Abstract

Prion protein has two isoforms including cellular prion protein (PrPC) and scrapie prion protein (PrPSc). PrPSc is the pathological aggregated form of prion protein and it plays an important role in neurodegenerative diseases. PrPC is a glycosylphosphatidylinositol (GPI)-anchored protein that can attach to a membrane. Its expression begins at embryogenesis and reaches the highest level in adulthood. PrPC is expressed in the neurons of the nervous system as well as other peripheral organs. Studies in recent years have disclosed the involvement of PrPC in various aspects of cancer biology. In this review, we provide an overview of the current understanding of the roles of PrPC in proliferation, cell survival, invasion/metastasis, and stem cells of cancer cells, as well as its role as a potential therapeutic target.

Highlights

  • Prion protein (PrP) is expressed throughout the whole body

  • Studies in recent years show that Cellular prion protein (PrPC) is involved in various aspects of cancer biology such as cell proliferation, metastasis, cell death, drug resistance and cancer stem cells [14,15,16,17,18,19,20,21]

  • Liang et al demonstrated that overexpression of PrPC promoted cell proliferation through activation of the phosphatidylinositide 3kinase (PI3K) pathway and promotion of the G1/S phase transition by upregulating cyclin D1, in gastric cancer cells [22]

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Summary

INTRODUCTION

Prion protein (PrP) is expressed throughout the whole body. It has two isoforms, cellular prion protein (PrPC) and its pathogenic form-scrapie prion protein (PrPSc) [1, 2]. PrPSc is well known for its ability to cause a series of neurodegenerative diseases in human and other mammals [1, 3] It results from post-translational conversion of the glycosylphosphatidylinositol (GPI)-anchored PrPC [4, 5]. The biosynthetic pathway of PrPC is similar to that of other membrane-attached and secreted proteins [5] (Figure 1). It is synthesized in endoplasmic reticulum (ER)-attached ribosomes followed by its import into ER where it is glycosylated and modified by GPI anchor before it is transported into Golgi for further modification.

Cellular Prion Protein and Cancer
PrPC PROMOTES CANCER CELL PROLIFERATION
PrPC PROMOTES CANCER CELL DRUG RESISTANCE
PrPC PROMOTES CANCER STEM CELL DEVELOPMENT
CONCLUSION
Findings
AUTHOR CONTRIBUTIONS
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