CD44/Cellular prion protein interact in multidrug resistant breast cancer cells and correlate with responses to neoadjuvant chemotherapy in breast cancer patients

Cheng, Yuanyuan; Tao, Lili; Xu, Jiawen; Li, Qingquan; Yu, Juan; Jin, Yonglong; Chen, Qi; Xu, Zu-De; Zou, Qiang; Liu, Xiuping

doi:10.1002/mc.22021

Cited by 50 publications

(57 citation statements)

References 35 publications

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“…It has been suggested that gain of PrP c function may contribute to cancer growth and metastasis in patients with PrP c -associated cancer (25,26). Previous studies on PrP c in cancer are generally consistent with the notion that PrP c expression increases resistance to cytotoxicity (27)(28)(29)(30)(31).…”

Section: Effect Of Fucoidan On Ht29 Colon Cancer Cell Apoptosis Htmentioning

confidence: 59%

Silencing Prion Protein in HT29 Human Colorectal Cancer Cells Enhances Anticancer Response to Fucoidan

Yun

Lee

et al. 2016

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Developing natural products and dietary supplements has proven to be a promising strategy for the cancer therapy and prevention. Among them, fucoidan, which is isolated from brown seaweed such as Cladosiphon okamuranus and Fucus evanescens (1, 2), is structurally similar to heparin, with a substantial percentage of L-fucose (3, 4). Recent studies have shown its various effects on biological activities such as antiinflammatory, anti-coagulant (5), anti-HIV, and anticancer (6-9) activities. With respect to cancer therapy, fucoidan appears to be highly efficient in treating certain types of cancer, including breast, prostate and lung, as well as leukemia (10-12). Furthermore, fucoidan can also play a crucial role in inhibiting induced cancer signaling molecules, such as vascular endothelial growth factor (VEGF) (13,14). Although these results support the potential development of fucoidan as an anticancer drug, there is little information on the anticancer effect of fucoidan on colorectal cancer (CRC).CRC is the second most commonly diagnosed cancer among females and third among males worldwide. It also contributes significantly to cancer-related deaths, despite continuous progress in developing diagnostic and therapeutic methods (15). It is thought that CRC may be caused by a combination of both genetic susceptibilities and Iifestyle factors such as a meat-rich diet (16). Although the discovery of factors that cause CRC give new insights into the growth and metastasis of CRC, there is still little information on the etiology of most CRC, therapeutic agents, and anti-CRC targeting molecules. However, cellular prion protein (PrP c ) expression has been identified as a risk or susceptibility factor for developing CRC (17). In essence, PrP c is a highly conserved cell-surface glycoprotein that has been identified in all vertebrates, with the same protein sequence as the prion proteins that cause 4449

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Section: Effect Of Fucoidan On Ht29 Colon Cancer Cell Apoptosis Htmentioning

confidence: 59%

Silencing Prion Protein in HT29 Human Colorectal Cancer Cells Enhances Anticancer Response to Fucoidan

Yun

Lee

et al. 2016

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“…Moreover, more recently it was suggested that PrP C might also promote human tumor development and diffusion, and the induction of drug resistance [22, 36]. PrP C overexpression was observed in gastric cancer lesions as compared to non-tumor tissues representing a predictive marker of poor prognosis [66], while PrP C down-regulation reduced tumor cell proliferation [67] or caused cell death via the activation of the autophagic pathway [68]. However, most of these studies have been performed in continuous cell lines evaluating the effects of PrP C on the biological behavior of the cells.…”

Section: Discussionmentioning

confidence: 99%

Cellular prion protein controls stem cell-like properties of human glioblastoma tumor-initiating cells

et al. 2016

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Prion protein (PrPC) is a cell surface glycoprotein whose misfolding is responsible for prion diseases. Although its physiological role is not completely defined, several lines of evidence propose that PrPC is involved in self-renewal, pluripotency gene expression, proliferation and differentiation of neural stem cells. Moreover, PrPC regulates different biological functions in human tumors, including glioblastoma (GBM). We analyzed the role of PrPC in GBM cell pathogenicity focusing on tumor-initiating cells (TICs, or cancer stem cells, CSCs), the subpopulation responsible for development, progression and recurrence of most malignancies. Analyzing four GBM CSC-enriched cultures, we show that PrPC expression is directly correlated with the proliferation rate of the cells. To better define its role in CSC biology, we knocked-down PrPC expression in two of these GBM-derived CSC cultures by specific lentiviral-delivered shRNAs. We provide evidence that CSC proliferation rate, spherogenesis and in vivo tumorigenicity are significantly inhibited in PrPC down-regulated cells. Moreover, PrPC down-regulation caused loss of expression of the stemness and self-renewal markers (NANOG, Sox2) and the activation of differentiation pathways (i.e. increased GFAP expression). Our results suggest that PrPC controls the stemness properties of human GBM CSCs and that its down-regulation induces the acquisition of a more differentiated and less oncogenic phenotype.

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“…33 Moreover, PrP c interacts with CD44 and both proteins enhance the ability of migration and invasion of breast cancer cells. 36 Surprisingly, in this latter study, a predominant nuclear localization of PrP c in the breast tumor samples was observed, which, as emphasized by the authors, needed further investigations. In that context, it is interesting to note that CD44 is a target gene of Wnt effectors, the b-catenin/TCF complex, 37 that we demonstrated activated by nuclear PrP c .…”

Section: Prp C Interaction With Junctional and Nuclear Partners: A Romentioning

confidence: 56%

The nucleo-junctional interplay of the cellular prion protein: A new partner in cancer-related signaling pathways?

Rousset

Leturque

Thenet

2016

Prion

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ABSTRACT. The cellular prion protein PrP c plays important roles in proliferation, cell death and survival, differentiation and adhesion. The participation of PrP c in tumor growth and metastasis was pointed out, but the underlying mechanisms were not deciphered completely. In the constantly renewing intestinal epithelium, our group demonstrated a dual localization of PrP c , which is targeted to cell-cell junctions in interaction with Src kinase and desmosomal proteins in differentiated enterocytes, but is predominantly nuclear in dividing cells. While the role of PrP c in the dynamics of intercellular junctions was confirmed in other biological systems, we unraveled its function in the nucleus only recently. We identified several nuclear PrP c partners, which comprise g-catenin, one of its desmosomal partners, b-catenin and TCF7L2, the main effectors of the canonical Wnt pathway, and YAP, one effector of the Hippo pathway. PrP c up-regulates the activity of the b-catenin/TCF7L2 complex and its invalidation impairs the proliferation of intestinal progenitors. We discuss how PrP c could participate to oncogenic processes through its interaction with Wnt and Hippo pathway effectors, which are controlled by cell-cell junctions and Src family kinases and dysregulated during tumorigenesis. This highlights new potential mechanisms that connect PrP c expression and subcellular redistribution to cancer.

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CD44/Cellular prion protein interact in multidrug resistant breast cancer cells and correlate with responses to neoadjuvant chemotherapy in breast cancer patients

Cited by 50 publications

References 35 publications

Silencing Prion Protein in HT29 Human Colorectal Cancer Cells Enhances Anticancer Response to Fucoidan

Silencing Prion Protein in HT29 Human Colorectal Cancer Cells Enhances Anticancer Response to Fucoidan

Cellular prion protein controls stem cell-like properties of human glioblastoma tumor-initiating cells

The nucleo-junctional interplay of the cellular prion protein: A new partner in cancer-related signaling pathways?

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