Granger B L, Lazarides E
Mol Cell Biol. 1984 Oct;4(10):1943-50. doi: 10.1128/mcb.4.10.1943-1950.1984.
Synemin, a 230-kilodalton polypeptide component of avian muscle and erythrocyte intermediate filaments, is also found in association with the vimentin filaments of lens tissue. In chicken lens cells, synemin is bound to the core vimentin polymer with the same 180-nm periodicity that it exhibits in erythrocytes. Its solubility properties are characteristic of those of intermediate filaments in general and similar to those of synemin in muscle cells and erythrocytes. Synemin appears at an early stage of lens development and undergoes a dramatic accumulation as the epithelial cells elongate and differentiate into fiber cells. In contrast to synemin in cultured skeletal muscle, lens synemin is not confined to postmitotic, terminally differentiating cells but is present in proliferative cells as well. It is lost from the fibers near the center of the lens, as are many other cellular structures including intermediate filaments. These findings provide new information about the occurrence and expression of avian synemin and new insight regarding its presumptive role as a modulator of intermediate-filament function.
联丝蛋白是鸟类肌肉和红细胞中间丝的一种230千道尔顿的多肽成分,在晶状体组织的波形蛋白丝中也有发现。在鸡晶状体细胞中,联丝蛋白以与它在红细胞中呈现的相同的180纳米周期与波形蛋白核心聚合物结合。它的溶解性特性总体上是中间丝的典型特性,与肌肉细胞和红细胞中联丝蛋白的特性相似。联丝蛋白出现在晶状体发育的早期阶段,随着上皮细胞伸长并分化为纤维细胞,它会大量积累。与培养的骨骼肌中的联丝蛋白不同,晶状体联丝蛋白并不局限于有丝分裂后终末分化的细胞,增殖细胞中也有。它与包括中间丝在内的许多其他细胞结构一样,在晶状体中心附近的纤维中消失。这些发现提供了关于鸟类联丝蛋白的存在和表达的新信息,以及关于其作为中间丝功能调节剂的推测作用的新见解。