Cross-linking activity of the 14-kilodalton beta-galactoside-specific vertebrate lectin with asialofetuin: comparison with several galactose-specific plant lectins.
Cross-linking activity of the 14-kilodalton beta-galactoside-specific vertebrate lectin with asialofetuin: comparison with several galactose-specific plant lectins.
复制标题
14 千道尔顿 β-半乳糖苷特异性脊椎动物凝集素与去唾液酸胎球蛋白的交联活性：与几种半乳糖特异性植物凝集素的比较。
DOI：
10.1021/bi00151a012
复制
发表时间：
1992
期刊：
影响因子：
2.9
通讯作者：
Brewer,CF
中科院分区：
文献类型：
--
作者：
Mandal,DK;Brewer,CF
修订稿于 1992 年 6 月 16 日收到 摘要：我们之前已经证明，具有广泛碳水化合物结合特异性的植物凝集素可以结合并交联（沉淀）特定的多触角寡糖和糖肽 [cf. Bhattacharyya, L.、Fant, J.、Lonn, H. 和 Brewer, C. F.(1990) 生物化学 29, 7523-7530]。这导致了结合特异性的新来源：即凝集素和碳水化合物之间均匀交联晶格的形成。最近，我们证明了在 D-Man/D-Glc 特异性植物凝集素伴刀豆球蛋白 A 和大豆凝集素之间存在高度有序的交联晶格，大豆凝集素是一种四聚体糖蛋白，每个单体拥有一条 Man9 寡甘露糖链 [Khan, M. I., Mandal, DK, & Brewer, C. F.(1991) Carbohid.资源。 213、69-77]。在本研究中，我们比较了来自小牛脾的 14-kDa/3-半乳糖苷特异性凝集素（一种二聚体 S 型动物凝集素）和来自刺桐、红刺桐和大豆（大豆凝集素）的几种半乳糖特异性植物凝集素与脱唾液酸胎蛋白 (ASF) 形成特异性交联复合物的能力， 48 kDa 单体糖蛋白，使用定量沉淀分析。结果显示，ASF 与 14-kDa 凝集素形成 1:9 和 1:3 化学计量交联复合物（每个单体），具体取决于它们在溶液中的相对比例。有证据表明，ASF 的三个三触角 N-连接复合型寡糖链介导交联相互作用，并且每条链在 1:9 交联复合物中表达三价，在 1:3 复合物中表达单价。两种二聚刺桐凝集素还形成 1:9 和 1:3 ASF-凝集素交联复合物，以及在高相对浓度的 ASF 下形成较低比例的复合物。在四聚体大豆凝集素存在的情况下，仅形成 1:3 ASF-凝集素交联复合物，可能是由于凝集素尺寸较大。与植物凝集素不同，14-kDa 凝集素无法与来自 ASF 的游离三触角糖肽或寡糖或其他相关的支链碳水化合物沉淀，这表明这可能是动物凝集素与植物凝集素的交联活性的重要差异。还深入了解了交联复合物中三触角寡糖的构象特性，以及影响连接到蛋白质基质的寡糖链价态的因素。因此，目前的结果表明，14-kDa 动物凝集素具有与几种 Gal 特异性植物凝集素相似但不同的交联活性，以形成具有明确碳水化合物表位的糖蛋白。讨论了与凝集素及其相应糖复合物受体的生物学特性有关的发现。凝集素是与糖蛋白和糖脂的碳水化合物部分结合的蛋白质，而糖蛋白和糖脂反过来又作为受体参与多种生物识别过程，包括细胞识别、粘附、信号转导和转移（Brandley & Schnaar，1986；Lennarz，1980；Monsigny， 1984）。凝集素广泛分布于自然界，存在于植物、微生物、细菌和动物中（Kobata，1984；Komfeld & Kornfeld，1985；Nicol-son，1976；Snider，1984；Lis & Sharon，1986）。由于植物凝集素含量丰富且易于分离（Goldstein & Poretz，1986），植物凝集素已被广泛用于研究从正常细胞和转化细胞中分离出的多种碳水化合物的结合表位（Lis & Sharon，1986）。
Revised Manuscript Received June 16, 1992 abstract: We have previously shown that plant lectins with a wide range of carbohydrate binding specificities can bind and cross-link (precipitate) specific multiantennary oligosaccharidesand glycopeptides [cf. Bhattacharyya, L., Fant, J., Lonn, H., & Brewer, C. F.(1990) Biochemistry 29, 7523-7530]. This leads to a new source of binding specificity: namely, the formation of homogeneous cross-linked lattices between lectins and carbohydrates. Recently, we have demonstrated the existence of highly ordered cross-linked lattices that form between the D-Man/D-Glc-specific plant lectin concanavalin A and the soybean agglutinin which is a tetrameric glycoprotein possessing a single Man9 oligomannose chain per monomer[Khan, M. I., Mandal, DK, & Brewer, C. F.