ArticleJournal of physiology and biochemistry2025
P4HA2 promotes the progression of thyroid cancer by regulating PFKP-mediated glycolysis.
Article in Journal of physiology and biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- HNRNPU K181 Lactylation Drives Cervical Cancer Growth by Upregulating PHGDH and Reprogramming Serine Metabolism.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Targeting phosphofructokinase in cancer: integrating natural products for metabolic reprogramming and therapeutic innovation.Frontiers in pharmacology · 2026Review
- PFKP in malignant tumors: bridging metabolic reprogramming, post-translational modifications, and the immunosuppressive microenvironment.Frontiers in cell and developmental biology · 2026Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Emerging evidence suggests that prolyl-4-hydroxylase α subunit 2 (P4HA2) plays critical roles in cancer progression through multiple mechanisms. Notably, P4HA2 has been implicated in modulating glycolytic pathways in malignancies. Phosphofructokinase (PFKP), a key glycolytic enzyme, exhibits significant overexpression in thyroid cancer. This study investigates the functional of P4HA2 in thyroid cancer and elucidates the P4HA2/PFKP axis in regulating cancer cell glycolysis. Bioinformatics analysis using GEPIA website revealed P4HA2 expression patterns in thyroid cancer samples. P4HA2 protein levels were detected in thyroid cancer cell lines by western blot assay. Functional characterization was performed through siRNA-mediated P4HA2 knockdown followed by evaluation of proliferative capacity, cell cycle progression, migratory/invasive potential, and glycolytic activity. Rescue experiments employing PFKP overexpression were conducted to delineate molecular interactions. Significant P4HA2 up-regulation was observed in thyroid cancer tissues and cell lines. P4HA2 silencing marked inhibited cellular proliferation, suppressed cell cycle regulators, and attenuated metastatic potential. Glycolytic parameters including glucose consumption, lactate production, and ATP synthesis were significantly compromised following P4HA2 knockdown. Mechanistically, P4HA2 depletion down-regulated PFKP expression, while PFKP overexpression partially rescued the oncogenic phenotype. Our data indicated that P4HA2 promoted cell proliferation, cell cycle, migration, invasion, glycolysis and tumor growth, suggesting that it might be a valuable therapeutic target for thyroid cancer.
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