Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation

Bae, Gyu‐Un; Lee, Jae-Rin; Kim, Bok-Geon; Han, Jiwon; Leem, Young-Eun; Lee, Hey-Jin; Ho, Seok‐Man; Hahn, Myong‐Joon; Kang, Jong‐Sun

doi:10.1091/mbc.e09-12-1011

Cited by 52 publications

(71 citation statements)

References 54 publications

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“…Cell Culture and Expression Vectors-C2C12 and 293T cells were cultured as described previously (38). C2C12 cells were cultured in Dulbecco modified Eagle's medium (DMEM) containing 15% fetal bovine serum (growth medium) and induced to differentiate at near confluence in DMEM, 2% horse serum (differentiation medium (DM)).…”

Section: Methodsmentioning

confidence: 99%

“…C2C12 cells were cultured in Dulbecco modified Eagle's medium (DMEM) containing 15% fetal bovine serum (growth medium) and induced to differentiate at near confluence in DMEM, 2% horse serum (differentiation medium (DM)). Myotube formation in stable and transient transfection assays was quantified as described previously (38). Primary myoblasts were obtained from the hind limbs of wild type and Cdo Ϫ/Ϫ mice as described previously (34).…”

Section: Methodsmentioning

confidence: 99%

“…Drug-resistant cells were pooled and analyzed for Western blotting or MHC staining. The rescue ability of ASK1 and TAK1 for differentiation of Cdo-depleted C2C12 cells was assessed by a transient coexpression approach as described previously (38). Briefly, those cells were cotransfected with ASK1 or TAK1 expression vector plus a GFP expression vector with a ratio of 10:1, respectively.…”

Section: Methodsmentioning

confidence: 99%

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TGF-β-activated Kinase 1 (TAK1) and Apoptosis Signal-regulating Kinase 1 (ASK1) Interact with the Promyogenic Receptor Cdo to Promote Myogenic Differentiation via Activation of p38MAPK Pathway

Tran

Kim

et al. 2012

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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TGF-β-activated Kinase 1 (TAK1) and Apoptosis Signal-regulating Kinase 1 (ASK1) Interact with the Promyogenic Receptor Cdo to Promote Myogenic Differentiation via Activation of p38MAPK Pathway

Tran

Kim

et al. 2012

Journal of Biological Chemistry

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“…Quantitative RT-PCR (qRT-PCR) analysis was carried out as previously described (40) Western blot analysis was performed as previously described (41,42). Briefly, cells were lysed in cell extraction buffer (10 mmol/L Tris-HCl, pH 8.0; 150 mmol/L NaCl; 1 mmol/L EDTA; and 1% Triton X-100) containing complete protease inhibitor cocktail (Roche), followed by SDS-PAGE and incubation with primary and secondary antibodies.…”

Section: Rna Protein Analysis and Mitochondrial Dna Contentsmentioning

confidence: 99%

“…Cell Culture, Constructs, Luciferase Assay, and Chromatin Immunoprecipitation C2C12 myoblasts (44) and 293T and 10T1/2 cells were cultured as previously described (41). For the generation of stable cell lines, C2C12 cells were transfected with pSuper or pSuper/Prmt7 short hairpin (sh)RNA and selected with 1 mg/mL puromycin followed by pooling the colonies and analyzed.…”

Section: Rna Protein Analysis and Mitochondrial Dna Contentsmentioning

confidence: 99%

Prmt7 Deficiency Causes Reduced Skeletal Muscle Oxidative Metabolism and Age-Related Obesity

