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Yousaf, S.;  Ahmad, M.;  Wu, S.;  Zia, M.A.;  Ahmed, I.;  Iqbal, H.M.N.;  Liu, Q.;  Rehman, S.U. Cellular Prion Protein in Cancer Biology. Encyclopedia. Available online: (accessed on 11 December 2023).
Yousaf S,  Ahmad M,  Wu S,  Zia MA,  Ahmed I,  Iqbal HMN, et al. Cellular Prion Protein in Cancer Biology. Encyclopedia. Available at: Accessed December 11, 2023.
Yousaf, Saba, Muhammad Ahmad, Siwen Wu, Muhammad Anjum Zia, Ishtiaq Ahmed, Hafiz M. N. Iqbal, Qingyou Liu, Saif Ur Rehman. "Cellular Prion Protein in Cancer Biology" Encyclopedia, (accessed December 11, 2023).
Yousaf, S.,  Ahmad, M.,  Wu, S.,  Zia, M.A.,  Ahmed, I.,  Iqbal, H.M.N.,  Liu, Q., & Rehman, S.U.(2022, November 24). Cellular Prion Protein in Cancer Biology. In Encyclopedia.
Yousaf, Saba, et al. "Cellular Prion Protein in Cancer Biology." Encyclopedia. Web. 24 November, 2022.
Cellular Prion Protein in Cancer Biology

Prion-like proteins and prions (PrPC), the prion protein cellular form, shares 90% of its amino acid sequence with other mammalian proteins. PrPCs are expressed almost in all tissues of an organism, but a higher amount of PrPCs has been found in the central nervous system (CNS), particularly the synaptic membranes and PrPC are linked. Scrapie PrP (PrPSc), a mutant cellular prion protein with an altered structure, is assumed to be the key etiological cause of prion diseases. Cancers are worldwide health concerns, whether they are sporadic or hereditary. The fundamental mechanism that causes somatic or oncogenic mutations and ultimately aids cancer development is still unknown. However, mammalian cells with protein-only somatic inheritance may also contribute to cancerous malignancies. Emerging data from a recent study show that prion-like proteins and prions (PrPC) are crucial entities that have a functional role in developing neurological disorders and cancer. Furthermore, excessive PrPC expression profiling has also been detected in non-neuronal tissues, such as the lymphoid cells, kidney, GIT, lung, muscle, and mammary glands. PrPC expression is strongly linked with the proliferation and metastasis of pancreatic, prostate, colorectal, and breast malignancies. Experimental investigation presented that the PrPC expression, including the prion protein-coding gene (PRNP) and p53 ag are directly associated with tumorigenicity and metastasis (tumor suppressor gene). The ERK2 (extracellular signal-regulated kinase) pathway also confers a robust metastatic capability for PrPC-induced epithelial to mesenchymal transition. Additionally, prions could alter the epigenetic regulation of genes and overactive the mitogen-activated protein kinase (MAPK) signaling pathway, which promotes the development of cancer in humans. Protein overexpression or suppression caused by a prion and prion-like proteins has also been linked to oncogenesis and metastasis. Meanwhile, additional studies have discovered resistance to therapeutic targets, 

