Cole G J, Schachner M, Fliesler S J
Department of Anatomy and Cell Biology, Medical University of South Carolina, Charleston 29425.
Neurosci Lett. 1988 Nov 11;93(2-3):170-5. doi: 10.1016/0304-3940(88)90076-6.
Recent studies have described the role of various regions of the neural cell adhesion molecule (NCAM) in cell-cell interactions. Monoclonal antibodies (L2/HNK-1) directed against a sulfated, glucuronic acid-containing, N-linked carbohydrate epitope have also been shown to inhibit NCAM-mediated neural cell adhesion. In the present study we show that dissociated retinal neurons in an in vitro model system can bind as well to normal NCAM as to NCAM lacking the L2/HNK-1 epitope or to glycopeptidase F-treated NCAM. These data suggest that N-linked oligosaccharide chains do not confer upon NCAM the adhesional properties associated with its role in neuron-neuron interactions.
最近的研究描述了神经细胞黏附分子(NCAM)各个区域在细胞间相互作用中的作用。针对一种含硫酸化、葡萄糖醛酸的N-连接碳水化合物表位的单克隆抗体(L2/HNK-1)也已被证明可抑制NCAM介导的神经细胞黏附。在本研究中,我们表明,在体外模型系统中分离的视网膜神经元既能与正常NCAM结合,也能与缺乏L2/HNK-1表位的NCAM或经糖肽酶F处理的NCAM结合。这些数据表明,N-连接寡糖链并未赋予NCAM与其在神经元-神经元相互作用中的作用相关的黏附特性。