The ubiquitin proteasome system (UPS) is essential for many cellular processes, including the cell cycle, the regulation of gene expression and cell survival. Dysfunctional UPS can be associated with the underlying pathophysiology of specific diseases. The 20S proteasome core is composed of 28 subunits, which are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven ? subunits, and the two central rings are each formed by seven ? subunits. The The over expression of LMP2/?1i in trophoblast cells of hydatidiform moles may contribute to its highly invasive phenotype. LMP2/?1i-deficient mice reportedly exhibit uterine neoplasms, with a disease prevalence of 36% by 12 months of age. Embryo implantation involves the invasion of placental extravillous trophoblast cells (EVTs) into the uterus. Normal human placentas or placentas from hydatidiform mole patients were collected and the expression of LMP2/?1i in different cell types including trophoblastic column (TC), cytotrophoblast cells (CTB) and syncytiotrophoblasts (STBs) was examined under different pathological states by pathological analysis. The expression of LMP2/?1i in TC of partial hydatidiform mole and complete hydatidiform mole placentas, was higher than that in TC of normal human placentas. Further the experiments with human and mouse uterine tissues clarified the physiological significance of LMP2/?1i in malignant myometrium transformation. In this mini review, we covered recent insights into the molecular pathways involved in LMP2/?1i-mediated physiological functions, with a particular focus on embryo implantation and uterine mesenchymal tumorigenesis.
LMP2/?1i, implantation, trophoblast, leiomyosarcoma, leiomyoma
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