The mechanism of binding of neural cell adhesion molecules.
The mechanism of binding of neural cell adhesion molecules.
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神经细胞粘附分子的结合机制。
DOI：
10.1007/978-1-4684-4868-9_12
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发表时间：
1984
影响因子：
--
通讯作者：
Edelman,GM
中科院分区：
文献类型：
--
作者：
Hoffman,S;Edelman,GM
高等生物神经系统的形态和细胞间的相互联系是在整个发育过程中发生的复杂的细胞-细胞相互作用的结果。为了确定调节这些相互作用的粘附的细胞表面分子，已经使用了多种检测方法，并提出了几种分子参与神经细胞粘附（Merrell等人，1975；Hausman和Moscona, 1976； Urushihara等人，1979；Marchase等人，1981；Magnani等人，1981；Grunwald等人，1982；Roth和Pierce, 1982； Sadoul等人，1983；Lindner等人，1983）。在我们的实验室里，我们中的一个人（GME）设计了一种免疫学方法，鉴定（Brackenbury等人，1977；Thiery~ t等人，1977）并纯化了一种与钙无关的神经细胞粘附有关的蛋白质，该蛋白质被命名为神经细胞粘附分子或N-CAM。许多其他不同结构和特异性的CAMs已经被确定（见Edelman， 1983，关于回顾）。N-CAM是从鸡胚脑中分离出来的一种高分子量、富含唾液酸的细胞表面糖蛋白（Hoffman et al., 1982）。在酶解唾液酸后，两条表观分子量为140,000和170,000的多肽链可以被分解（Cunningham et al., 1983）。去除所有的n链碳水化合物，它们的分子量减少到130,000和160,000。在N-CAM分子的线性模型中，唾液酸的大部分似乎定位于一个中间结构域，介于结合结构域和参与将蛋白质锚定到细胞表面的结构域之间（Cunningham et al., 1983）。N-CAM中的唾液酸主要以聚唾液酸的形式出现（Hoffman等）。, 1982;Finne et a1。, 1983)。N-CAM中的两条~多肽链
The morphology and cellular interconnections within the nervous system of higher organisms arise as a result of complex cell-cell interactions occurring throughout development. In order to identify the cell surface molecules mediating the adhesion that regulates many of these interactions, a variety of assays have been used and several molecules have been proposed to be involved in neural cell adhesion (Merrell et al., 1975; Hausman and Moscona, 1976; Urushihara et al., 1979; Marchase et al., 1981; Magnani et al., 1981; Grunwald et al., 1982; Roth and Pierce, 1982; Sadoul et al., 1983; Lindner et al., 1983). In our laboratory, an immunological approach devised by one of us (GME) led to the identification (Brackenbury et al., 1977; Thiery~ t al., 1977) and purification of a protein involved in calcium-independent neural cell adhesion which has been named the neural cell adhesion molecule or N-CAM. A number of other CAMs of different structure and specificity have since been identified (See Edelman, 1983, for a· review).N-CAM, isolated from embryonic chick brains, is a high molecular weight, sialic acid-rich, cell surface glycoprotein (Hoffman et al., 1982). Following the enzymatic removal of the sialic acid, two polypeptide chains of apparent molecular weight 140,000 and 170,000 can be resolved (Cunningham et al., 1983). Removal of all N-linked carbohydrate reduces these molecular weights to 130,000 and 160,000. In a linear model of the N-CAM molecule, the bulk of the sialic acid appears to be localized in a middle domain, between the binding domain and the domain involved in anchoring the protein to the cell surface (Cunningham et al., 1983). The sialic acid in N-CAM appears primarily in the form of po1ysia1ic acid (Hoffman et a1., 1982; Finne et a1., 1983). The two~ olypeptide chains in N-CAM