(1991) Carbohydr. Res. 213, 69-77]. In the present study, we have compared the ability of the 14-kDa/3-galactoside-specific lectinfrom calf spleen, a dimeric S-type animal lectin, and several galactose-specific plant lectins from Erythrina indica, Erythrina cristagalli, and Glycine max (soybean agglutinin) to form specific cross-linked complexes with asialofetuin (ASF), a 48-kDa monomeric glycoprotein, using quantitative precipitation analyses. The results show the formation of 1: 9 and 1: 3 stoichiometric cross-linkedcomplexes (per monomer) of ASF to the 14-kDa lectin, depending on their relative ratio in solution. Evidence indicates that the three triantennary N-linked complex-type oligosaccharide chains of ASF mediate the cross-linking interactions and that each chain expresses either trivalency in the 1: 9 cross-linked complex or univalency in the 1: 3 complex. The two dimeric Erythrina lectins also form 1: 9 and 1: 3 ASF-lectin cross-linked complexes as well as a lower ratio complex at high relative concentrations of ASF. In the presence of tetrameric soybean agglutinin, only a 1: 3 ASF-lectin cross-linked complex is formed, presumably due to the larger size of the agglutinin. Unlike the plant lectins, the 14-kDa lectin fails to precipitate with the free triantennary glycopeptide or oligosaccharide from ASF, or with other related branched-chain carbohydrates, which suggests that this may be an important difference in the cross-linking activities of the animal lectin compared to the plant lectins. Insight has also been obtained into the conformational properties of the triantennary oligosaccharide in cross-linkedcomplexes, and the factorsaffecting thevalency of the oligosaccharide chain attached to a protein matrix. The present results thus demonstrate that the 14-kDa animal lectin possesses similar but distinct cross-linking activities from several Gal-specific plant lectins toward a glycoprotein with well-defined carbohydrate epitopes. The findings are discussed in relation tothe biological properties of lectinsand their corresponding glycoconjugate receptors.Lectins are proteins which bind to the carbohydrate moieties of glycoproteins and glycolipids which, in turn, havebeen implicated as receptors in a variety of biological recognition processes including cellular recognition, adhesion, signal transduction, and metastasis (Brandley & Schnaar, 1986; Lennarz, 1980; Monsigny, 1984). Lectins are widely distributed in nature, and are found in plants, microorganisms, bacteria, and animals (Kobata, 1984; Komfeld & Kornfeld, 1985; Nicol-son, 1976; Snider, 1984; Lis & Sharon, 1986). Because of their abundance and ease of isolation (Goldstein & Poretz, 1986), plant lectins have been widely used toinvestigate the binding epitopes of a variety of carbohydrates isolated from both normal and transformed cells (Lis & Sharon, 1986).
生物科学和医学中的杂交瘤技术
DOI：
--
发表时间：
2012
期刊：
Springer US
影响因子：
--
作者：
T. Springer
通讯作者：
T. Springer