Tissue‐ and developmental stage‐specific forms of a neural cell surface antigen linked to differences in glycosylation of a common polypeptide.
Tissue‐ and developmental stage‐specific forms of a neural cell surface antigen linked to differences in glycosylation of a common polypeptide.
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神经细胞表面抗原的组织和发育阶段特异性形式与常见多肽的糖基化差异有关。
DOI：
10.1002/j.1460-2075.1982.tb00019.x
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发表时间：
1982
期刊：
影响因子：
--
通讯作者：
C. Goridis
中科院分区：
文献类型：
--
作者：
G. Rougon;H. Deagostini;M. Hirn;C. Goridis
我们之前已经鉴定了小鼠神经系统的细胞表面糖蛋白，称为脑细胞表面蛋白-2（BSP-2）。在这里，我们报告说，这种抗原不是一个单一的，离散的实体，而是一个家庭的抗原和结构相关的分子。180、140和120 K的三个组分是更成熟的神经组织的特征。成年大脑皮质含有140-K和120-K抗原，成年脊髓仅含有120-K抗原，而年轻小鼠的背根神经节主要含有180-K抗原。在未成熟的神经组织中发现了非常不同形式的抗原，其在SDS-聚丙烯酰胺凝胶中作为180 - 250-K的扩散区迁移。在神经母细胞瘤细胞系中发现了一种与以前不同的分子。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，以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是由于相同多肽的不同糖基化。神经细胞表面蛋白可以以不同方式糖基化的发现对于细胞表面特异性的产生具有重要意义。
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.