cDNA for R-cognin: homology with a multifunctional protein.
cDNA for R-cognin: homology with a multifunctional protein.
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R-cognin 的 cDNA：与多功能蛋白的同源性。
DOI：
10.1073/pnas.90.7.2950
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发表时间：
1993
影响因子：
11.1
通讯作者：
Hausman,RE
中科院分区：
文献类型：
--
作者：
KrishnaRao,AS;Hausman,RE
视网膜认知蛋白 (R-cognin) 是一种发育调节蛋白，从鸡胚视网膜细胞膜中分离出来。它在体外介导来自鸡和小鼠胚胎的视网膜细胞的粘附和重新聚集，但不介导来自其他组织的细胞，并且可能参与神经元分化。我们在这里报告了 R-cognin cDNA 的克隆。在 lambda gt11 载体中构建鸡胚视网膜 cDNA 文库，并用多克隆 R-cognin 抗血清进行筛选，产生几个免疫反应性克隆。针对由一种重组溶原菌产生的R-cognin-β-半乳糖苷酶融合蛋白制备的抗血清识别源自视网膜细胞膜的50-kDa R-cognin蛋白。这种抗血清抑制分离的视网膜细胞和免疫染色的鸡胚视网膜组织的重新聚集，其模式与用 R-cognin 抗血清获得的模式相似。来自 cDNA 亚克隆的 RNA 的体外翻译产生了 50 kDa 的蛋白质，该蛋白质在蛋白质印迹上被 R-cognin 抗血清识别。根据这些标准，我们将 cDNA 克隆鉴定为编码 R-cognin 的基因的代表。该 cDNA 与多功能蛋白 cDNA 的主要部分几乎相同，该多功能蛋白是脯氨酰 4-羟化酶的 β 亚基，并且具有蛋白二硫键异构酶活性和甲状腺激素结合活性。这些发现表明 R-cognin 与其他细胞粘附分子不同，并表明其在细胞粘附和神经元分化中的作用可能机制。
Retina cognin (R-cognin) is a developmentally regulated 50-kDa protein that was isolated from chicken embryo retina cell membranes. It mediates the adhesion and reaggregation in vitro of retina cells from chicken and mouse embryos, but not of cells from other tissues, and may be involved in neuronal differentiation. We report here the cloning of a cDNA for R-cognin. A chicken embryo retina cDNA library was constructed in lambda gt11 vector and was screened with polyclonal R-cognin antiserum, yielding several immunoreactive clones. Antiserum prepared to the R-cognin-beta-galactosidase fusion protein produced by one recombinant lysogen recognized the 50-kDa R-cognin protein derived from retina cell membranes. This antiserum inhibited the reaggregation of dissociated retina cells and immunostained chicken embryo retina tissue in a pattern similar to that obtained with R-cognin antiserum. In vitro translation of RNA from a cDNA subclone yielded a 50-kDa protein that was recognized by R-cognin antiserum on a Western blot. By these criteria we identify the cDNA clone as representative of the gene encoding R-cognin. This cDNA is nearly identical to a major portion of the cDNA for the multifunctional protein that is the beta subunit of prolyl 4-hydroxylase and has both protein disulfide isomerase activity and thyroid hormone-binding activity. These findings demonstrate that R-cognin differs from other cell adhesion molecules and suggest possible mechanisms for its action in cell adhesion and neuronal differentiation.