Karlstrom R O, Wilder L P, Bastiani M J
Department of Biology, University of Utah, Salt Lake City 84112.
Development. 1993 Jun;118(2):509-22. doi: 10.1242/dev.118.2.509.
We describe the developmental expression in grasshopper (Schistocerca americana) and molecular characterization in grasshopper and fruit fly (Drosophila melanogaster) of Lachesin, a novel immunoglobulin superfamily protein. Lachesin is expressed on the surfaces of differentiating neuronal cells from the onset of neurogenesis in both the central and peripheral nervous systems. Lachesin expression begins in some cells of the neurogenic ectoderm immediately after engrailed expression begins in the posterior cells of each future segment. All neurogenic cells express Lachesin early, but only those cells that become neuroblasts continue to express Lachesin. Ectodermal cells in the neurogenic region that adopt non-neuronal fates lose Lachesin at the time that they diverge from a potentially neurogenic pathway. Neuroblasts, ganglion mother cells and neurons all express Lachesin early in their lives, but expression becomes restricted to a subset of neurons as development progresses. Sensory neurons express Lachesin as they delaminate from the body wall ectoderm. Lachesin is also present on growing axons of the CNS and PNS and becomes restricted to a subset of axons later in development. This expression is unique among known insect neurogenic genes and suggests a role for Lachesin in early neuronal differentiation and axon outgrowth. Grasshopper Lachesin is a 38 x 10(3) M(r) protein linked to cell membranes through a glycosyl phosphatidylinositol anchor. We have cloned the Lachesin gene from both grasshopper and fly. The proteins are highly conserved (70% identical) between the two species. Lachesin is similar to Drosophila amalgam, bovine OBCAM and the human poliovirus receptor, putting it into a subgroup of the immunoglobulin superfamily containing one V- and two C2-type immunoglobulin domains. Lachesin is also similar to several other vertebrate immunoglobulin superfamily proteins (TAG-1, F11, L1 and NgCAM) known to function in neurite outgrowth and other cell surface recognition events.
我们描述了一种新型免疫球蛋白超家族蛋白——拉辛蛋白(Lachesin)在美洲沙漠蝗(Schistocerca americana)中的发育表达情况,以及在美洲沙漠蝗和果蝇(Drosophila melanogaster)中的分子特征。从神经发生开始,拉辛蛋白就在中枢神经系统和外周神经系统中分化的神经元细胞表面表达。在每个未来体节的后部细胞中, engrailed 表达开始后不久,神经外胚层的一些细胞就开始表达拉辛蛋白。所有神经源性细胞早期都表达拉辛蛋白,但只有那些成为神经母细胞的细胞会继续表达。神经源性区域中采用非神经元命运的外胚层细胞在偏离潜在神经源性途径时会失去拉辛蛋白表达。神经母细胞、神经节母细胞和神经元在其生命早期都表达拉辛蛋白,但随着发育的进行,表达会局限于一部分神经元。感觉神经元从体壁外胚层脱层时表达拉辛蛋白。拉辛蛋白也存在于中枢神经系统和外周神经系统正在生长的轴突上,在发育后期会局限于一部分轴突。这种表达在已知的昆虫神经源性基因中是独特的,表明拉辛蛋白在早期神经元分化和轴突生长中起作用。美洲沙漠蝗的拉辛蛋白是一种 38×10³ M(r) 的蛋白,通过糖基磷脂酰肌醇锚定与细胞膜相连。我们已经从蝗虫和果蝇中克隆了拉辛蛋白基因。这两种物种的蛋白质高度保守(70% 相同)。拉辛蛋白与果蝇的 amalgam、牛的 OBCAM 和人类的脊髓灰质炎病毒受体相似,属于免疫球蛋白超家族中包含一个 V 型和两个 C2 型免疫球蛋白结构域的亚组。拉辛蛋白也与其他几种已知在神经突生长和其他细胞表面识别事件中起作用的脊椎动物免疫球蛋白超家族蛋白(TAG-1、F11、L1 和 NgCAM)相似。