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首页> 外文期刊>Journal of bone and mineral research: the official journal of the American Society for Bone and Mineral Research >Expression and function of the splice variant of the human cadherin-11 gene in subordination to intact cadherin-11.
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Expression and function of the splice variant of the human cadherin-11 gene in subordination to intact cadherin-11.

机译：从属于完整的钙黏着蛋白11的人钙黏着蛋白11基因的剪接变体的表达和功能。

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摘要

Cadherin-11, a member of the type II classic cadherin subfamily, differs from type I family molecules such as P-, E-, and N-cadherins. An isoform of the human cadherin-11 gene, termed the variant form, encodes a truncated protein with a different cytoplasmic domain. The resulting protein does not possess any part of the cytoplasmic domain common to other cadherins. In the present study, analysis of the genomic organization of the cadherin-11 gene revealed that an insertion of 179 bp in an intron generates an alternatively spliced form. The mRNA expression of the variant form of cadherin-11 was examined in normal tissues by reverse transcription-polymerase chain reaction and/or Northern blot analyses. The variant form was expressed in the heart, brain, placenta, lung, and bone, but not in the kidney, skeletal muscle, pancreas, and liver. Western blot analyses revealed that the variant form is expressed as an 85 kDa protein, and that an additional secreted form also exists as an 80 kDa protein originated from cleavage of the intact form. Gene transfer of the variant form into L cells demonstrated that it lacked the adhesion properties characteristic of the intact form of cadherin-11 but enhanced the activity of Ca2+-dependent adhesion of the intact form of cadherin-11. The variant was expressed on the surface together with the intact form and stabilized the interaction between the intact form and beta-catenin. These findings suggest that expression of the variant form of human cadherin-11 may regulate the intact cadherin-11-mediated adhesion and alter the morphogenetic processes during mesenchymal cell differentiation including osteoblasts.
机译：Cadherin-11是II型经典钙粘蛋白亚家族的成员，与I型家族分子（例如P-，E-和N-钙粘蛋白）不同。人钙粘蛋白11基因的同工型，称为变异体，编码具有不同胞质结构域的截短蛋白。所得蛋白质不具有其他钙黏着蛋白共有的胞质结构域的任何部分。在本研究中，对钙粘着蛋白11基因的基因组组织的分析表明，内含子中179 bp的插入会产生另一种剪接形式。通过逆转录-聚合酶链反应和/或RNA印迹分析在正常组织中检查了钙粘蛋白11变体形式的mRNA表达。变异形式在心脏，大脑，胎盘，肺和骨骼中表达，但在肾脏，骨骼肌，胰腺和肝脏中不表达。蛋白质印迹分析表明，变体形式表达为85 kDa蛋白质，另外一个分泌形式也作为80 kDa蛋白质存在，其起源于完整形式的切割。变体形式向L细胞的基因转移表明，它缺乏完整形式的钙粘着蛋白11的粘附特性，但增强了完整形式的钙粘着蛋白11的Ca2 +依赖性粘附活性。该变体与完整形式一起在表面上表达，并稳定了完整形式与β-连环蛋白之间的相互作用。这些发现表明，人钙粘着蛋白11的变体形式的表达可能调节完整的钙粘着蛋白11介导的粘附并改变包括成骨细胞在内的间充质细胞分化过程中的形态发生过程。

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