et al. 2016

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Maintenance of skeletal muscle function is critical for metabolic health and the disruption of which exacerbates many chronic diseases such as obesity and diabetes. Skeletal muscle responds to exercise or metabolic demands by a fiber-type switch regulated by signaling-transcription networks that remains to be fully defined. Here, we report that protein arginine methyltransferase 7 (Prmt7) is a key regulator for skeletal muscle oxidative metabolism. Prmt7 is expressed at the highest levels in skeletal muscle and decreased in skeletal muscles with age or obesity. Prmt7−/− muscles exhibit decreased oxidative metabolism with decreased expression of genes involved in muscle oxidative metabolism, including PGC-1α. Consistently, Prmt7−/− mice exhibited significantly reduced endurance exercise capacities. Furthermore, Prmt7−/− mice exhibit decreased energy expenditure, which might contribute to the exacerbated age-related obesity of Prmt7−/− mice. Similarly to Prmt7−/− muscles, Prmt7 depletion in myoblasts also reduces PGC-1α expression and PGC-1α–promoter driven reporter activities. Prmt7 regulates PGC-1α expression through interaction with and activation of p38 mitogen-activated protein kinase (p38MAPK), which in turn activates ATF2, an upstream transcriptional activator for PGC-1α. Taken together, Prmt7 is a novel regulator for muscle oxidative metabolism via activation of p38MAPK/ATF2/PGC-1α.

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Indoprofen prevents muscle wasting in aged mice through activation of PDK1/AKT pathway

Kim

Cho

Jeong

et al. 2020

J cachexia sarcopenia muscle

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Background Muscle wasting, resulting from aging or pathological conditions, leads to reduced quality of life, increased morbidity, and increased mortality. Much research effort has been focused on the development of exercise mimetics to prevent muscle atrophy and weakness. In this study, we identified indoprofen from a screen for peroxisome proliferator‐activated receptor γ coactivator α (PGC‐1α) inducers and report its potential as a drug for muscle wasting. Methods The effects of indoprofen treatment on dexamethasone‐induced atrophy in mice and in 3‐phosphoinositide‐dependent protein kinase‐1 (PDK1)‐deleted C2C12 myotubes were evaluated by immunoblotting to determine the expression levels of myosin heavy chain and anabolic‐related and oxidative metabolism‐related proteins. Young, old, and disuse‐induced muscle atrophic mice were administered indoprofen (2 mg/kg body weight) by gavage. Body weight, muscle weight, grip strength, isometric force, and muscle histology were assessed. The expression levels of muscle mass‐related and function‐related proteins were analysed by immunoblotting or immunostaining. Results In young (3‐month‐old) and aged (22‐month‐old) mice, indoprofen treatment activated oxidative metabolism‐related enzymes and led to increased muscle mass. Mechanistic analysis using animal models and muscle cells revealed that indoprofen treatment induced the sequential activation of AKT/p70S6 kinase (S6K) and AMP‐activated protein kinase (AMPK), which in turn can augment protein synthesis and PGC‐1α induction, respectively. Structural prediction analysis identified PDK1 as a target of indoprofen and, indeed, short‐term treatment with indoprofen activated the PDK1/AKT/S6K pathway in muscle cells. Consistent with this finding, PDK1 inhibition abrogated indoprofen‐induced AKT/S6K activation and hypertrophic response. Conclusions Our findings demonstrate the effects of indoprofen in boosting skeletal muscle mass through the sequential activation of PDK1/AKT/S6K and AMPK/PGC‐1α. Taken together, our results suggest that indoprofen represents a potential drug to prevent muscle wasting and weakness related to aging or muscle diseases.

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Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation

Cited by 52 publications

References 54 publications

TGF-β-activated Kinase 1 (TAK1) and Apoptosis Signal-regulating Kinase 1 (ASK1) Interact with the Promyogenic Receptor Cdo to Promote Myogenic Differentiation via Activation of p38MAPK Pathway

TGF-β-activated Kinase 1 (TAK1) and Apoptosis Signal-regulating Kinase 1 (ASK1) Interact with the Promyogenic Receptor Cdo to Promote Myogenic Differentiation via Activation of p38MAPK Pathway

Prmt7 Deficiency Causes Reduced Skeletal Muscle Oxidative Metabolism and Age-Related Obesity

Indoprofen prevents muscle wasting in aged mice through activation of PDK1/AKT pathway

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