de la Escalera S, Bockamp E O, Moya F, Piovant M, Jiménez F
Centro de Biología Molecular, Universidad Autónoma-CSIC, Madrid, Spain.
EMBO J. 1990 Nov;9(11):3593-601. doi: 10.1002/j.1460-2075.1990.tb07570.x.
Monoclonal antibodies have served to characterize neurotactin, a novel Drosophila protein for which a role in cell adhesion is postulated. Neurotactin is a transmembrane protein, as indicated by epitope mapping and amino acid sequence. Similarly to other cell adhesion molecules, neurotactin accumulates in parts of the membrane where neurotactin-expressing cells contact each other. The protein is only detected during cell proliferation and differentiation, and it is found mainly in neural tissue and also in mesoderm and imaginal discs. Neurotactin has a large cytoplasmic domain rich in charged residues and an extracellular domain similar to cholinesterase that lacks the active site serine required for esterase activity. The extracellular domain also contains three copies of the tripeptide leucine-arginine-glutamate, a motif that forms the primary sequence of the adhesive site of vertebrate s-laminin.
单克隆抗体已用于鉴定神经趋触蛋白，这是一种新的果蝇蛋白，推测其在细胞黏附中起作用。如抗原表位作图和氨基酸序列所示，神经趋触蛋白是一种跨膜蛋白。与其他细胞黏附分子类似，神经趋触蛋白在表达神经趋触蛋白的细胞相互接触的膜区域积累。该蛋白仅在细胞增殖和分化过程中被检测到，主要存在于神经组织中，也存在于中胚层和成虫盘。神经趋触蛋白有一个富含带电荷残基的大细胞质结构域和一个类似于胆碱酯酶的细胞外结构域，该结构域缺乏酯酶活性所需的活性位点丝氨酸。细胞外结构域还包含三个亮氨酸-精氨酸-谷氨酸三肽拷贝，这是构成脊椎动物s-层粘连蛋白黏附位点一级序列的基序。
