Department of Frontier Health Sciences, Graduate School of Human Health Sciences, Tokyo Metropolitan University, 7-2-10 Higashiogu, Arakawa-Ku, Tokyo, 116-8551, Japan.
J Physiol Sci. 2024 Apr 10;74(1):24. doi: 10.1186/s12576-024-00918-3.
Actin linked regulatory mechanisms are known to contribute contraction/relaxation in smooth muscle. In order to clarify whether modulation of polymerization/depolymerization of actin filaments affects relaxation process, we examined the effects of cytochalasin D on relaxation process by Ca removal after Ca-induced contraction of β-escin skinned (cell membrane permeabilized) taenia cecum and carotid artery preparations from guinea pigs. Cytochalasin D, an inhibitor of actin polymerization, significantly suppressed the force during relaxation both in skinned taenia cecum and carotid artery. The data fitting analysis of the relaxation processes indicates that cytochalasin D accelerates slow (latch-like) bridge dissociation. Cytochalasin D seems to directly disrupts actin filament organization or its length, resulting in modulation of actin filament structure that prevents myosin binding.
众所周知,肌动蛋白连接的调节机制有助于平滑肌的收缩/松弛。为了阐明肌动蛋白丝的聚合/解聚调节是否影响松弛过程,我们研究了细胞松弛素 D 对去 Ca 后由 Ca 诱导的β-刀豆球蛋白去皮(细胞膜通透化)豚鼠回肠和颈动脉制剂收缩引起的松弛过程的影响。细胞松弛素 D 是肌动蛋白聚合的抑制剂,它显著抑制了在去皮回肠和颈动脉中的松弛过程中的力。松弛过程的数据拟合分析表明,细胞松弛素 D 加速了缓慢(闩锁样)桥的解离。细胞松弛素 D 似乎直接破坏肌动蛋白丝的组织或其长度,从而调节肌动蛋白丝结构,防止肌球蛋白结合。