Abstract
Simple SummaryThe cellular prion protein PrPC is best known for its involvement, under its pathogenic isoform, in a group of neurodegenerative diseases. Notwithstanding, an emerging role for PrPC in various cancer-associated processes has attracted increasing attention over recent years. PrPC is overexpressed in diverse types of solid cancers and has been incriminated in various aspects of cancer biology, most notably proliferation, migration, invasion and metastasis, as well as resistance to cytotoxic agents. This article aims to provide a comprehensive overview of the current knowledge of PrPC with respect to the hallmarks of cancer, a reference framework encompassing the major characteristics of cancer cells.Beyond its causal involvement in a group of neurodegenerative diseases known as Transmissible Spongiform Encephalopathies, the cellular prion protein PrPC is now taking centre stage as an important contributor to cancer progression in various types of solid tumours. The prion cancer research field has progressively expanded in the last few years and has yielded consistent evidence for an involvement of PrPC in cancer cell proliferation, migration and invasion, therapeutic resistance and cancer stem cell properties. Most recent data have uncovered new facets of the biology of PrPC in cancer, ranging from its control on enzymes involved in immune tolerance to its radio-protective activity, by way of promoting angiogenesis. In the present review, we aim to summarise the body of literature dedicated to the study of PrPC in relation to cancer from the perspective of the hallmarks of cancer, the reference framework defined by Hanahan and Weinberg.
Highlights
Published: 8 October 2021The cellular prion protein PrPC was discovered in the mid-1980s as the normal counterpart of the scrapie prion protein, denoted PrPSc, itself responsible for the development of a group of fatal neurodegenerative diseases known as Transmissible SpongiformEncephalopathies or prion diseases [1]
Two non-mutually exclusive mechanisms may be at play: the proliferation of recipient cells may be directly regulated by exosomal PrPC, the level of which is increased following hypoxia [31], or it may depend upon other exosomal proteins whose abundance in exosomes is influenced by the expression of PrPC in cancer cells
We recently demonstrated that PrPC levels positively control the phosphorylation of neurofibromatosis type 2 (NF2) on serine 518, itself negatively regulating NF2 activity, in colorectal cancer [26]
Summary
The cellular prion protein PrPC was discovered in the mid-1980s as the normal counterpart of the scrapie prion protein, denoted PrPSc , itself responsible for the development of a group of fatal neurodegenerative diseases known as Transmissible Spongiform. The variety of PrPC isoforms may explain why by been ascribed a pletho a powerful strategy to understand how the corruption of these functions may contribute functions, ranging from broad roles in the physiology of the central nervous system to pathological contexts, prion diseases [7] and other disorders, including sistance to various of disorders stresses,orcell fate[8].and differentiation, adhesion an Alzheimer’s disease,types immune cancer. The contribution of this review, we will summarise the overall data relating to the biology of PrPC in cancer stem cell properties or theexcept potential therapeutic strategies to target this protein in c according to each hallmark, the enabling replicative immortality hallmark due to a will not discussed here and have beensome covered by pertaining several reviews [9,10,11,12]. I review, we will summarise the overall data relating to the biology of PrPC in canc cording to each hallmark, except the enabling replicative immortality hallmark du Cancers 2021, 13, 5032
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