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Open Access 01-04-2013 | Research article

Endoplasmic reticulum stress induces PRNP prion protein gene expression in breast cancer

Authors: Marc-André Déry, Julie Jodoin, Josie Ursini-Siegel, Olga Aleynikova, Cristiano Ferrario, Saima Hassan, Mark Basik, Andréa C LeBlanc

Published in: Breast Cancer Research | Issue 2/2013

Abstract

Introduction

High prion protein (PrP) levels are associated with breast, colon and gastric cancer resistance to treatment and with a poor prognosis for the patients. However, little is known about the underlying molecular mechanism(s) regulating human PrP gene (PRNP) expression in cancers. Because endoplasmic reticulum (ER) stress is associated with solid tumors, we investigated a possible regulation of PRNP gene expression by ER stress.

Methods

Published microarray databases of breast cancer tissues and breast carcinoma cell lines were analyzed for PrP mRNA and ER stress marker immunoglobulin heavy chain binding protein (BiP) levels. Breast cancer tissue microarrays (TMA) were immunostained for BiP and PrP. Breast carcinoma MCF-7, MDA-MB-231, HS578T and HCC1500 cells were treated with three different ER stressors - Brefeldin A, Tunicamycin, Thapsigargin - and levels of PrP mRNA or protein assessed by RT-PCR and Western blot analyses. A human PRNP promoter-luciferase reporter was used to assess transcriptional activation by ER stressors. Site-directed mutagenesis identified the ER stress response elements (ERSE). Chromatin immunoprecipitation (ChIP) analyses were done to identify the ER stress-mediated transcriptional regulators. The role of cleaved activating transcription factor 6α (ΔATF6α) and spliced X-box protein-1 (sXBP1) in PRNP gene expression was assessed with over-expression or silencing techniques. The role of PrP protection against ER stress was assessed with PrP siRNA and by using Prnp null cell lines.

Results

We find that mRNA levels of BiP correlated with PrP transcript levels in breast cancer tissues and breast carcinoma cell lines. PrP mRNA levels were enriched in the basal subtype and were associated with poor prognosis in breast cancer patients. Higher PrP and BiP levels correlated with increasing tumor grade in TMA. ER stress was a positive regulator of PRNP gene transcription in MCF-7 cells and luciferase reporter assays identified one ER stress response element (ERSE) conserved among primates and rodents and three primate-specific ERSEs that regulated PRNP gene expression. Among the various transactivators of the ER stress-regulated unfolded protein response (UPR), ATF6α and XBP1 transactivated PRNP gene expression, but the ability of these varied in different cell types. Functionally, PrP delayed ER stress-induced cell death.

Conclusions

These results establish PRNP as a novel ER stress-regulated gene that could increase survival in breast cancers.

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Kuwahara C, Takeuchi AM, Nishimura T, Haraguchi K, Kubosaki A, Matsumoto Y, Saeki K, Yokoyama T, Itohara S, Onodera T: Prions prevent neuronal cell-line death. Nature. 1999, 400: 225-226. 10.1038/22241.CrossRefPubMed

Bounhar Y, Zhang Y, Goodyer CG, LeBlanc A: Prion protein protects human neurons against Bax-mediated apoptosis. J Biol Chem. 2001, 276: 39145-39149. 10.1074/jbc.C100443200.CrossRefPubMed

Roucou X, Guo Q, Zhang Y, Goodyer CG, LeBlanc AC: Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons. J Biol Chem. 2003, 278: 40877-40881. 10.1074/jbc.M306177200.CrossRefPubMed

Roucou X, Giannopoulos PN, Zhang Y, Jodoin J, Goodyer CG, LeBlanc A: Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells. Cell Death Differ. 2005, 12: 783-795. 10.1038/sj.cdd.4401629.CrossRefPubMed

Bounhar Y, Mann KK, Roucou X, LeBlanc AC: Prion protein prevents Bax-mediated cell death in the absence of other Bcl-2 family members in Saccharomyces cerevisiae. FEMS Yeast Res. 2006, 6: 1204-1212. 10.1111/j.1567-1364.2006.00122.x.CrossRefPubMed

Lin DT, Jodoin J, Baril M, Goodyer CG, LeBlanc AC: Cytosolic prion protein is the predominant anti-Bax prion protein form: exclusion of transmembrane and secreted prion protein forms in the anti-Bax function. Biochim Biophys Acta. 2008, 1783: 2001-2012. 10.1016/j.bbamcr.2008.05.022.CrossRefPubMedPubMedCentral

