Role of p-anisaldehyde in the Differentiation of C2C12 Myoblasts
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In this study, we investigated whether p-anisaldehyde (PAA), the main component of essential oils derived from anise seeds, influences the differentiation of mouse C2C12 myoblasts. Cells were induced to differentiate over 5 days using a differentiation medium with or without PAA (50 or 200 mg/mL). Myotube length and diameter were measured, and the expressions of myogenic markers (myoblast determination protein 1, myogenin, myocyte enhancer factor 2, muscle creatine kinase, and myosin heavy chain) and atrophy-related genes (atrogin-1 and muscle ring finger-1 [MuRF-1]) were assessed by quantitative real-time polymerase chain reaction. Additionally, protein kinase B (Akt) phosphorylation was monitored by western blotting. PAA significantly induced the formation of smaller and thinner myotubes and reduced myogenic marker expression. Furthermore, PAA increased the expressions of atrogin-1 and MuRF-1 and simultaneously reduced Akt phosphorylation. Our findings indicate that PAA inhibits the myogenic differentiation of C2C12 cells by reducing the phosphorylation and activation of Akt.
Abstract
In this study, we investigated whether p-anisaldehyde (PAA), the main component of essential oils derived from anise seeds, influences the differentiation of mouse C2C12 myoblasts. Cells were induced to differentiate over 5 days using a differentiation medium with or without PAA (50 or 200 mg/mL). Myotube length and diameter were measured, and the expressions of myogenic markers (myoblast determination protein 1, myogenin, myocyte enhancer factor 2, muscle creatine kinase, and myosin heavy chain) and atrophy-related genes (atrogin-1 and muscle ring finger-1 [MuRF-1]) were assessed by quantitative real-time polymerase chain reaction. Additionally, protein kinase B (Akt) phosphorylation was monitored by western blotting. PAA significantly induced the formation of smaller and thinner myotubes and reduced myogenic marker expression. Furthermore, PAA increased the expressions of atrogin-1 and MuRF-1 and simultaneously reduced Akt phosphorylation. Our findings indicate that PAA inhibits the myogenic differentiation of C2C12 cells by reducing the phosphorylation and activation of Akt.
참고문헌 (30)
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