UPP1 (Uridine Phosphorylase 1)

Further study revealed that KLF5 negatively regulated the expression of UPP1 through transcriptional modulation. Our findings establish that the dysregulation of UPP1 in ESCC is modulated by METTL3 in an m6A-YTHDC1-KLF5-mediated manner, indicating a potential therapeutic target for ESCC.

Knockout or inhibition of UPP1 in mice with mammary tumours increases T-cell numbers and reduces fibronectin content in the lung, and decreases the proportion of mice that develop lung metastasis. These data indicate that UPP1 influences neutrophil behaviour and extracellular matrix deposition in the lung, and suggest that circulating uracil could be a marker of metastasis, and that pharmacological inhibition of UPP1 could be a strategy to reduce recurrence.

This study identifies UPP1 and AHSA1 as key proteins linked to PC differentiation and progression, highlighting their potential as diagnostic markers and therapeutic targets. These insights enhance our understanding of the molecular mechanisms underlying PC and open new avenues for precision treatment strategies.

Alterations induced by KMT5C knockdown were partly reversed by UPP1 inhibition. Overall, we demonstrate that KMT5C, recruited by NR2C2, suppresses OSCC progression by inhibiting UPP1 transcription in a H4K20me3-dependent way.

Based on these findings, we propose that the TYMP-UPP1 complex, co-regulated by MAZ, plays a pivotal role in nucleotide metabolism in ccRCC. These results suggest that TYMP may contribute to the pathophysiology of ccRCC and that promoter methylation offers potential as a prognostic indicator, providing novel insights into the molecular underpinnings of ccRCC and potential avenues for therapeutic intervention.

These findings highlight the power of combining diverse machine learning methods to identify valuable clinical markers involved in glioma pathogenesis. Identifying UPP1 as a tumor growth and immune escape driver may be a promising therapeutic target for this devastating disease.

However, the STAT3 inhibitor diminished UPP1 expression because STAT3 can bind to the UPP1 promoter. In conclusion, UPP1 was significantly activated by the IL-6/STAT3 pathway and could modulate glycolysis to regulate cell proliferation and cell-cycle progression in keratinocytes during the development of psoriasis.