...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Endocrinology >An occludin-focal adhesion kinase protein complex at the blood-testis barrier: a study using the cadmium model.
【24h】

An occludin-focal adhesion kinase protein complex at the blood-testis barrier: a study using the cadmium model.

机译：血睾丸屏障中的一种闭合素-黏着斑激酶蛋白复合物：使用镉模型的研究。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Several integral membrane proteins that constitute the blood-testis barrier (BTB) in mammalian testes, in particular rodents, are known to date. These include tight junction (TJ) proteins (e.g. occludin, junctional adhesion molecule-A, claudins), basal ectoplasmic specialization proteins (e.g. N-cadherin), and gap junction proteins (e.g. connexin43). However, the regulators (e.g. protein kinases and phosphatases) that affect these proteins, such as their interaction with the cytoskeletal actin, which in turn confer cell adhesion at the TJ, remain largely unknown. We report herein that focal adhesion kinase (FAK) is a putative interacting partner of occludin, but not claudin-11 or junctional adhesion molecule-A. Immunohistochemistry and fluorescence microscopy studies illustrated that the expression of FAK in the seminiferous epithelium of adult rat testes was stage specific. FAK colocalized with occludin at the BTB in virtually all stages of the seminiferous epithelial cycle but considerably diminished in stages VIII-IX, at the time of BTB restructuring to facilitate the transit of primary leptotene spermatocytes. Using Sertoli cells cultured in vitro with established TJ-permeability barrier and ultrastructures of TJ, basal ectoplasmic specialization and desmosome-like junction that mimicked the BTB in vivo, FAK was shown to colocalize with occludin and zonula occludens-1 (ZO-1) at the Sertoli-Sertoli cell interface. When these Sertoli cell cultures were treated with CdCl(2) to perturb the TJ-barrier function, occludin underwent endocytic-mediated internalization in parallel with FAK and ZO-1. Thus, these findings demonstrate that FAK is an integrated regulatory component of the occludin-ZO-1 protein complex, suggesting that functional studies can be performed to study the role of FAK in BTB dynamics.
机译：迄今为止，已知几种构成哺乳动物睾丸中的血液-睾丸屏障（BTB）的完整膜蛋白，特别是啮齿动物。这些包括紧密连接（TJ）蛋白（例如occludin，连接粘附分子-A，claudins），基础胞浆特化蛋白（例如N-钙黏着蛋白）和间隙连接蛋白（例如connexin43）。但是，影响这些蛋白质的调节剂（例如蛋白激酶和磷酸酶），例如它们与细胞骨架肌动蛋白的相互作用，进而赋予细胞在TJ的粘附力，仍然是未知的。我们在这里报道，粘着斑激酶（FAK）是occludin的假定的相互作用伴侣，但不是claudin-11或连接粘附分子-A。免疫组织化学和荧光显微镜研究表明，成年大鼠睾丸生精上皮中FAK的表达具有阶段特异性。 FAK在几乎整个生精上皮周期的所有阶段都与闭塞素在BTB共定位，但在BTB重组以促进初级瘦素精子细胞通过时，在VIII-IX阶段则大大减少。使用体外培养的具有建立的TJ渗透性屏障和TJ超微结构，基础胞浆特化和在体内模拟BTB的桥粒样连接的Sertoli细胞，FAK被证明与occludin和zonula occludens-1（ZO-1）共定位Sertoli-Sertoli细胞界面。当这些Sertoli细胞培养物用CdCl（2）处理以扰动TJ屏障功能时，occludin经历了内吞介导的内在化，与FAK和ZO-1平行。因此，这些发现表明FAK是occludin-ZO-1蛋白复合物的整合调节成分，表明可以进行功能研究来研究FAK在BTB动力学中的作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号