Life sciences · Journal article
Frontiers in Oncology · September 28, 2026
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Prion proteins (PrP) are primarily known for their role in neurodegenerative conditions like Creutzfeldt-Jakob Disease, where the misfolded, pathogenic isoform PrPSc propagates by using the normal cellular prion protein, PrP c, as a template, leading to aggregation and neuronal death. PrP c is a widely expressed glycoprotein that, beyond its role in prion disease, has emerged in specific contexts as a modulator of several hallmark cancer processes, including proliferation, apoptosis resistance, cellular signaling, adhesion, survival, and motility. This paper explores current evidence on how PrP c, and its misprocessed isoform pro-PrP, contribute to tumor progression across multiple cancer types, using colorectal cancer (CRC) as a unifying disease model to integrate mechanisms that are otherwise dispersed across the literature. This review will examine PrP c ’s role in sustaining proliferative signaling, resisting apoptosis, promoting migration and metastasis through its interaction with filamin A (FLNa), and contributing to therapy resistance. The goal is to consider the extent to which these mechanisms converge specifically in CRC, and what this means for PrP c ’s potential as a diagnostic and therapeutic target.