The function of the nuclear cathepsin L and the analysis of nucleocytoplasmic transport mechanism in pregnant uterine decidua

在蜕膜化过程中，孕酮诱导核孔复合体蛋白的表达，引起核孔结构的改变，并将受孕酮调控的组织蛋白酶L和CTLA-2 α输入细胞核。组织蛋白酶L在细胞核内与CTLA-2 α结合，作为蛋白酶，通过产生短的转录因子CDP/Cux，促进细胞周期蛋白的表达，从而加速细胞分裂，同时Arpc 2的核转运也可能引起核结构的改变。arpc 2参与肌动蛋白聚合，从而导致染色质重塑和蜕膜化诱导因子的转录。

During the process of decidualization, progesterone induces the expression of a number of nuclear pore complex proteins, which in turn cause structural changes in the nuclear pores.Cathepsin L and CTLA-2 alpha, proteins which are similarly regulated by progesterone, are then imported into the nucleus. Cathepsin L binds to CTLA-2alpha in the nucleus and acts as a protease, promoting the expression of cell-cycle proteins by generating short isoforms of the transcription factor CDP/Cux, resulting in accelerated cell division.Simultaneously, the nuclear transport of Arpc2 may also give rise to changes in the nuclear structure. Arpc2 participates in actin polymerization, which leads to chromatin remodeling and the transcription of decidualization-inducing factors.