Laroche-Pierre S, Jodoin J, LeBlanc AC: Helix 3 is necessary and sufficient for prion protein's anti-Bax function. J Neurochem. 2009, 108: 1019-1031. 10.1111/j.1471-4159.2008.05851.x.CrossRefPubMedPubMedCentral

Brown DR, Schulz-Schaeffer WJ, Schmidt B, Kretzschmar HA: Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp Neurol. 1997, 146: 104-112. 10.1006/exnr.1997.6505.CrossRefPubMed

Mitteregger G, Vosko M, Krebs B, Xiang W, Kohlmannsperger V, Nolting S, Hamann GF, Kretzschmar HA: The Role of the Octarepeat Region in Neuroprotective Function of the Cellular Prion Protein. Brain Pathol. 2007, 17: 174-183. 10.1111/j.1750-3639.2007.00061.x.CrossRefPubMedPubMedCentral

10.

Moore RC, Mastrangelo P, Bouzamondo E, Heinrich C, Legname G, Prusiner SB, Hood L, Westaway D, DeArmond SJ, Tremblay P: Doppel-induced cerebellar degeneration in transgenic mice. Proc Natl Acad Sci USA. 2001, 98: 15288-15293. 10.1073/pnas.251550798.CrossRefPubMedPubMedCentral

11.

Shmerling D, Hegyi I, Fischer M, Blattler T, Brandner S, Gotz J, Rulicke T, Flechsig E, Cozzio A, von Mering C: Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell. 1998, 93: 203-214. 10.1016/S0092-8674(00)81572-X.CrossRefPubMed

12.

Meslin F, Hamai A, Gao P, Jalil A, Cahuzac N, Chouaib S, Mehrpour M: Silencing of prion protein sensitizes breast adriamycin-resistant carcinoma cells to TRAIL-mediated cell death. Cancer Res. 2007, 67: 10910-10919. 10.1158/0008-5472.CAN-07-0512.CrossRefPubMed

13.

Diarra-Mehrpour M, Arrabal S, Jalil A, Pinson X, Gaudin C, Pietu G, Pitaval A, Ripoche H, Eloit M, Dormont D, Chouaib S: Prion protein prevents human breast carcinoma cell line from tumor necrosis factor alpha-induced cell death. Cancer Res. 2004, 64: 719-727. 10.1158/0008-5472.CAN-03-1735.CrossRefPubMed

14.

Meslin F, Conforti R, Mazouni C, Morel N, Tomasic G, Drusch F, Yacoub M, Sabourin JC, Grassi J, Delaloge S, Mathieu MC, Chouaib S, Andre F, Mehrpour M: Efficacy of adjuvant chemotherapy according to Prion protein expression in patients with estrogen receptor-negative breast cancer. Ann Oncol. 2007, 18: 1793-1798. 10.1093/annonc/mdm406.CrossRefPubMed

15.

Li C, Yu S, Nakamura F, Yin S, Xu J, Petrolla AA, Singh N, Tartakoff A, Abbott DW, Xin W, Sy MS: Binding of pro-prion to filamin A disrupts cytoskeleton and correlates with poor prognosis in pancreatic cancer. J Clin Invest. 2009, 119: 2725-2736. 10.1172/JCI39542.CrossRefPubMedPubMedCentral

16.

Li C, Yu S, Nakamura F, Pentikainen OT, Singh N, Yin S, Xin W, Sy MS: Pro-prion binds filamin A, facilitating its interaction with integrin beta1, and contributes to melanomagenesis. J Biol Chem. 2010, 285: 30328-30339. 10.1074/jbc.M110.147413.CrossRefPubMedPubMedCentral

17.

Liang J, Pan YL, Ning XX, Sun LJ, Lan M, Hong L, Du JP, Liu N, Liu CJ, Qiao TD, Fan DM: Overexpression of PrPC and its antiapoptosis function in gastric cancer. Tumour Biol. 2006, 27: 84-91. 10.1159/000092488.CrossRefPubMed

18.

Wang JH, Du JP, Zhang YH, Zhao XJ, Fan RY, Wang ZH, Wu ZT, Han Y: Dynamic changes and surveillance function of prion protein expression in gastric cancer drug resistance. World J Gastroenterol. 2011, 17: 3986-3993. 10.3748/wjg.v17.i35.3986.CrossRefPubMedPubMedCentral

19.

