Kaltner Herbert, Solís Dolores, Kopitz Jürgen, Lensch Martin, Lohr Michaela, Manning Joachim C, Mürnseer Michael, Schnölzer Martina, André Sabine, Sáiz José Luis, Gabius Hans-Joachim
Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität München, Veterinärstr. 13, D-80539 München, Germany.
Biochem J. 2008 Jan 15;409(2):591-9. doi: 10.1042/BJ20070419.
Prototype galectins are versatile modulators of cell adhesion and growth via their reactivity to certain carbohydrate and protein ligands. These functions and the galectins' marked developmental regulation explain their attractiveness as models to dissect divergent evolution after gene duplication. Only two members have so far been assumed to constitute this group in chicken, namely the embryonic muscle/liver form {C-16 or CLL-I [16 kDa; chicken lactose lectin, later named CG-16 (chicken galectin-16)]} and the embryonic skin/intestine form (CLL-II or C-14; later named CG-14). In the present study, we report on the cloning and expression of a third prototype CG. It has deceptively similar electrophoretic mobility compared with recombinant C-14, the protein first isolated from embryonic skin, and turned out to be identical with the intestinal protein. Hydrodynamic properties unusual for a homodimeric galectin and characteristic traits in the proximal promoter region set it apart from the two already known CGs. Their structural vicinity to galectin-1 prompts their classification as CG-1A (CG-16)/CG-1B (CG-14), whereas sequence similarity to mammalian galectin-2 gives reason to refer to the intestinal protein as CG-2. The expression profiling by immunohistochemistry with specific antibodies discerned non-overlapping expression patterns for the three CGs in several organs of adult animals. Overall, the results reveal a network of three prototype galectins in chicken.
原型半乳糖凝集素是细胞黏附和生长的多功能调节剂,通过它们与某些碳水化合物和蛋白质配体的反应发挥作用。这些功能以及半乳糖凝集素显著的发育调控特性,解释了它们作为基因复制后剖析趋异进化模型的吸引力。迄今为止,在鸡中仅假定有两个成员构成这一组,即胚胎肌肉/肝脏形式(C-16或CLL-I [16 kDa;鸡乳糖凝集素,后来命名为CG-16(鸡半乳糖凝集素-16)])和胚胎皮肤/肠道形式(CLL-II或C-14;后来命名为CG-14)。在本研究中,我们报道了第三个原型CG的克隆和表达。与首次从胚胎皮肤中分离出的重组C-14相比,它具有看似相似的电泳迁移率,结果证明它与肠道蛋白相同。作为一种同二聚体半乳糖凝集素,其不同寻常的流体动力学特性以及近端启动子区域的特征性特征使其与另外两种已知的CG区分开来。它们在结构上与半乳糖凝集素-1相近,促使将它们分类为CG-1A(CG-16)/CG-1B(CG-14),而与哺乳动物半乳糖凝集素-2的序列相似性使得将肠道蛋白称为CG-2。用特异性抗体进行免疫组织化学分析的表达谱显示,成年动物的几个器官中这三种CG的表达模式不重叠。总体而言,结果揭示了鸡体内三种原型半乳糖凝集素的网络。