Berberine Hydrochloride Protects C2C12 Myoblast Cells Against Oxidative Stress-Induced Damage via Induction of Nrf-2-Mediated HO-1 Expression

2016 ◽  
Vol 77 (6) ◽  
pp. 310-318 ◽  
Author(s):  
Yung Hyun Choi
Keyword(s):  
Oxidative Stress ◽  
C2c12 Myoblast ◽  
Berberine Hydrochloride ◽  
Myoblast Cells

scholarly journals Curcumin Ameliorated Oxidative Stress and Inflammation-Related Muscle Disorders in C2C12 Myoblast Cells

Antioxidants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 476
Author(s):  
Da-Yeon Lee ◽  
Yoon-Seok Chun ◽  
Jong-Kyu Kim ◽  
Jeong-Ok Lee ◽  
Young-Joon Lee ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Radical Scavenging ◽  
C2c12 Cells ◽  
C2c12 Myoblast ◽  
Related Factor ◽  
Dependent Manner ◽  
Quinone Oxidoreductase ◽  
Muscle Disorders ◽  
Myoblast Cells ◽  
Dose Dependent

The purpose of the current study was to investigate antioxidant and anti-inflammatory effects of spray dry powder containing 40% curcumin (CM-SD) in C2C12 myoblast cells. CM-SD increased DPPH radical scavenging activity in a dose-dependent manner, and up to 30 μg/mL of CM-SD did not express cytotoxicity in C2C12 cells. Exposure to hydrogen peroxide (H2O2) drastically decreased the viability of C2C12 cells, but pre-treatment of CM-SD significantly increased the cell viability (p < 0.01). CM-SD significantly transactivated the nuclear factor erythroid-2-related factor 2 (Nrf2)-dependent luciferase activity in a dose-dependent manner and enhanced the levels of heme oxygenase (HO)-1, glutamate cysteine ligase catalytic subunit (GCLC), and NAD(P)H-dependent quinone oxidoreductase (NQO)-1. CM-SD also significantly reduced reactive oxygen species (ROS) production and lipid peroxidation and restored glutathione (GSH) depletion in H2O2-treated C2C12 cells. Moreover, CM-SD significantly reduced lipopolysaccharides (LPS)-mediated interleukin (IL)-6 production in the conditioned medium. Results from the current study suggest that CM-SD could be a useful candidate against oxidative stress and inflammation-related muscle disorders.

Cartap-induced cytotoxicity in mouse C2C12 myoblast cell line and the roles of calcium ion and oxidative stress on the toxic effects

Toxicology ◽  
2006 ◽  
Vol 219 (1-3) ◽  
pp. 73-84 ◽  
Author(s):  
Jiunn-Wang Liao ◽  
Jaw-Jou Kang ◽  
Chian-Ren Jeng ◽  
Shao-Kuang Chang ◽  
Ming-Jang Kuo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Line ◽  
Calcium Ion ◽  
Toxic Effects ◽  
C2c12 Myoblast ◽  
Myoblast Cell Line ◽  
Myoblast Cell ◽  
And Oxidative Stress

scholarly journals 57 Carnosine prevents oxidative damage in myoblast cells derived from porcine skeletal muscle

2019 ◽  
Vol 97 (Supplement_3) ◽  
pp. 59-59
Author(s):  
Marie-France Palin ◽  
Jérôme Lapointe ◽  
Claude Gariépy ◽  
Danièle Beaudry ◽  
Claudia Kalbe
Keyword(s):  
Oxidative Stress ◽  
Oxidative Damage ◽  
Metal Ion ◽  
Antioxidant Activities ◽  
Radical Scavenging ◽  
Biochemical Properties ◽  
Antioxidant Enzyme Activities ◽  
Antioxidant Genes ◽  
Mitochondrial Functions ◽  
Myoblast Cells

