Khurana Ashwani, Dey Chinmoy S
Signal Transduction Research Laboratory, Department of Biotechnology, National Institute of Pharmaceutical Education and Research, Punjab, India.
Differentiation. 2003 Jan;71(1):42-50. doi: 10.1046/j.1432-0436.2003.700604.x.
Skeletal muscle differentiation is marked by enhanced myotube formation and increased cytoskeletal rearrangement. Actin, a cytoskeletal protein is involved in various cellular functions such as glucose transport, intracellular trafficking, cell shape, and coordinated cell movement in response to various extracellular signals. The present study reveals an association between actin and p38 MAPK only in differentiated myotubes, not in proliferating myoblasts. Actin filament disassembly caused by cytochalasinD can be reversed using the potent activator of p38 MAPK, anisomycin. Pretreatment of myotubes with anisomycin partially resisted the effect of cytochalasinD. However, inhibition of p38 MAPK completely abolished the anisomycin-mediated actin remodeling. Data suggests that p38 MAPK interacts with actin and modulates actin filament rearrangement in differentiated L6E9 skeletal muscle cells.
骨骼肌分化的特征是肌管形成增强和细胞骨架重排增加。肌动蛋白是一种细胞骨架蛋白，参与多种细胞功能，如葡萄糖转运、细胞内运输、细胞形态以及响应各种细胞外信号的协调细胞运动。本研究揭示，肌动蛋白与p38丝裂原活化蛋白激酶（p38 MAPK）之间的关联仅存在于分化的肌管中，而不存在于增殖的成肌细胞中。细胞松弛素D引起的肌动蛋白丝解聚可使用p38 MAPK的强效激活剂茴香霉素逆转。用茴香霉素预处理肌管可部分抵抗细胞松弛素D的作用。然而，抑制p38 MAPK完全消除了茴香霉素介导的肌动蛋白重塑。数据表明，p38 MAPK与肌动蛋白相互作用，并调节分化的L6E9骨骼肌细胞中的肌动蛋白丝重排。
