Factors (MRF) and Myosin Heavy Chain (MyHC) expressions of SMSCs were analyzed on days 1, 3, 4, and 5. Results:The expressions of Myf5, MyoD, Myf6, and MyoG in Mth-15 were significantly higher than in Mth-3 on days 1, 3, and 4 (p<0.05). However, MyoG expression in Mth-15 was significantly lower than in Mth-3 on day 5 (p<0.05). The expressions of MyHC I, MyHC IIa, A c c e p t e dA r t i c l e 3 and MyHC IIx in Mth-15 were significantly higher than in Mth-3 on days 1 and 3 (p<0.05), and MyHC IIb were significantly lower than in Mth-3 on days 3 and 4 (p<0.05). In contrast, the expression of MyHC IIx in Mth-15 was significantly lower and MyHC IIb was significantly higher than in Mth-3 on days 5 (p<0.05). Conclusion:The slaughter age altered the expression of MRFs and MyHCs in SMSCs while differentiation, which caused the variation of myogenic characteristics, and thus may affect the meat quality of Wurank sheep.

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Akirin2 promotes slow myosin heavy chain expression by CaN/NFATc1 signaling in porcine skeletal muscle satellite cells

Cited by 6 publications

References 33 publications

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

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

Akirin proteins in development and disease: critical roles and mechanisms of action

Effects of sheep slaughter age on myogenic characteristics in skeletal muscle satellite cells

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