prion protein cancer biology PRNP

1. Introduction

The prion-like proteins and prions (PrPC) and PrPSc could interact with each other using α-helices present in PrPC and β-sheets of the PrPSc while the precise method of this transformation is still not fully known. Prion is a protein constituting infectious particles that leads to a variety of neurodegenerative diseases as well as cancer. There are two isoforms of the prion protein: the cellular prion protein (PrPC) and the scrapie prion protein (PrPSc) [1]. However, the precise role and mechanism of PrPSc are unknown. This research intends to shed light on PrPSc, the underlying cause of deadly illnesses, such as cancer and neurological disorders. In this reverence, there is a dire need to improve the survival rates, and considerable attention is required. PrPC can be exploited as a therapeutic target in cancer therapy. The glycosylphosphatidylinositol (GPI) is an anchored protein attached to the membrane of prion protein (PrPC) and the expression of PrPC is initiated during embryogenesis and maximum, during puberty. Cellular prion protein is present in peripheral organs, neurons and the nervous system [2]. PrPSc can cause disease (neurodegenerative disorders) in a certain way that normal prion protein found on cell surfaces behave abnormally (i.e., misfolding) and accumulate in the brain, which subsequently results in brain damage and neurodegenerative disorders like Creutzfeldt Jakob disease [3]. PrPC altered expression is involved in cancer progression, and PrPSc (i.e., altered variant) misfolded form is responsible for causing neurodegenerative diseases. More extensive work is required to rule out the exact mechanism of disease progression. Prions are normally distributed in the whole body of an organism, but disease-causing prions are distinguished in their structure and composition. PrPC has a lipid chain of GPI attached to its structure and is present in ample amounts in CNS [4]. In humans, prion protein (PrP) is encoded by the PRNP gene that is present on the 20th chromosome. Previously, it was assumed that PrPC primarily affects the CNS only. However, it is now found in other non-neuronal tissues like lungs, heart, kidneys, GIT, muscles, lymphoid cells, mammary glands, etc. [5]. It was reported that PrPC also participates in causing incurable diseases like breast carcinoma, gastric cancer, prostate cancer, and glioblastoma [6]. PrPC also boosts cancer cell proliferation, tumorigenesis, and G1/S transitions in cancer. In addition, PrPC introduces helpers to complete its function in the signaling pathways [7]. Thus, PrPC is a pathologically aggregated prion protein involved in neurodegenerative disorders [8].
PrP plays a significant role in the progression of various neurodegenerative disorders and cancer, but the precise pattern of their action is still unknown. The fluctuations in PrPC expression pattern (either increased or decreased) might cause the development of various malignancies such as the PrPSc misfolding could result in severe catastrophic neurological diseases.

2. Boosts Proliferation of Cancer Cells

PrPC has the ability to stimulate cancer cell growth and in gastric cancer cells, the overexpression of PrPC was found to be associated with cell proliferation by activating the phosphatidylinositide 3-kinase (PI3K) pathway and promoting the G1/S phase transition by upregulating cyclin D1 [9]. The transition from the G1 to S phase is likewise related to PrPC. In HT29 (cell line for human colorectal adenocarcinoma) colon cancer cells, knocking down PrPC decreased the cell growth and increased the inhibitory effect of fucoidan by reducing the production of cyclins and cyclin-dependent kinase (CDK) [10]. In glioblastoma (GBM) cells, the PrPC interaction with the co-chaperone Hsp70/90 organizing protein (HOP) could boost the proliferation via activating the PI3K and extracellular signal-regulated kinase (ERK1/2) pathways [11]. Additionally, the HOP and PrPC interaction might increase the propagation of glioma stem-like cells, while the decreased expressions of PrPC suggested that HOP could be used as a GBM therapy [12]. Cancer cells prefer to produce their energy by aerobic glycolysis; therefore, this leads to a reduction in the available energy for synthesis, cell survival, and proliferation [13]. The overexpression of PrPC could also induce the Warburg effect in colorectal cancer cells by up-regulating glucose transporter 1 (Glut1) expression, which in turn enhances the absorption of glucose via epigenetic regulation of the Fyn-HIF-2a-Glut1 pathway [14]. Moreover, it also interacted with Notch1 to promote proliferation in pancreatic ductal adenocarcinoma (PDAC) [15]. PrPC stimulates the ERK1/2 and PI3K/protein kinase B (AKT) signaling pathways that promote cell proliferation in schwannoma cells when it binds with the 37/67 kDa non-integrin laminin receptor. In this way, prion protein interrupts different signaling pathways and metabolic cycles, altering normal biosynthetic processes thereby promoting cancer cell invasion and growth.

