Moos M, Tacke R, Scherer H, Teplow D, Früh K, Schachner M
Department of Neurobiology, University of Heidelberg, FRG.
Nature. 1988 Aug 25;334(6184):701-3. doi: 10.1038/334701a0.
Diverse glycoproteins of cell surfaces and extracellular matrices operationally termed 'adhesion molecules' are important in the specification of cell interactions during development, maintenance and regeneration of the nervous system. These adhesion molecules have distinct functions involving different cells at different developmental stages, but may cooperate when expressed together. Families of adhesion molecules which share common carbohydrate domains do exist, despite the structural and functional diversity of these glycoproteins. These include the Ca2+-independent neural adhesion molecules: N-CAM, myelin associated glycoprotein (MAG) and L1. L1 is involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, cerebellar granule cell migration, neurite outgrowth on Schwann cells and interactions among epithelial cells of intestinal crypts. We show here that in addition to sharing carbohydrate epitopes with N-CAM and MAG, L1 is also a member of the immunoglobulin superfamily. It contains six C2 domains and also shares three type III domains with the extracellular matrix adhesion molecule fibronectin.
细胞表面和细胞外基质中各种糖蛋白在神经系统发育、维持和再生过程中细胞相互作用的特化中起着重要作用，这些糖蛋白在操作上被称为“粘附分子”。这些粘附分子具有不同的功能，在不同发育阶段涉及不同细胞，但共同表达时可能会协同作用。尽管这些糖蛋白在结构和功能上具有多样性，但确实存在具有共同碳水化合物结构域的粘附分子家族。其中包括不依赖钙离子的神经粘附分子：神经细胞粘附分子（N-CAM）、髓鞘相关糖蛋白（MAG）和L1。L1参与神经元-神经元粘附、神经突成束、神经突生长、小脑颗粒细胞迁移、雪旺细胞上神经突的生长以及肠隐窝上皮细胞之间的相互作用。我们在此表明，L1除了与N-CAM和MAG共享碳水化合物表位外，还是免疫球蛋白超家族的成员。它含有六个C2结构域，还与细胞外基质粘附分子纤连蛋白共享三个III型结构域。
