Ubiquitin-Specific Protease 1 Promotes Bladder Cancer Progression by Stabilizing c-MYC
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View abstract on PubMed
Summary
This summary is machine-generated.High expression of ubiquitin-specific protease 1 (USP1) promotes bladder cancer progression by stabilizing c-MYC. USP1 may be a new therapeutic target for bladder cancer treatment.
Area Of Science
- Oncology
- Molecular Biology
- Biochemistry
Background
- Ubiquitination is a critical post-transcriptional modification for cell homeostasis.
- Ubiquitin-specific protease 1 (USP1), a deubiquitination enzyme, is linked to tumor progression.
- The role of USP1 in bladder cancer remains largely uncharacterized.
Purpose Of The Study
- To investigate USP1 expression levels in bladder cancer.
- To elucidate the functional role of USP1 in bladder cancer progression.
- To identify potential therapeutic targets for bladder cancer.
Main Methods
- USP1 expression analysis using GEPIA web server.
- Construction of USP1-knockout and USP1-overexpressing bladder cancer cell lines (UMUC3, T24).
- Cellular assays (CCK8, colony formation, Transwell) to assess proliferation and migration.
- RNA-sequencing and dual-luciferase reporter assays to identify signaling pathways.
- Co-immunoprecipitation and immunofluorescence to study USP1-c-MYC interaction.
- In vivo studies using a xenograft mouse model.
Main Results
- USP1 expression is upregulated in bladder cancer and correlates with poor patient prognosis.
- USP1 overexpression enhances bladder cancer cell proliferation, clone formation, and migration.
- USP1 deficiency inhibits tumor growth in vivo.
- The c-MYC pathway is significantly activated by USP1.
- USP1 interacts with c-MYC and enhances its stability in a catalytically dependent manner.
Conclusions
- Elevated USP1 expression drives bladder cancer progression through c-MYC stabilization.
- USP1 represents a potential novel therapeutic target for bladder cancer treatment.
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