STRESS FIBER SARCOMERES OF FIBROBLASTS ARE CONTRACTILE

STRESS FIBER SARCOMERES OF FIBROBLASTS ARE CONTRACTILE
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DOI:
10.1016/0092-8674(80)90365-7
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发表时间:
1980-01-01
期刊:
影响因子:
64.5
通讯作者:
BIRCHMEIER, W
BIRCHMEIER, W
中科院分区:
生物学1区
文献类型:
--
作者:
KREIS, TE;BIRCHMEIER, W

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将活的培养的[人]成纤维细胞用罗丹明标记的平滑肌α-SMA显微注射。辅肌动蛋白并通过视频增强荧光显微镜观察。α-辅肌动蛋白掺入到应力纤维中并呈现规则的条纹排列。荧光标记的应力纤维保持完整,尽管甘油或毛地黄皂苷提取的细胞,这些细胞模型收缩后,加入MgATP。在此过程中,α-β的部分辅肌动蛋白标记的应力纤维收缩25%,缩短在应力纤维肌节的非荧光部分进行。在甘油提取的细胞模型中,腺苷酰亚胺二磷酸,ADP和焦磷酸抑制,但钒酸盐,N-乙基马来酰亚胺修饰的重肌球蛋白,细胞松弛素B,秋水仙素,鬼笔环肽和DNA酶I没有。细胞松弛素B在甘油提取前加入到完整细胞中时具有抑制作用。这些形态学和生化研究结果表明,应力纤维肌节成纤维细胞的收缩元素,并支持的概念,肌动球蛋白系统可能参与。
Living cultured [human] fibroblasts were microinjected with rhodamine-labeled smooth muscle .alpha.-actinin and visualized by video-intensified fluorescence microscopy. The .alpha.-actinin incorporated into the stress fibers and exhibited a regularly striped arrangement. The fluorescently labeled stress fibers remained intact despite glycerol or digitonin extraction of the cells; these cell models contracted upon addition of MgATP. During this process, sections of .alpha.-actinin-labeled stress fibers contracted up to 25%; shortening proceeded in the nonfluorescent part of the stress fiber sarcomeres. In glycerol-extracted cell models, adenylylimidodiphosphate, ADP and pyrophosphate inhibited but vanadate, N-ethylmaleimide-modified heavy meromyosin, cytochalasin B, colchicine, phalloidin and DNAase I did not. Cytochalasin B was inhibitory when added to the intact cells before glycerol extraction. These morphological and biochemical findings demonstrate that stress fiber sarcomeres of fibroblasts are contractile elements and support the concept that an actomyosin system may be involved.