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USP7 promotes cervical cancer progression by stabilizing MTDH expression through deubiquitination
Na Wang1, Jing Xu2, Yujing Wang1
1Department of Gynecology, The First Hospital of Hebei Medical University, No. 89, Donggang Road, Yuhua District, Shijiazhuang City, 050031, Hebei Province, China.
Journal of Cancer Research and Clinical Oncology
|April 16, 2024
Summary
Ubiquitin specific protease 7 (USP7) promotes cervical cancer (CC) progression by stabilizing metadherin (MTDH). USP7 deubiquitination of MTDH enhances CC cell proliferation, migration, invasion, angiogenesis, and tumor growth.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- Metadherin (MTDH) and ubiquitin specific protease 7 (USP7) are implicated in cervical cancer (CC) tumorigenesis.
- USP7 functions as a deubiquitinating enzyme, suggesting a role in regulating protein stability.
Purpose of the Study:
- To investigate if USP7 influences CC progression by interacting with MTDH.
- To determine if USP7 regulates MTDH stability through deubiquitination.
Main Methods:
- Gene and protein expression analyzed via qRT-PCR and western blotting.
- Cellular functions assessed using EdU, flow cytometry, transwell, and tube formation assays.
- Protein interactions confirmed by co-immunoprecipitation; in vivo efficacy tested in a mouse xenograft model.
Main Results:
- MTDH overexpression correlated with enhanced CC cell proliferation, migration, invasion, angiogenesis, and M2 polarization.
- USP7 directly binds and deubiquitinates MTDH, stabilizing it.
- USP7 knockdown inhibited CC progression, effects reversed by MTDH overexpression; USP7 knockdown impeded tumor growth in vivo.
Conclusions:
- USP7 promotes CC proliferation, migration, invasion, angiogenesis, and M2 polarization in vitro.
- USP7 enhances CC tumor growth in vivo by regulating MTDH stability.
- USP7-mediated regulation of MTDH is a key driver of cervical cancer progression.
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