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Role of ubiquitin‑proteasome system in preeclampsia (Review)
Chang-Zhu Pei1, Xiao-Xing Song1, Hao Xu1
1Department of Gynecology, Lianyungang Maternal and Child Health Hospital, Lianyungang, Jiangsu 222000, P.R. China.
Insights
Preeclampsia involves abnormal protein regulation via ubiquitination and deubiquitination. Targeting these processes offers new therapeutic strategies for this pregnancy disorder.
Area of Science:
- Reproductive biology
- Molecular biology
- Biochemistry
Background:
- Preeclampsia (PE) is a pregnancy disorder marked by hypertension and proteinuria.
- It stems from placental issues and endothelial dysfunction.
- Ubiquitination and deubiquitination are key post-translational modifications.
Purpose of the Study:
- To review the role of ubiquitination and deubiquitination in preeclampsia pathogenesis.
- To explore novel therapeutic strategies targeting the ubiquitin-proteasome system for PE.
Main Methods:
- Literature review focusing on ubiquitination/deubiquitination pathways in PE.
- Analysis of the impact of these modifications on trophoblast function.
- Examination of emerging therapeutic approaches.
Main Results:
- Dysregulation of ubiquitination and deubiquitination pathways impairs trophoblast function.
- These pathways are critical in the development of preeclampsia.
- Targeting the ubiquitin-proteasome system shows therapeutic potential.
Conclusions:
- Ubiquitination and deubiquitination are crucial in preeclampsia.
- Targeting these mechanisms offers promising therapeutic avenues.
- Further research may yield novel interventions for improved maternal and fetal outcomes.
Abstract:
Preeclampsia (PE) is a multifactorial pregnancy disorder characterized by hypertension and proteinuria, primarily resulting from placental abnormalities and endothelial dysfunction. The present review explores the role of ubiquitination and deubiquitination (key post‑translational modifications), in the pathogenesis of PE. Ubiquitination, catalyzed by E1, E2 and E3 enzymes, and reversed by deubiquitinating enzymes, regulates protein stability and function, thereby influencing key cellular processes in trophoblasts. Dysregulation of these pathways impairs trophoblast functions and contributes to PE development. In addition, the present review discusses emerging therapeutic strategies targeting the ubiquitin‑proteasome system, including deubiquitinase‑targeting chimera and proteolysis‑targeting chimeras. Targeting ubiquitination and deubiquitination mechanisms presents a promising avenue for the treatment of PE. Further research into these pathways may lead to novel interventions aimed at improving maternal and fetal outcomes.
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