Abstract Carnosine (β-alanyl-L-histidine) is a molecule naturally and exclusively present in muscle food with the highest concentrations found in skeletal muscles and brain of the animal. Among its numerous biochemical properties, carnosine has antioxidant activity which include metal ion chelation and free radical scavenging. We have recently reported that high muscle carnosine content in pig is associated with better meat quality. Moreover, supplementing pigs with β-alanine reduced oxidative damage to Longissimus muscle (LM) lipids and proteins. Among previously reported antioxidant activities, carnosine was found to limit the production of reactive oxygen species (ROS) and increase antioxidant enzyme activities. However, these studies were mainly conducted in rodents and cell lines and mechanisms in play remain to be characterized. To determine the effect of carnosine in preventing oxidative damage and characterize the mechanisms in play, we have undertaken experiments using the progeny (myoblasts) of satellite cells isolated from the LM of newborn piglets. Cells were treated with carnosine (0, 10, 25 and 50 mM) for 48 h and were then either collected immediately or treated with H2O2 (0.3 mM, 1 h) to induce an oxidative stress. Our results showed that carnosine prevents oxidative stress through the reduction of total intracellular ROS and by modulating the antioxidant system in myoblasts.Carnosine increased the mRNA abundance of NEF2L2, a transcription factor activated by oxidative stress, and several of its downstream regulated antioxidant genes. Western blot analyses further suggest that the protective effect of carnosine on H2O2-induced oxidative stress is mediated through the p38 MAPK intracellular pathway. Finally, the addition of carnosine to H2O2-treated myoblasts increased the basal cellular oxygen consumption rate (OCR), the ATP-linked OCR and proton leaks, thus suggesting an effect of carnosine on mitochondrial functions. Taken together, these findings demonstrate the important role of carnosine in preventing oxidative damage in porcine muscle cells.

scholarly journals Atractylenolide III Attenuates Muscle Wasting in Chronic Kidney Disease via the Oxidative Stress-Mediated PI3K/AKT/mTOR Pathway

2019 ◽  
Vol 2019 ◽  
pp. 1-16 ◽  
Author(s):  
Mingqing Wang ◽  
Rong Hu ◽  
Yanjing Wang ◽  
Lingyu Liu ◽  
Haiyan You ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Chronic Kidney Disease ◽  
Kidney Disease ◽  
Skeletal Muscles ◽  
Muscle Wasting ◽  
Mtor Pathway ◽  
C2c12 Myoblast ◽  
Model Group ◽  
Atractylenolide Iii

Oxidative stress contributes to muscle wasting in advanced chronic kidney disease (CKD) patients. Atractylenolide III (ATL-III), the major active constituent of Atractylodes rhizome, has been previously reported to function as an antioxidant. This study is aimed at investigating whether ATL-III has protective effects against CKD-induced muscle wasting by alleviating oxidative stress. The results showed that the levels of serum creatinine (SCr), blood urea nitrogen (BUN), and urinary protein significantly decreased in the ATL-III treatment group compared with the 5/6 nephrectomy (5/6 Nx) model group but were higher than those in the sham operation group. Skeletal muscle weight was increased, while inflammation was alleviated in the ATL-III administration group compared with the 5/6 Nx model group. ATL-III-treated rats also showed reduced dilation of the mitochondria, increased CAT, GSH-Px, and SOD activity, and decreased levels of MDA both in skeletal muscles and serum compared with 5/6 Nx model rats, suggesting that ATL-III alleviated mitochondrial damage and increased the activity of antioxidant enzymes, thus reducing the production of ROS. Furthermore, accumulated autophagosomes (APs) and autolysosomes (ALs) were reduced in the gastrocnemius (Gastroc) muscles of ATL-III-treated rats under transmission electron microscopy (TEM) together with the downregulation of LC3-II and upregulation of p62 according to Western blotting. This evidence indicated that ATL-III improved skeletal muscle atrophy and alleviated oxidative stress and autophagy in CKD rats. Furthermore, ATL-III could also increase the protein levels of p-PI3K, p-AKT, and p-mTOR in skeletal muscles in CKD rats. To further reveal the relevant mechanism, the oxidative stress-mediated PI3K/AKT/mTOR pathway was assessed, which showed that a reduced expression of p-PI3K, p-AKT, and p-mTOR in C2C12 myoblast atrophy induced by TNF-α could be upregulated by ATL-III; however, after the overexpression of Nox2 to increase ROS production, the attenuated effect was reversed. Our findings indicated that ATL-III is a potentially protective drug against muscle wasting via activation of the oxidative stress-mediated PI3K/AKT/mTOR pathway.

