Rougon G, Deagostini-Bazin H, Hirn M, Goridis C
EMBO J. 1982;1(10):1239-44. doi: 10.1002/j.1460-2075.1982.tb00019.x.
We have previously identified a cell surface glycoprotein of the mouse nervous system named brain cell surface protein-2 (BSP-2). Here we report that this antigen is not a single, discrete entity, but a family of antigenically and structurally related molecules. Three components of 180, 140, and 120 K were characteristic for more mature nervous tissues. Adult cerebral cortex contained the 140-K and 120-K antigens, adult spinal cord only the 120-K, and dorsal root ganglia from young mice mainly the 180-K component. Very different forms of the antigen that migrated as a diffuse zone from 180-250-K in SDS-polyacrylamide gels were found in immature nervous tissues. A molecule different from the previous ones was found in a neuroblastoma line. Evidence is presented that the structural diversity of BSP-2 is due to differences in glycosylation. This result indicates that cell type- and developmental stage-specific glycoprotein patterns previously found in the nervous system may in part be due to different glycosylation of identical polypeptides. The finding that a neural cell surface protein may be glycosylated in different ways has important implications for the generation of cell surface specificity.
我们之前鉴定出一种小鼠神经系统的细胞表面糖蛋白，命名为脑细胞表面蛋白-2（BSP-2）。在此我们报告，这种抗原并非单一、离散的实体，而是一个在抗原性和结构上相关的分子家族。180K、140K和120K的三种成分是更成熟神经组织的特征。成年大脑皮层含有140K和120K抗原，成年脊髓仅含120K抗原，幼鼠背根神经节主要含180K成分。在未成熟神经组织中发现了抗原的非常不同的形式，在SDS-聚丙烯酰胺凝胶中迁移为180 - 250K的弥散区。在一个神经母细胞瘤细胞系中发现了一种与之前不同的分子。有证据表明BSP-2的结构多样性是由于糖基化的差异。这一结果表明，先前在神经系统中发现的细胞类型和发育阶段特异性糖蛋白模式可能部分归因于相同多肽的不同糖基化。神经细胞表面蛋白可能以不同方式进行糖基化这一发现对细胞表面特异性的产生具有重要意义。
