CADHERIN CELL-ADHESION MOLECULES WITH DISTINCT BINDING SPECIFICITIES SHARE A COMMON STRUCTURE
CADHERIN CELL-ADHESION MOLECULES WITH DISTINCT BINDING SPECIFICITIES SHARE A COMMON STRUCTURE
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DOI：
10.1002/j.1460-2075.1986.tb04525.x
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发表时间：
1986-10-01
期刊：
影响因子：
11.4
通讯作者：
TAKEICHI, M
中科院分区：
文献类型：
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作者：
SHIRAYOSHI, Y;HATTA, K;TAKEICHI, M
钙离子依赖细胞-细胞粘附分子，称为钙粘蛋白，分为亚类具有不同的组织分布和不同的细胞结合特异性。为了阐明这些亚类的生化关系，我们比较了小鼠肝E-cadherin与鸡脑N-cadherin的胰蛋白酶裂解模式和部分氨基酸序列。虽然这两种钙粘蛋白的细胞结合和免疫特异性不同，但它们具有相同的分子量和相似的色氨酸切割模式。我们分离了E-和n -钙粘蛋白的色氨酸片段，并确定了它们的氨基末端的9个氨基酸残基的序列。结果表明，这两种钙粘蛋白从氨基端到第7个残基的氨基酸序列完全相同。因此，我们认为具有不同特异性的钙粘蛋白具有共同的基因起源。
Ca2+-dependent cell-cell adhesion molecules, termed cadherins, are divided into subclasses with distinct tissue distributions and distinct cell-binding specificities. To elucidate the biochemical relationship of these subclasses, we compared the pattern of tryptic cleavage and the partial amino acid sequence of mouse liver E-cadherin with those of chicken brain N-cadherin. Although these two cadherins are distinct in their cell-binding and immunological specificities, they showed an identical mol. wt and a similar tryptic cleavage pattern. We isolated tryptic fragments of E- and N-cadherin, and determined the sequences of nine amino acid residues of their amino terminus. The results showed that sequences of amino acids from the amino terminus to the 7th residues are identical in these two cadherins. We thus suggest that cadherins with distinct specificities have a common genic origin.