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鬼笔环肽和细胞松弛素B对培养大鼠肝细胞细胞骨架结构的影响。

Effects of phalloidin and cytochalasin B on cytoskeletal structures in cultured rat hepatocytes.

作者信息

Nickola I, Frimmer M

出版信息

Cell Tissue Res. 1986;245(3):635-41. doi: 10.1007/BF00218566.

Abstract

In short-term cultures of rat hepatocytes, bile canaliculi enclosed between unseparated cell couplets are able to perform periodical contractions resulting in expulsion of bile. Pericanalicular cytoskeletal proteins are involved in canalicular contractility: F-actin, myosin and tropomyosin are associated around bile canaliculi, as revealed by staining with tetramethylrhodaminyl-phalloidin and by immunofluorescence. Bile canalicular contractility is distributed by cholestatic agents that are known to interfere with actin polymerization; e.g., phalloidin and also cytochalasin B inhibit canalicular contractility and cause pericanalicular vacuolization and formation of blebs. Whereas the association of the cytoskeletal proteins is not affected by treatment with cytochalasin B, treatment with phalloidin results in dissociation of F-actin and myosin, indicating that binding of phalloidin to F-actin impairs its molecular interaction with myosin.

摘要

在大鼠肝细胞的短期培养中,未分离的细胞对之间包绕的胆小管能够进行周期性收缩,从而排出胆汁。胆小管周围的细胞骨架蛋白参与胆小管的收缩性:用四甲基罗丹明鬼笔环肽染色和免疫荧光显示,F-肌动蛋白、肌球蛋白和原肌球蛋白在胆小管周围聚集。已知干扰肌动蛋白聚合的胆汁淤积剂可抑制胆小管收缩性;例如,鬼笔环肽和细胞松弛素B均可抑制胆小管收缩性,并导致胆小管周围空泡化和形成泡状突起。虽然细胞松弛素B处理不影响细胞骨架蛋白的聚集,但鬼笔环肽处理会导致F-肌动蛋白和肌球蛋白解离,这表明鬼笔环肽与F-肌动蛋白的结合会损害其与肌球蛋白的分子相互作用。

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