USP28 promotes tumor progression and glycolysis by stabilizing PKM2/Hif1-α in cholangiocarcinoma
View abstract on PubMed
Summary
This summary is machine-generated.Ubiquitin specific protease 28 (USP28) promotes cholangiocarcinoma progression by deubiquitinating PKM2, activating Hif1-α signaling and glycolysis. This finding highlights USP28 as a potential therapeutic target for this cancer.
Area Of Science
- Biochemistry
- Oncology
- Molecular Biology
Background
- Ubiquitination is a key protein modification reversed by deubiquitinating enzymes (DUBs).
- Ubiquitin-specific protease 28 (USP28) is implicated in cancer progression, but its role in cholangiocarcinoma (CCA) is unknown.
Purpose Of The Study
- To investigate the role and molecular mechanisms of USP28 in cholangiocarcinoma (CCA).
Main Methods
- USP28 expression analysis via tissue microarray, qRT-PCR, and databases.
- In vitro and in vivo functional assays to assess USP28's impact on CCA progression.
- Western blotting, immunofluorescence, and mass spectrometry to explore downstream pathways.
Main Results
- Higher USP28 expression in CCA tissues correlated with malignancy and poor prognosis.
- USP28 deubiquitinates PKM2, activating Hif1-α signaling.
- USP28 promotes glycolysis and tumor progression in CCA.
Conclusions
- USP28 enhances CCA progression by deubiquitinating PKM2, activating Hif1-α, and increasing glycolysis.
- USP28 is a potential therapeutic target for cholangiocarcinoma.
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