Mitsugumin 53 promotes mitochondrial autophagy through regulating Ambra1 expression in C2C12 myoblast cells

2019 ◽  
Vol 43 (3) ◽  
pp. 290-298 ◽  
Author(s):  
Gu Lijie ◽  
Zhang Yueyue ◽  
Zhu Nan ◽  
Wang Ling ◽  
Wang Xuan ◽  
...  
Keyword(s):  
C2c12 Myoblast ◽  
Myoblast Cells

scholarly journals Osteocalcin Induces Proliferation via Positive Activation of the PI3K/Akt, P38 MAPK Pathways and Promotes Differentiation Through Activation of the GPRC6A-ERK1/2 Pathway in C2C12 Myoblast Cells

2017 ◽  
Vol 43 (3) ◽  
pp. 1100-1112 ◽  
Author(s):  
Suifeng Liu ◽  
Feng Gao ◽  
Lei Wen ◽  
Min Ouyang ◽  
Yi Wang ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
P38 Mapk ◽  
C2c12 Cell ◽  
C2c12 Cells ◽  
Myoblast Differentiation ◽  
C2c12 Myoblast ◽  
C2c12 Myoblasts ◽  
Mapk Phosphorylation ◽  
Mapk Pathways ◽  
Myoblast Cells

Background/Aims: Sarcopenia is characterized by an age-related decline in skeletal muscle plus low muscle strength and/or physical performance. Despite the clinical significance of sarcopenia, the molecular pathways underlying sarcopenia remain elusive. The recent demonstration that undercarboxylated osteocalcin (ucOC) favours muscle function related to insulin sensitivity and glucose metabolism raises the question of whether this hormone may also regulate muscle mass. The present study explored the promotive effects of ucOC in proliferation and differentiation processes of C2C12 myoblasts as well as the possible signalling pathways involved. Methods: The effects of exogenous ucOC on C2C12 myoblasts proliferation were assessed using CCK8 and immunohistological staining assays. C2C12 cells were pretreated with PI3K/Akt or P38 MAPK inhibitors to investigate the possible involvement of the PI3K/Akt and P38 MAPK pathways in proliferation. The levels of Akt, phosphorylated-Akt (p-Akt), P38, and phosphorylated-P38 (p-P38) were measured by Western Blotting. The effects of ucOC on myoblast differentiation were quantified by morphological analysis. A silencing experiment was conducted in which the expression of GPRC6A in C2C12 myoblasts was modified. The expression of GPRC6A, myosin heavy chain (MyHC) and the related ERK1/2 signalling pathway in C2C12 myoblasts were monitored by qRT-PCR and Western Blotting. Results: We showed that treatment with exogenous ucOC stimulated the priming of C2C12 myoblasts proliferation. Inhibition of Akt phosphorylation by wortmannin or inhibition of P38 MAPK phosphorylation by SB203580 decreased C2C12 cell proliferation. Wortmannin also reduced P38 MAPK phosphorylation, whereas SB203580 did not affect Akt activation. Furthermore, ucOC promoted C2C12 myoblast differentiation. Inhibition of ERK1/2 phosphorylation with U0126 decreased C2C12 cell differentiation. Finally, GPRC6A expression was substantially increased after ucOC treatment of C2C12 cells. GPRC6A silencing inhibited Akt, P38 MAPK phosphorylation in C2C12 cells, and ERK1/2 phosphorylation in C2C12 myotubes; GPRC6A silencing also decreased cell proliferation, decreased cell differentiation, and downregulated MyHC expression. Conclusions: The present data suggest that ucOC induces myoblast proliferation via sequential activation of the PI3K/Akt and p38 MAPK pathways in C2C12 myoblast cells. Moreover, ucOC enhances myogenic differentiation via a mechanism involving GPRC6A-ERK1/2 signalling.

scholarly journals Brazilian green propolis promotes the cytoprotective expression of heme oxygenase-1 against oxidative stress injury in murine myoblast cells

2020 ◽  
Vol 10 (12) ◽  
pp. 493
Author(s):  
Wataru Otsu ◽  
Naoki Chinen ◽  
Kazuki Ohuchi ◽  
Shiori Ando ◽  
Shinsuke Nakamura ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Caffeic Acid ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Oxygen Species ◽  
Coumaric Acid ◽  
Stress Injury ◽  
Antioxidative Effects ◽  
Myoblast Cell ◽  
Myoblast Cells

