Cholesterol suppresses AMFR-mediated PDL1 ubiquitination and degradation in HCC.

ABSTRACT: The degradation of proteasomes or lysosomes is emerging as a principal determinant of programmed death ligand 1 (PDL1) expression, which affects the efficacy of immunotherapy in various malignancies. Intracellular cholesterol plays a central role in maintaining the expression of membrane receptors; however, the specific effect of cholesterol on PDL1 expression in cancer cells remains poorly understood. Cholesterol starvation and stimulation were used to modulate the cellular cholesterol levels. Immunohistochemistry and western blotting were used to analyze the protein levels in the samples and cells. Quantitative real-time PCR, co-immunoprecipitation, and confocal co-localization assays were used for mechanistic investigation. A xenograft tumor model was constructed to verify these results

SUBMITTER: Shao WQ 

PROVIDER: S-EPMC11842428 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature