Actin-associated protein palladin is required for migration behavior and differentiation potential of C2C12 myoblast cells

• Published in: Biochemical and biophysical research communications 2014-09, Vol.452 (3), p.728-733
• Main Authors: Nguyen, Ngoc Uyen Nhi, Liang, Vincent Roderick, Wang, Hao-Ven
• Format: Article
• Language: English
• Subjects: 60 APPLIED LIFE SCIENCES; ACTIN; Actin Cytoskeleton - chemistry; Actin Cytoskeleton - genetics; Actin Cytoskeleton - metabolism; Actins - genetics; Actins - metabolism; ANIMAL TISSUES; Animals; C2C12; Cell Differentiation; Cell Line; Cell Movement; CELL PROLIFERATION; Cell Survival; Cytoskeletal Proteins - antagonists & inhibitors; Cytoskeletal Proteins - genetics; Cytoskeletal Proteins - metabolism; Differentiation; Gene Expression Regulation; IN VITRO; MICE; Migration; MODULATION; Muscle Development - genetics; MYOBLASTS; Myoblasts - cytology; Myoblasts - metabolism; Myogenesis; MYOSIN; Myosin Heavy Chains - genetics; Myosin Heavy Chains - metabolism; Palladin; Phosphoproteins - antagonists & inhibitors; Phosphoproteins - genetics; Phosphoproteins - metabolism; Proliferation; RNA; RNA, Small Interfering - genetics; RNA, Small Interfering - metabolism; Signal Transduction; VIABILITY
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2014.08.143

•Palladin is involved in myogenesis in vitro.•Palladin knockdown by siRNA increases myoblast proliferation, viability and differentiation.•Palladin knockdown decreases C2C12 myoblast migration ability. The actin-associated protein palladin has been shown to be involved in differentiation processes in non-muscle tissues. However, but its function in skeletal muscle has rarely been studied. Palladin plays important roles in the regulation of diverse actin-related signaling in a number of cell types. Since intact actin-cytoskeletal remodeling is necessary for myogenesis, in the present study, we pursue to investigate the role of actin-associated palladin in skeletal muscle differentiation. Palladin in C2C12 myoblasts is knocked-down using specific small interfering RNA (siRNA). The results show that down-regulation of palladin decreased migratory activity of mouse skeletal muscle C2C12 myoblasts. Furthermore, the depletion of palladin enhances C2C12 vitality and proliferation. Of note, the loss of palladin promotes C2C12 to express the myosin heavy chain, suggesting that palladin has a role in the modulation of C2C12 differentiation. It is thus proposed that palladin is required for normal C2C12 myogenesis in vitro.