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平滑肌细胞中肌动蛋白-膜附着的几何学:纽蛋白和α-辅肌动蛋白的定位

Geometry of actin-membrane attachments in the smooth muscle cell: the localisations of vinculin and alpha-actinin.

作者信息

Small J V

出版信息

EMBO J. 1985 Jan;4(1):45-9. doi: 10.1002/j.1460-2075.1985.tb02315.x.

Abstract

Antibodies to vinculin, a component of actin-membrane attachment sites, revealed by immunofluorescence microscopy a parallel co-axial array of continuous rib-like bands on the surface of isolated vertebrate smooth muscle cells. Images of extended and shortened cells showed that these ribs remain co-axially organised on contraction. Reference to earlier studies and labelling of thin sections indicates that the ribs correspond in position to the adhesion plaques previously described in electron microscope studies. Alpha-actinin showed a punctate distribution consistent with its presence in the cytoplasmic dense bodies, but did not show a constant association with the vinculin-containing ribs. It is suggested that alpha-actinin is an intracellular actin linker and not membrane associated, as earlier supposed, and that vinculin is, as deduced by others, a mediator of actin membrane attachment. The apparent co-association of these two proteins, noted previously, is concluded to arise from the inevitable geometrical apposition of peripheral and pre-terminal parts of the contractile machinery with the cell membrane.

摘要

用免疫荧光显微镜观察发现,针对肌动蛋白-膜附着位点的一个组成部分纽蛋白的抗体,在分离的脊椎动物平滑肌细胞表面呈现出连续的肋状条带平行共轴排列。伸展和缩短细胞的图像显示,这些肋条在收缩时仍保持共轴排列。参考早期研究以及薄切片的标记表明,这些肋条在位置上与先前电子显微镜研究中描述的黏着斑相对应。α-辅肌动蛋白呈现出点状分布,与其存在于细胞质致密体中一致,但并未显示出与含纽蛋白的肋条有恒定关联。研究表明,α-辅肌动蛋白是一种细胞内肌动蛋白连接蛋白,并非如先前推测的那样与膜相关,并且如其他人所推断的,纽蛋白是肌动蛋白与膜附着的介质。先前注意到的这两种蛋白质的明显共关联,被认为是由于收缩机制的外周和末端前部分与细胞膜不可避免的几何并置所致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa7c/554149/63bcbc4e8fca/emboj00266-0052-a.jpg

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