Edds K T
J Cell Biol. 1979 Oct;83(1):109-15. doi: 10.1083/jcb.83.1.109.
Isolated petaloid coelomocytes from the sea urchin Strongylocentrotus droebachiensis transform to a filopodial morphology in hypotonic media. Electron micrographs of negatively stained Triton-insoluble cytoskeletons show that the petaloid form consists of a loose net of microfilaments while the filopodial form consists of paracrystalline bundles of microfilaments. Actin is the major protein of both forms of the cytoskeleton. Additional polypeptides have molecular weights of approximately 220,000, 64,000, 57,000, and 27,000 daltons. Relative to actin the filopodial cytoskeletons have an average of 2.5 times as much 57k polypeptide as the petaloid cytoskeletons. Treatment with 0.25 M NaCl dissociates the filament bundles into individual actin filaments free of the actin-associated polypeptides. Thus, one or more of these actin-associated polypeptides may be responsible for crosslinking the actin filaments into bundles and maintaining the three-dimensional nature of the cytoskeletons.
从海胆强壮刺海胆（Strongylocentrotus droebachiensis）中分离出的花瓣状体腔细胞在低渗介质中会转变为丝状伪足形态。经负染的不溶于 Triton 的细胞骨架的电子显微镜照片显示，花瓣状形态由微丝的松散网络组成，而丝状伪足形态由微丝的平行晶体束组成。肌动蛋白是两种细胞骨架形式的主要蛋白质。其他多肽的分子量约为 220,000、64,000、57,000 和 27,000 道尔顿。相对于肌动蛋白，丝状伪足细胞骨架中的 57k 多肽平均是花瓣状细胞骨架的 2.5 倍。用 0.25 M NaCl 处理会使丝束解离成不含肌动蛋白相关多肽的单个肌动蛋白丝。因此，这些肌动蛋白相关多肽中的一种或多种可能负责将肌动蛋白丝交联成束并维持细胞骨架的三维结构。