Pan Y, Zhao L, Liang J, Liu J, Shi Y, Liu N, Zhang G, Jin H, Gao J, Xie H, Wang J, Liu Z, Fan D: Cellular prion protein promotes invasion and metastasis of gastric cancer. FASEB J. 2006, 20: 1886-1888. 10.1096/fj.06-6138fje.CrossRefPubMed

20.

Liang J, Pan Y, Zhang D, Guo C, Shi Y, Wang J, Chen Y, Wang X, Liu J, Guo X, Chen Z, Qiao T, Fan D: Cellular prion protein promotes proliferation and G1/S transition of human gastric cancer cells SGC7901 and AGS. FASEB J. 2007, 21: 2247-2256. 10.1096/fj.06-7799com.CrossRefPubMed

21.

Liang J, Bai F, Luo G, Wang J, Liu J, Ge F, Pan Y, Yao L, Du R, Li X, Fan R, Zhang H, Guo X, Wu K, Fan D: Hypoxia induced overexpression of PrP(C) in gastric cancer cell lines. Cancer Biol Ther. 2007, 6: 769-774. 10.4161/cbt.6.5.4001.CrossRefPubMed

22.

Liang J, Luo G, Ning X, Shi Y, Zhai H, Sun S, Jin H, Liu Z, Zhang F, Lu Y, Zhao Y, Chen X, Zhang H, Guo X, Wu K, Fan D: Differential expression of calcium-related genes in gastric cancer cells transfected with cellular prion protein. Biochem Cell Biol. 2007, 85: 375-383. 10.1139/O07-052.CrossRefPubMed

23.

Liang J, Ge F, Guo C, Luo G, Wang X, Han G, Zhang D, Wang J, Li K, Pan Y, Yao L, Yin Z, Guo X, Wu K, Ding J, Fan D: Inhibition of PI3K/Akt partially leads to the inhibition of PrP(C)-induced drug resistance in gastric cancer cells. FEBS J. 2009, 276: 685-694. 10.1111/j.1742-4658.2008.06816.x.CrossRefPubMed

24.

McEwan JF, Windsor ML, Cullis-Hill SD: Antibodies to prion protein inhibit human colon cancer cell growth. Tumour Biol. 2009, 30: 141-147. 10.1159/000225243.CrossRefPubMed

25.

Li QQ, Sun YP, Ruan CP, Xu XY, Ge JH, He J, Xu ZD, Wang Q, Gao WC: Cellular prion protein promotes glucose uptake through the Fyn-HIF-2alpha-Glut1 pathway to support colorectal cancer cell survival. Cancer Sci. 2011, 102: 400-406. 10.1111/j.1349-7006.2010.01811.x.CrossRefPubMed

26.

Antonacopoulou AG, Palli M, Marousi S, Dimitrakopoulos FI, Kyriakopoulou U, Tsamandas AC, Scopa CD, Papavassiliou AG, Kalofonos HP: Prion protein expression and the M129V polymorphism of the PRNP gene in patients with colorectal cancer. Mol Carcinog. 2010, 49: 693-699.PubMed

27.

Jodoin J, Laroche-Pierre S, Goodyer CG, LeBlanc AC: Defective retrotranslocation causes loss of anti-Bax function in human familial prion protein mutants. J Neurosci. 2007, 27: 5081-5091. 10.1523/JNEUROSCI.0957-07.2007.CrossRefPubMed

28.

Bridges JP, Xu Y, Na CL, Wong HR, Weaver TE: Adaptation and increased susceptibility to infection associated with constitutive expression of misfolded SP-C. J Cell Biol. 2006, 172: 395-407. 10.1083/jcb.200508016.CrossRefPubMedPubMedCentral

29.

Tabuchi Y, Takasaki I, Kondo T: Identification of genetic networks involved in the cell injury accompanying endoplasmic reticulum stress induced by bisphenol A in testicular Sertoli cells. Biochem Biophys Res Commun. 2006, 345: 1044-1050. 10.1016/j.bbrc.2006.04.177.CrossRefPubMed

30.

Ron D, Walter P: Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol. 2007, 8: 519-529. 10.1038/nrm2199.CrossRefPubMed

31.

Kaufman RJ: Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 1999, 13: 1211-1233. 10.1101/gad.13.10.1211.CrossRefPubMed

32.

