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有孔虫运动的研究。I. 宽颈全毛虫(阿诺德)网状伪足网络的超微结构。

Studies on the motility of the foraminifera. I. Ultrastructure of the reticulopodial network of Allogromia laticollaris (Arnold).

作者信息

Travis J L, Allen R D

出版信息

J Cell Biol. 1981 Jul;90(1):211-21. doi: 10.1083/jcb.90.1.211.

Abstract

Allogromia laticollaris, a benthic marine foraminifer, extends numerous trunk filopodia that repeatedly branch, anastomose, and fuse again to form the reticulopodial network (RPN), within which an incessant streaming of cytoplasmic particles occurs. The motion of the particles is saltatory and bidirectional, even in the thinnest filopodia detected by optical microscopy. Fibrils are visible by differential interference microscopy, and the PRN displays positive birefringence in polarized light. These fibrils remain intact after lysis and extraction of the RPN in solutions that stabilize microtubules (MTs). Electron micrographs of thin sections through these lysed and stabilized cytoskeletal models reveal bundles of MTs. The RPNs of living Allogromia may be preserved by standard EM fixatives only after acclimatization to calcium-free seawater, in which the streaming is normal. The MTs in the RPN are typically arranged in bundles that generally lie parallel to the long axis of the trunk and branch filopodia. Stereo electron micrographs of whole-mount, fixed, and critical-point-dried organisms show that the complex pattern of MT deployment reflects the pattern of particle motion in both flattened and highly branched portions of the RPN. Cytoplasmic particles, some of which have a fuzzy coat, are closely associated with, and preferentially oriented along, either single MTs or MT bundles. Thin filaments (approximately 5 nm) are also observed within the network, lying parallel to and interdigitating with the MTs, and in flattened terminal areas of the filopodia. These filaments do not bind skeletal muscle myosin S1 under conditions that heavily decorate actin filaments in controls (human blood platelets), and are approximately 20% too thin to be identified ultrastructurally as F-actin.

摘要

乳突异网足虫是一种底栖海洋有孔虫,它伸出许多主干丝状伪足,这些伪足反复分支、相互吻合并再次融合,形成网状伪足网络(RPN),在该网络内细胞质颗粒持续流动。即使在光学显微镜检测到的最细的丝状伪足中,颗粒的运动也是跳跃式且双向的。通过微分干涉显微镜可以看到纤维,并且网状伪足网络在偏振光下显示正双折射。在稳定微管(MT)的溶液中对网状伪足网络进行裂解和提取后,这些纤维仍保持完整。对这些裂解并稳定的细胞骨架模型进行超薄切片的电子显微镜照片显示有微管束。只有在适应无钙海水(其中流动正常)后,标准的电子显微镜固定剂才能保存活的乳突异网足虫的网状伪足网络。网状伪足网络中的微管通常排列成束,这些束通常与主干和分支丝状伪足的长轴平行。对整装、固定并经过临界点干燥的生物体进行的立体电子显微镜照片显示,微管分布的复杂模式反映了网状伪足网络扁平部分和高度分支部分中颗粒的运动模式。一些带有模糊包膜的细胞质颗粒与单个微管或微管束紧密相关,并优先沿其排列。在网络内还观察到细丝(约5纳米),它们与微管平行并相互交错,位于丝状伪足的扁平末端区域。在对照(人血小板)中能大量修饰肌动蛋白丝的条件下,这些细丝不与骨骼肌肌球蛋白S1结合,并且其粗细约比超微结构鉴定为F -肌动蛋白的细丝细20%。

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