Molecular properties and chromosomal location of cadherin-8
Molecular properties and chromosomal location of cadherin-8
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DOI：
10.1006/geno.1997.5152
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发表时间：
1998-03-01
期刊：
影响因子：
4.4
通讯作者：
Suzuki, ST
中科院分区：
文献类型：
--
作者：
Kido, M;Obata, S;Suzuki, ST
大鼠钙粘蛋白-8 cDNA 的克隆证明了两种类型的 cDNA。由一种类型的 cDNA 定义的蛋白质的总体结构与经典钙粘蛋白的结构基本相同，而由另一种类型的 cDNA 定义的蛋白质的末端靠近胞外结构域第五个重复序列 (EC5) 的 N 末端，并在 C 末端包含一个短的独特序列。还从人类 cDNA 文库中获得了相同的截短型 cDNA。在大鼠脑mRNA的Northern印迹分析中，EC5探针检测到约3.5-4.3knt的多个条带，而替代形式的探针与约3.5knt的条带杂交。 Western blot 实验表明，针对大鼠 cadherin-8 胞外结构域的抗体在大鼠脑提取物中染色出约 95 kDa 的条带和约 130 kDa 的微弱条带。这些结果表明，cadherin-8在脑中以两种形式表达，完整形式和不具有跨膜结构域或细胞质结构域的截短形式。 L细胞中表达的完整形式的cadherin-8的分子量约为130 kDa，位于细胞外围，主要位于细胞与细胞的接触部位。然而，我们未能在 L 细胞中表达截短的形式。完整形式的转染子表现出弱的细胞粘附活性。完整形式的 cadherin-8 对胰蛋白酶消化敏感，与经典的钙粘蛋白相比，Ca2+ 不能保护 cadherin-8 免受消化。完整的形式。 cadherin-8 与 β-连环蛋白共沉淀，但与 α-连环蛋白或 γ-连环蛋白不能很好地免疫沉淀，Cadherin-8 以及 cadherin-II 被定位到 8 号染色体的特定区域，该区域还包括 cadherins-1、3 和 -5。 (C) 1998 年学术出版社。
Cloning of rat cadherin-8 cDNA demonstrated tow, types of cDNAs. The overall structure of in protein defined by one type of the cDNA is essentially the same as that of classic cadherins, whereas the protein defined by the other type of cDNA ends near the N-terminus of the fifth repeat of the extracellular domain (EC5) and contains a short unique sequence at the C-terminus. The same truncated type of cDNA was also obtained from a human cDNA library. In Northern blot analysis of rat brain mRNA, a probe for EC5 detected multiple bands of about 3.5-4.3 knt, whereas a probe for the alternative form hybridized with a band of about 3.5 knt. Western blot experiments showed that an antibody against the extracellular domain of rat cadherin-8 stained a band of about 95 kDa and a faint band of about 130 kDa in rat brain extract. These results suggest that cadherin-8 is expressed in two forms, a complete form and a truncated form without a transmembrane domain or cytoplasmic domain, in brain. The complete form of cadherin-8 expressed in L cells was about 130 kDa in molecular-mass and was located at the cell periphery, mainly at the cell-cell contact sites. However, we failed to express the truncated form in L cells. The transfectants of the complete form showed weak cell adhesion activity. The complete form of cadherin-8 was sensitive to trypsin digestion, and Ca2+ did not protect cadherin-8 from digestion, in contrast to the classic cadherins. The complete form. of cadherin-8 coprecipitated with beta-catenin, but did not immunoprecipitate well with alpha-catenin or gamma-catenin, Cadherin-8, as well as cadherin-ll, was mapped to a specific region of chromosome 8 that also includes cadherins-1, 3, and -5. (C) 1998 Academic Press.