Background: Sarcopenia is a progressive skeletal muscle disorder characterized by the progressive loss of muscle mass and function, resulting in physical disability and mortality. Although sarcopenia impacts a large proportion of elderly individuals, no effective treatment for this disease has yet been identified. The excessive production of reactive oxygen species (ROS) can damage tissues and promote aging, and the daily use of dietary antioxidants can be effective for maintaining skeletal muscle health. Propolis, a natural substance that is collected by honey bees, has been used as traditional medicine, and many reports have described its antioxidative properties. However, how propolis exhibits cytoprotective effects and antioxidative effects in skeletal muscles remains unclear. The purpose of this study was to investigate the antioxidative effects of ethanol-extracted Brazilian green propolis (EEBP, from Baccharis dracunculifolia) and its three constituents using an in vitro myoblast cell model.Methods: Murine myoblast C2C12 cells were treated with either EEBP or its constituents, including caffeic acid, trans-ferulic acid, and p-coumaric acid, in the presence of 100 or 300 mM H2O2 to induce oxidative stress injury. The cell death ratio and cell viability were assessed by Hoechst 33342 and propidium iodide staining and the WST-8 assay, respectively. Simultaneously, intracellular ROS production was measured by CM-H2DCFDA [5-(and-6)-chloromethyl-2’,7’-dichlorodihydrofluorescein diacetate, acetyl ester] assay. Finally, immunoblotting was performed in myoblast cell lysates to assess the expression level of an antioxidative enzyme, heme oxygenase-1 (HO-1).Results: We demonstrated that EEBP significantly reduced H2O2-induced cell death at a concentration of 3 µg/ml in myoblasts. Additionally, caffeic acid at 100 µM improved cell viability under oxidative stress conditions, but not trans-ferulic acid or p-coumaric acid. Both EEBP and caffeic acid inhibited the H2O2-induced increase in ROS production. Finally, HO-1 expression was increased by treatment with either EEBP or caffeic acid. The increase in HO-1 expression induced by H2O2 was enhanced in the presence of EEBP and caffeic acid.Conclusions: These findings indicated that EEBP has protective effects against oxidative damage in C2C12 murine myoblast cell line. Caffeic acid is an EEBP constituent that contributes to cytoprotective activity. EEBP may act as an inducer of HO-1 to prevent oxidative stress-induced myoblast death.Keywords: C2C12 murine myoblast cells, heme oxygenase-1, oxidative stress, propolis, reactive oxygen species

scholarly journals Nogo-A is critical for pro-inflammatory gene regulation in myocytes and macrophages

2020 ◽  
Author(s):  
H M Arif Ullah ◽  
A. K. Elfadl ◽  
SunYoung Park ◽  
Yong Deuk Kim ◽  
Myung-Jin Chung ◽  
...  
Keyword(s):  
Inflammatory Process ◽  
Vital Role ◽  
C2c12 Cells ◽  
Inflammatory Factors ◽  
Mdx Mice ◽  
C2c12 Myoblast ◽  
Homologous Protein ◽  
Inflammatory Processes ◽  
Myoblast Cells ◽  
Factor C

Abstract Background: Nogo-A (Rtn 4A), a member of the reticulon 4 (Rtn4) protein family, is a neurite outgrowth inhibitor protein that is primarily expressed in the central nervous system (CNS). However, the role of Nogo-A in inflammatory mechanisms remains unclear. Therefore, in this study, we used Nogo-knockout (KO) mice to explore its potential role in the inflammatory process. Here, we investigated whether Nogo-A affects the inflammatory process through transcription factor C/EBP homologous protein (CHOP). Results: Our results demonstrated that Nogo-A, CHOP, and pro-inflammatory factors were activated in the following: notexin-induced muscle injury, in human Duchenne muscular dystrophy (DMD) patients, in dystrophin-deficient (mdx) mice, in differentiated C2C12 myoblast cells, and in lipopolysaccharide (LPS)-stimulated bone marrow-derived macrophages (BMDM). Moreover, we found that Nogo-KO BMDM exhibited lower migratory ability compared with wild type (WT) BMDM after LPS treatment. Conclusion: Our data demonstrated that the Nogo-A-CHOP signaling pathway regulated the inflammatory process in notexin-induced injured muscle, in mdx mice, in DMD patients, in differentiated C2C12 cells, and in LPS-stimulated BMDM. Taken together, these results suggest that Nogo-A plays a vital role in inflammatory processes, which resembles the pathological mechanisms observed in the CNS.

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