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作者机构:Univ Bergen Expt Cardiol Unit Dept Radiol N-5021 Bergen Norway Duke Univ Med Ctr Dept Cell Biol Div Physiol Durham NC 27710 USA Duke Univ Med Ctr Dept Pathol Durham NC 27710 USA Univ Bergen Dept Pathol Gade Inst N-5021 Bergen Norway
出 版 物:《HISTOCHEMISTRY AND CELL BIOLOGY》 (组织化学和细胞生物学)
年 卷 期:1999年第112卷第4期
页 面:307-316页
核心收录:
学科分类:0710[理学-生物学] 07[理学] 071009[理学-细胞生物学] 09[农学] 0804[工学-仪器科学与技术] 0901[农学-作物学] 090102[农学-作物遗传育种]
基 金:United States-Norway Fulbright Foundation Norges Forskningsråd
主 题:细胞膜/超微结构 细胞 培养的 细胞支架蛋白质类/代谢 细胞支架蛋白质类/超微结构 细胞骨架/代谢 细胞骨架/超微结构 细胞内膜/代谢 细胞内膜/超微结构 显微镜检查 共焦 显微镜检查 免疫电子 心肌/细胞学 心肌/代谢 动物 鸡胚
摘 要:Distribution of cytoskeletal proteins with emphasis on the membrane-cytoskeleton interface was examined in cultured cardiac myocytes. Using specific antibodies recognizing alpha-sarcomeric actin, desmin, beta-tubulin, spectrin/alpha-fodrin and ankyrin, respectively, the cellular localization of these cytoskeletal proteins was detected by laser scanning confocal microscopy. In addition, the fine filamentous structure of these proteins was identified by combining silver-enhanced immunogold labelling with electron microscopy. The latter technique employed the sequence of quick-freezing, deep-etching and rotary shadowing of the specimens. Conventional transmission electron microscopy of the spherical cardiac myocytes revealed a filamentous submembranous layer, approximately 100 nm thick. Specific immunolabelling of alpha-sarcomeric actin and spectrin/alpha-fodrin as well as ankyrin was seen beneath the plasmalemma. A three-dimensional meshwork of spectrin/alpha-fodrin was shown. Numerous desmin filaments that exhibited a tortuous course throughout the cells were also observed running in parallel with the surface in the submembranous area, whereas beta-tubulin was infrequently detected in these areas. In conclusion, the present study shows that spherical cardiac myocytes contain a distinct and complex three-dimensional membrane skeleton. Major constituents of this distinct submembranous layer were spectrin/alpha-fodrin fibres as well as actin and desmin filaments.