| Summary: | Cellular prion protein (PrP<sup>C</sup>) is seminal to modulate a variety of baseline cell functions to grant homeostasis. The classic role of such a protein was defined as a chaperone-like molecule being able to rescue cell survival. Nonetheless, PrP<sup>C</sup> also represents the precursor of the deleterious misfolded variant known as scrapie prion protein (PrP<sup>Sc</sup>). This variant is detrimental in a variety of prion disorders. This multi-faceted role of PrP is greatly increased by recent findings showing how PrP<sup>C</sup> in its folded conformation may foster tumor progression by acting at multiple levels. The present review focuses on such a cancer-promoting effect. The manuscript analyzes recent findings on the occurrence of PrP<sup>C</sup> in various cancers and discusses the multiple effects, which sustain cancer progression. Within this frame, the effects of PrP<sup>C</sup> on stemness and differentiation are discussed. A special emphasis is provided on the spreading of PrP<sup>C</sup> and the epigenetic effects, which are induced in neighboring cells to activate cancer-related genes. These detrimental effects are further discussed in relation to the aberrancy of its physiological and beneficial role on cell homeostasis. A specific paragraph is dedicated to the role of PrP<sup>C</sup> beyond its effects in the biology of cancer to represent a potential biomarker in the follow up of patients following surgical resection.
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