USP10 promotes proliferation and migration and inhibits apoptosis of endometrial stromal cells in endometriosis through activating the Raf-1/MEK/ERK pathway

Chen Q, Qiong Chen, Hang Y, Yuanyuan Hang, Tingting Zhang, Li Tan, Tan L, Shuangdi Li, Jin Y, Yuli Jin
American journal of physiology. Cell physiology · 2018 · vol. 315(6) , pp. C863–C872 · doi:10.1152/ajpcell.00272.2018 · PMID:30281322 · W2894856132
Lab / animal OA: bronze CC0 ⤵ 63 in-corpus citations
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USP10 promotes endometrial stromal cell proliferation and migration while inhibiting apoptosis in endometriosis by deubiquitinating and activating Raf-1, thus activating the Raf-1/MEK/ERK pathway.

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Abstract

Endometriosis has been initially described as endometrial-like tissue outside of the uterine cavity. The mitogen-activated protein kinase/ERK kinase (MEK)/extracellular signal-regulated kinase (ERK) signaling pathway playing an important role in the regulation of cell proliferation, apoptosis, and migration has been found to be activated in endometriosis. However, regulation of the MEK/ERK signaling pathway in endometriosis has not been fully understood. In this study, primary-cultured endometrial stromal cells were collected from patients with endometriosis and healthy controls, and the proliferation, apoptosis, and migration of ectopic endometrial stromal cells transfected with ubiquitin-specific protease 10 (USP10)-small-interfering RNA (siRNA) or pLVX-Puro-USP10 with or without MEK inhibitor PD-98059 or exogenous signaling stimulation such as epidermal growth factor (EGF) were measured by CCK-8, flow cytometry, and Transwell, respectively. The gene and protein expressions were measured by real-time PCR or Western blot. USP10 overexpression promoted ectopic endometrial stromal cell migration and proliferation, suppressed cell apoptosis, and activated MEK/ERK signaling that is a critical downstream target of the serine/threonine protein kinase Raf-1, which was significantly blocked by PD-98059. USP10 silencing demonstrated the inverse effects, and these effects induced by USP10 silencing were significantly blocked by EGF. USP10 overexpression promoted Raf-1 protein expression, but not mRNA expression, through deubiquitination. In conclusion, these results suggest that USP10 promotes proliferation and migration and inhibits apoptosis of endometrial stromal cells in endometriosis through activating the Raf-1/MEK/ERK pathway.

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Condition tags

endometriosis

MeSH descriptors

Endometriosis Endometrium Proto-Oncogene Proteins c-raf Ubiquitin Thiolesterase Apoptosis Apoptosis Apoptosis Cell Movement Cell Movement Cell Movement Cell Proliferation Cell Proliferation Cell Proliferation Endometriosis Endometriosis Endometriosis Endometrium Endometrium Endometrium Epithelial Cells

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Papers in the corpus that this work cites (lower rings, blue) and that cite this one (upper rings, green). Dot size scales with the paper's in-corpus citation count — bigger dot = more influential within the endo/adeno field. Click a dot to open that paper. Outer rings show 2-hop neighbours — papers reached through the immediate citers/citees. [ collapse to 1-hop ]

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