3. Prion-Like Proteins and Prions Encourages Cancer Cells to Invade and Spread

Over 90 percent of the total cancer-related deaths are caused by metastasis, although the mechanisms which aid the phenomena require further exploration. The metastatic process is generally categorized into two stages. In the initial phase, the cancerous cells physically move from one location to another [16], whereas the second stage involves the initial tumor spreading to additional distant tissues. Cancer cells that have spread colonize their new surroundings. Epithelial-to-mesenchymal transition-in-between is referred to as EMT [17] and demonstrated to be significantly involved in several in vitro models. The PrP gene expression dramatically increased during EMT and the upregulated PrPC let the EMT-like cells to be undifferentiated. This characteristic has also been identified in invasive colorectal cancer cells (CRC) [18]. Most details about the EMT amplification in PrPC mechanics are unclear [19]. Moreover, the SATB1 (special AT-rich sequence-binding protein 1) is a nuclear matrix-associated protein. Tumor metastasis can be characterized through chromatin structure modifications, up-regulating the metastasis-associated genes, and down-regulation of the tumor-suppressor genes [20]. Fyn and specificity protein 1 (SP1) played a significant role in the reduced expression of SATB1 and tumor progression in CRC following PRNP knockdown. The PrPC-Fyn-SP1-SATB1 axis may be up-regulated by PrPC, which would support tumor metastasis [21]. Moreover, overexpression of g-Syn and PrPC is also found in CRC. They might contribute to the spread of colorectal cancer cells by inducing an inflammatory response [22]. While the increased expression of PrPC in metastatic gastric cancer cells can endorse the invasion and metastasis by activating the mitogen-activated protein kinases (MEK)/ERK pathway, which leads to matrix metalloproteinase-11 transactivation (MMP11) [23]. The MMP11 can aid in tissue remodeling, inflammation, and matrix breakdown. The signal that PrPC uses to encourage invasion must be sent by its N-terminal section [24]. A type 1 endogenous matrix metalloproteinase inhibitor (MT1-MMP) is a tissue inhibitor of metalloprotease (TIMP) [25] and TIMP adhesion to the prion protein GPI anchor resulted in a membrane-bound, high-affinity designer TIMP that is exhibited on the cell surface and co-localized with cellular MTI-MMP. As depicted in Figure 1, PrPC as a main regulator of CSCs phenotype, biology, and functioning [19].
Figure 1. Schematic illustration of the regulatory role of PrPC in promoting cancer stem cells (CSCs) self-renewal, proliferation, and migration patterns. For a detailed description of CSCs phenotype, biology, functioning, and cross-talk between CSCs and major cellular components of the tumor micro-environment (TME), see Ref. [26]. Reprinted from Ref. [19] with permission under the terms and conditions of the Creative Commons Attribution (CC BY) license.
PrPC has been shown to boost EMT in colorectal cancer stem cells by activating the ERK2/(MAPK1) pathway. Thus, providing affirmed bases that the morphology of CSCs (cancer stem cells) and EMT are directly interlinked. Notch1 could influence the CSCs [9]. Both the CSC and EMT are co-localized on the cellular membrane and act as the downstream effectors of the PrPC that promote the metastasis of pancreatic cancer cells [27]. Through the down-regulation of PrPC-Oct4 pathways, 5-fluorouracil (5-FU) and melatonin can lower the octamer-binding transcription factor 4 (Oct4) markers for colon CSCs [28]. This method will probably prevent cancer from spreading by decreasing tumor-mediated angiogenesis [29]. PrPC-containing exosomes released by CRC may promote tumor growth even further by alleviating the body’s amount of cellular prion protein [30]. The anti-PrPC and 5-FU combination also slow down the growth of tumors. The immune system is one of the most important systems for halting the emergence and development of cancer [31]. One of the key targets of cancer immunotherapy is the regulatory T cells (Tregs), which suppress the immune response. Increased PrPC expression stimulates the proliferation of regulatory T cells by up-regulating the altered growth factor-beta (TGF-b) and programmed death ligand-1 (PD-L1), which speeds up the progression of the tumor, according to a lung metastatic melanoma model in Prnp0/0 and Tga20 animals. Moreover, it was also reported that PrPC expression encourages cancer cell spread [6]. However, one study reported that knocking down PRNP in mesenchymal embryonic mice cells with Ras/Myc transformation increased the likelihood of lung metastasis. Meanwhile, to fully understand the role of PrPC in cancer spread, further molecular mechanism-based modeled research is required.

