The multiple functions of PrPC in physiological, cancer, and neurodegenerative contexts

Grimaldi, Izabella; Leser, Felipe Saceanu; Janeiro, José Marcos; Rosa, Bárbara Gomes da; Campanelli, Ana Clara; Romão, Luciana; Lima, Flávia Regina Souza

doi:10.1007/s00109-022-02245-9

Cited by 9 publications

(5 citation statements)

References 220 publications

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“…Most PrP C are normally localized on the cell surface via a C-terminal, GPI anchor. It is also reported to overexpressed in many cancer cells and is regarded as an unfavorable prognostic marker in breast cancer, glioma, colorectal cancer, and gastric cancer. , To verify the correlation between PrP C and tumors, we used HA5-68 as a molecular probe to detect the expression of PrP C on the tumor cells stored in our laboratory.…”

Section: Resultsmentioning

confidence: 99%

DNA Aptamer Binding Octapeptide Repeat Region of Cellular Prion Protein

Sheng,

Zhang,

Long

et al. 2023

Anal. Chem.

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Section: Resultsmentioning

confidence: 99%

DNA Aptamer Binding Octapeptide Repeat Region of Cellular Prion Protein

Sheng,

Zhang,

Long

et al. 2023

Anal. Chem.

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“…Beyond the undoubted involvement of PrP C in neurological disorders [ 2 ], many proofs in recent years showed that it is overexpressed in diverse solid tumors and plays a role in the onset and development of cancer influencing cellular events, such as genome instability with consequent gene mutation, proliferation, migration and invasion together with resistance to autophagic death [ 16 , 148 ]. Among its wide number of ligands, PrP C interacts with RPSA protein, a versatile non integrin LM receptor whose overexpression in solid and haematological malignancies has been associated with the potential invasive and metastatic cell phenotype [ 10 , 50 ].…”

Section: Discussionmentioning

confidence: 99%

“…Silencing of PrP C expression through antisense oligonucleotide-based strategies could be helpful in the field of cancer therapy, as reported for certain type of tumors [ 48 , 148 ]. Recently, pro-PrP has been pinpointed as potential therapeutic target to reduce melanoma metastasis in vitro and in vivo, using a peptide that inhibited GPI–PSS of pro-PrP and some of its interacting partners [ 62 ].…”

Section: Discussionmentioning

confidence: 99%

Emerging roles of the cellular prion protein (PrPC) and 37/67 kDa laminin receptor (RPSA) interaction in cancer biology

Limone

Maggisano

Sarnataro

et al. 2023

Cell. Mol. Life Sci.

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The cellular prion protein (PrPC) is well-known for its involvement, under its pathogenic protease-resistant form (PrPSc), in a group of neurodegenerative diseases, known as prion diseases. PrPC is expressed in nervous system, as well as in other peripheral organs, and has been found overexpressed in several types of solid tumors. Notwithstanding, studies in recent years have disclosed an emerging role for PrPC in various cancer associated processes. PrPC has high binding affinity for 37/67 kDa laminin receptor (RPSA), a molecule that acts as a key player in tumorigenesis, affecting cell growth, adhesion, migration, invasion and cell death processes. Recently, we have characterized at cellular level, small molecules able to antagonize the direct PrPC binding to RPSA and their intracellular trafficking. These findings are very crucial considering that the main function of RPSA is to modulate key events in the metastasis cascade. Elucidation of the role played by PrPC/RPSA interaction in regulating tumor development, progression and response to treatment, represents a very promising challenge to gain pathogenetic information and discover novel specific biomarkers and/or therapeutic targets to be exploited in clinical settings. This review attempts to convey a detailed description of the complexity surrounding these multifaceted proteins from the perspective of cancer hallmarks, but with a specific focus on the role of their interaction in the control of proliferation, migration and invasion, genome instability and mutation, as well as resistance to cell death controlled by autophagic pathway.

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“…In addition to its involvement in prion diseases, several studies have attributed plenty of physiological roles to PrP C including anti/pro-apoptosis, metal homeostasis, anti-oxidative damage, cell adhesion and migration, signaling, immune modulation, cell differentiation, and epithelial junctions [20][21][22][23][24][25][26][27]. Yet, the PrP C physiological function is still enigmatic, since no obvious phenotype was observed in PrP C knockout mice [28,29].…”

Section: Prp C Expression and Functionsmentioning

confidence: 99%

The Multifaceted Functions of Prion Protein (PrPC) in Cancer

Abi Nahed,

Safwan-Zaiter,

Gemy

et al. 2023

Cancers

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The cellular prion protein (PrPC) is a glycoprotein anchored to the cell surface by glycosylphosphatidylinositol (GPI). PrPC is expressed both in the brain and in peripheral tissues. Investigations on PrPC’s functions revealed its direct involvement in neurodegenerative and prion diseases, as well as in various physiological processes such as anti-oxidative functions, copper homeostasis, trans-membrane signaling, and cell adhesion. Recent findings have revealed the ectopic expression of PrPC in various cancers including gastric, melanoma, breast, colorectal, pancreatic, as well as rare cancers, where PrPC promotes cellular migration and invasion, tumor growth, and metastasis. Through its downstream signaling, PrPC has also been reported to be involved in resistance to chemotherapy and tumor cell apoptosis. This review summarizes the variance of expression of PrPC in different types of cancers and discusses its roles in their development and progression, as well as its use as a potential target to treat such cancers.

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The multiple functions of PrPC in physiological, cancer, and neurodegenerative contexts

Cited by 9 publications

References 220 publications

DNA Aptamer Binding Octapeptide Repeat Region of Cellular Prion Protein

DNA Aptamer Binding Octapeptide Repeat Region of Cellular Prion Protein

Emerging roles of the cellular prion protein (PrPC) and 37/67 kDa laminin receptor (RPSA) interaction in cancer biology

The Multifaceted Functions of Prion Protein (PrPC) in Cancer

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