Pumplin D W
Department of Anatomy, University of Maryland School of Medicine, Baltimore 21201.
J Cell Biol. 1989 Aug;109(2):739-53. doi: 10.1083/jcb.109.2.739.
Cultured rat myotubes develop high concentrations of acetylcholine receptors (AChR) in specialized areas of attachment to their substrate. We examined the ultrastructure of identified AChR clusters by quick-freeze, deep-etch, rotary replication or by thin sectioning of whole myotubes fixed in the presence of saponin and tannic acid to preserve the cytoskeleton. Our findings show that AChR clusters are composed of at least three distinct domains, differing in their cytoskeletal, intramembrane, and external components. At contact domains, the myotube's ventral membrane lacked AChR and lay within 10-15 nm of the substrate; electron-dense strands connected the two. The overlying cytoplasm contained bundles of parallel microfilaments passing above and through an irregular network of globular material, resembling the relationship of microfilament bundles to focal contacts already described in fibroblasts. Coated-membrane domains lay between the microfilament bundles and were overlain by cytoplasmic plaques of a regular network of polygons having associated coated pits. These plaques closely resembled the network of polymerized clathrin described in fibroblasts and macrophages. Coated membrane also lacked AChR and adhered to the substrate by electron-dense strands, but did not anchor microfilament bundles. The cytoplasm overlying AChR domains contained a complex network composed of at least two layers. The layer closest to the membrane consisted of protrusions from the cytoplasmic surface, some connected by fine filaments less than 5 nm in diameter. An overlying layer contained larger diameter filaments, some forming an anastomotic network reminiscent of the cortical cytoskeleton of erythrocytes. Longer filaments inserting into this network appeared identical to members of nearby microfilament bundles. The morphology of AChR domains supports the idea that AChR are immobilized by a network containing actin and spectrin.
培养的大鼠肌管在附着于底物的特定区域会形成高浓度的乙酰胆碱受体(AChR)。我们通过快速冷冻、深度蚀刻、旋转复型,或对在皂角苷和单宁酸存在下固定以保存细胞骨架的整个肌管进行超薄切片,来检查已鉴定的AChR簇的超微结构。我们的研究结果表明,AChR簇由至少三个不同的结构域组成,其细胞骨架、膜内和外部成分各不相同。在接触结构域,肌管的腹侧膜缺乏AChR,位于底物上方10 - 15纳米处;电子致密链将两者连接起来。上方的细胞质包含平行微丝束,这些微丝束从一个不规则的球状物质网络上方穿过并贯穿其中,类似于成纤维细胞中已描述的微丝束与粘着斑的关系。被膜结构域位于微丝束之间,上方覆盖着由规则多边形网络组成的细胞质斑块,并伴有被膜小窝。这些斑块与成纤维细胞和巨噬细胞中描述的聚合网格蛋白网络非常相似。被膜也缺乏AChR,并通过电子致密链附着于底物,但不锚定微丝束。覆盖AChR结构域的细胞质包含一个由至少两层组成的复杂网络。最靠近膜的一层由细胞质表面的突起组成,一些突起由直径小于5纳米的细丝连接。上方的一层包含直径较大的细丝,一些细丝形成吻合网络,让人联想到红细胞的皮质细胞骨架。插入该网络的较长细丝似乎与附近微丝束的成员相同。AChR结构域的形态支持了AChR被包含肌动蛋白和血影蛋白的网络固定的观点。