4. Prion-Like Proteins and Prions Fosters Drug Resistance in Cancer Cells

Drug resistance predominantly antibiotics resistance is a crucial aspect in cancer treatment and can be caused by a variety of reasons [32]. Multi-drug resistance (MDR) and cell death inhibition are two important concerned mechanisms explaining the PrPC participation in developing drug resistance while treating cancer. The ability of a cancer cell to resist a variety of anti-cancer medications is referred to as multi-drug resistance (MDR) [33]. Necrosis, autophagic cell death, and apoptosis are the three main kinds of cell death (Type I programmed cell death). Apoptosis is characterized by DNA cleavage, chromatin condensation, membrane protrusions, cell shrinkage, and caspase activation [34]. A lysosomal intracellular destruction pathway called excessive autophagy, which is a kind of autophagy, results in autophagic cell death.
Necrosis (non-programmed cell death), which is brought on by unforeseen impacts on the cells, is characterized by plasma membrane rupture accompanied by cytoplasmic leakage [23]. In a variety of cancer cell types, PrPC up-regulation can lead to treatment resistance. PrPC increases the production of cell cycle-associated proteins, which in turn encourages growth and survival in colorectal cancer cells [35]. PrPC also stimulates the PI3K-Akt signaling pathway. Similarly, by up-regulating the inhibitors of apoptosis proteins, PrPC overexpression enabled colorectal cancer LS174T cells more resilient to doxorubicin-induced apoptosis (IAPs) [36]. When PrPC is up-regulated, oxaliplatin resistance is brought on by an increase in superoxide dismutase (SOD) and catalase activity, and also a decrease in endoplasmic reticulum stress and apoptosis [37]. PrPC interferes with the signaling cascade and apoptotic inhibitors, preventing cancer cell death by particular medicines. The phenomenon of drug resistance in several types of cancer is a crucial challenge.

5. Prion-Like Proteins and Prions as a Potential Cancer Biomarker

In a high-resolution cell membrane proteome analysis, PrPC was identified as a potential biomarker for the progression of colorectal adenoma to carcinoma. PrPC was able to differentiate between patients with early-stage colorectal cancer and normal colon tissue as well as high-risk and low-risk adenomas [38]. Several lines of evidence have suggested the possible functioning of PrPCs in modulating cancer susceptibility to chemotherapy and, as a result, monitoring the therapeutic efficacy and patient prognosis [39]. Individuals with higher PrPC expression exhibited better therapeutic tolerance, worsening 2-year survival, and a high fatality rate compared to those with lower PrPC expression [40]. As a result, PrPC overexpression in estrogen receptor (ER)-negative breast cancer patients is linked to decreased chemotherapy sensitivity, suggesting that PrPC could be a predictor of adjuvant chemotherapy benefit in ER-negative patients [28]. PrPC expression in human PDAC biopsies is associated with a worse prognosis than in PrP-negative cases, demonstrating that PrPC plays a vital tumor-promoting role in Pancreatic ductal adenocarcinoma (PDAC) [41]. Surprisingly, western blot and immunohistochemical examinations of surgically excised PDAC specimens reveal a significant difference between PDAC and control tissues [42]. PrPC is overexpressed very selectively within the ductal compartment in PDAC specimens, whereas normal control tissues only have a few ductal epithelial cells with moderate PrP staining [43]. While, the PrPC expression was not affected by the presence of dysplastic areas around the “healthy” pancreas, implying that PrPC levels are linked to tumor invasiveness and aggressiveness rather than preneoplastic lesions. However, further trials are needed to fully establish the predictive usefulness of PrPC discovery [44]. Prion protein even resists cancer cells’ response to pharmaceutical treatment. PrPC may alter the susceptibility of cancer to chemotherapy, which would allow it to be used to track the treatment’s effectiveness and patient prognosis.

6. Targeting Prion-Like Proteins and Prions as a Cancer Treatment

Numerous circumstantial evidence pointed the possibility that prion proteins could result in protein-only inheritance in the setting of the onset and development of cancer. It is hypothesized that the transformation of a regular cellular protein into a prion and the accompanying metabolic disturbance may increase the characteristics of cancer due to the overexpression of prion proteins and their effects on apoptosis, kinase signaling, and chaperone sequestration [4][45]. Infecting prions, like PrPSc, can spread to nearby cells via exosomes implying that prion introduction may aid in developing the cancer phenotype. Prior to the development of genetic mutations, this can encourage the rapid emergence of phenotypic heterogeneity, including chemotherapeutic tolerance, cancer spread, and metastasis. Therefore, it is imperative to ascertain the function of PrPC itself in cancer as well as prions that target PrPC (like PrPSc) and perhaps additional prions that have not yet been identified but may have an impact on other cellular signaling proteins that ultimately affect cancer [22][43][44]. Thus, available genetics or theoretical information could be used to develop possible plans for better prognostication, early detection, therapeutic intervention, and prevention of prion-dependent diseases, including various cancer types [4][28][32][45][46]. The data acquired could be used to develop prospective strategies to improve prognosis, early diagnosis, therapeutic intervention, and prevention of prion-dependent disorders, such as different cancer varieties. Prion protein has also been involved in the proliferation of carcinoma cells, which can be fatal.


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