{"title":"细胞松弛素 D 对豚鼠盲肠和颈动脉松弛过程的影响","authors":"Satoko Mihashi, Masaru Watanabe","doi":"10.1186/s12576-024-00918-3","DOIUrl":null,"url":null,"abstract":"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 Ca2+ removal after Ca2+-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.","PeriodicalId":22836,"journal":{"name":"The Journal of Physiological Sciences","volume":"34 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Effects of cytochalasin D on relaxation process of skinned taenia cecum and carotid artery from guinea pig\",\"authors\":\"Satoko Mihashi, Masaru Watanabe\",\"doi\":\"10.1186/s12576-024-00918-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"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 Ca2+ removal after Ca2+-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.\",\"PeriodicalId\":22836,\"journal\":{\"name\":\"The Journal of Physiological Sciences\",\"volume\":\"34 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-04-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Journal of Physiological Sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1186/s12576-024-00918-3\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Physiological Sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1186/s12576-024-00918-3","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
众所周知,肌动蛋白相关调节机制有助于平滑肌的收缩/松弛。为了明确肌动蛋白丝的聚合/解聚调节是否会影响松弛过程,我们研究了细胞松弛素 D 对豚鼠盲肠和颈动脉制备物在 Ca2+ 诱导收缩后通过 Ca2+ 去除松弛过程的影响。肌动蛋白聚合抑制剂细胞松弛素 D 能显著抑制带皮盲肠和颈动脉松弛时的收缩力。对松弛过程的数据拟合分析表明,细胞松弛素 D 会加速慢速(闩锁样)桥接解离。细胞松弛素 D 似乎直接破坏了肌动蛋白丝的组织或其长度,导致肌动蛋白丝结构的改变,从而阻止了肌球蛋白的结合。
Effects of cytochalasin D on relaxation process of skinned taenia cecum and carotid artery from guinea pig
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 Ca2+ removal after Ca2+-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.