Huang Y, Jellies J, Johansen K M, Johansen J
Department of Zoology and Genetics, Iowa State University, Ames, Iowa 50011, USA.
J Cell Biol. 1997 Jul 14;138(1):143-57. doi: 10.1083/jcb.138.1.143.
By immunoaffinity purification with the mAb Lan3-2, we have identified two novel Ig superfamily members, Tractin and LeechCAM. LeechCAM is an NCAM/FasII/ApCAM homologue, whereas Tractin is a cleaved protein with several unique features that include a PG/YG repeat domain that may be part of or interact with the extracellular matrix. Tractin and LeechCAM are widely expressed neural proteins that are differentially glycosylated in sets and subsets of peripheral sensory neurons that form specific fascicles in the central nervous system. In vivo antibody perturbation of the Lan3-2 glycoepitope demonstrates that it can selectively regulate extension of neurites and filopodia. Thus, these experiments provide evidence that differential glycosylation can confer functional diversity and specificity to widely expressed neural proteins.
通过使用单克隆抗体Lan3-2进行免疫亲和纯化，我们鉴定出了两个新的免疫球蛋白超家族成员，即Tractin和LeechCAM。LeechCAM是一种神经细胞黏附分子（NCAM）/FasII/ApCAM同源物，而Tractin是一种具有多个独特特征的裂解蛋白，其中包括一个可能是细胞外基质的一部分或与细胞外基质相互作用的PG/YG重复结构域。Tractin和LeechCAM是广泛表达的神经蛋白，它们在中枢神经系统中形成特定束状结构的外周感觉神经元的集合和子集中进行差异糖基化。体内对Lan3-2糖表位的抗体干扰表明，它可以选择性地调节神经突和丝状伪足的延伸。因此，这些实验提供了证据，证明差异糖基化可以赋予广泛表达的神经蛋白功能多样性和特异性。