Prostko CR, Brostrom MA, Brostrom CO: Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticular signaling. Mol Cell Biochem. 1993, 255-265. 127-128

33.

Hampton RY: ER stress response: getting the UPR hand on misfolded proteins. Curr Biol. 2000, 10: R518-521. 10.1016/S0960-9822(00)00583-2.CrossRefPubMed

34.

Schroder M, Kaufman RJ: The mammalian unfolded protein response. Annu Rev Biochem. 2005, 74: 739-789. 10.1146/annurev.biochem.73.011303.074134.CrossRefPubMed

35.

Yoshida H, Haze K, Yanagi H, Yura T, Mori K: Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem. 1998, 273: 33741-33749. 10.1074/jbc.273.50.33741.CrossRefPubMed

36.

Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K: XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell. 2001, 107: 881-891. 10.1016/S0092-8674(01)00611-0.CrossRefPubMed

37.

Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D: Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell. 2000, 5: 897-904. 10.1016/S1097-2765(00)80330-5.CrossRefPubMed

38.

Kokame K, Kato H, Miyata T: Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. J Biol Chem. 2001, 276: 9199-9205. 10.1074/jbc.M010486200.CrossRefPubMed

39.

Kakiuchi C, Ishiwata M, Hayashi A, Kato T: XBP1 induces WFS1 through an endoplasmic reticulum stress response element-like motif in SH-SY5Y cells. J Neurochem. 2006, 97: 545-555. 10.1111/j.1471-4159.2006.03772.x.CrossRefPubMed

40.

Li M, Baumeister P, Roy B, Phan T, Foti D, Luo S, Lee AS: ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol Cell Biol. 2000, 20: 5096-5106. 10.1128/MCB.20.14.5096-5106.2000.CrossRefPubMedPubMedCentral

41.

Ma Y, Brewer JW, Diehl JA, Hendershot LM: Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol. 2002, 318: 1351-1365. 10.1016/S0022-2836(02)00234-6.CrossRefPubMed

42.

Roy B, Lee AS: The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex. Nucleic Acids Res. 1999, 27: 1437-1443. 10.1093/nar/27.6.1437.CrossRefPubMedPubMedCentral

43.

Ubeda M, Habener JF: CHOP gene expression in response to endoplasmic-reticular stress requires NFY interaction with different domains of a conserved DNA-binding element. Nucleic Acids Res. 2000, 28: 4987-4997. 10.1093/nar/28.24.4987.CrossRefPubMedPubMedCentral

44.

Healy SJ, Gorman AM, Mousavi-Shafaei P, Gupta S, Samali A: Targeting the endoplasmic reticulum-stress response as an anticancer strategy. Eur J Pharmacol. 2009, 625: 234-246. 10.1016/j.ejphar.2009.06.064.CrossRefPubMed

45.

Koumenis C: ER stress, hypoxia tolerance and tumor progression. Curr Mol Med. 2006, 6: 55-69. 10.2174/156652406775574604.CrossRefPubMed

46.

Hassan S, Baccarelli A, Salvucci O, Basik M: Plasma stromal cell-derived factor-1: host derived marker predictive of distant metastasis in breast cancer. Clin Cancer Res. 2008, 14: 446-454. 10.1158/1078-0432.CCR-07-1189.CrossRefPubMed

47.

Lin JH, Li H, Yasumura D, Cohen HR, Zhang C, Panning B, Shokat KM, Lavail MM, Walter P: IRE1 signaling affects cell fate during the unfolded protein response. Science. 2007, 318: 944-949. 10.1126/science.1146361.CrossRefPubMedPubMedCentral

48.

Mahal SP, Asante EA, Antoniou M, Collinge J: Isolation and functional characterisation of the promoter region of the human prion protein gene. Gene. 2001, 268: 105-114. 10.1016/S0378-1119(01)00424-3.CrossRefPubMed

49.

Wang Y, Shen J, Arenzana N, Tirasophon W, Kaufman RJ, Prywes R: Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. J Biol Chem. 2000, 275: 27013-27020.PubMed

50.

Bommiasamy H, Back SH, Fagone P, Lee K, Meshinchi S, Vink E, Sriburi R, Frank M, Jackowski S, Kaufman RJ, Brewer JW: ATF6alpha induces XBP1-independent expansion of the endoplasmic reticulum. J Cell Sci. 2009, 122: 1626-1636. 10.1242/jcs.045625.CrossRefPubMedPubMedCentral

51.

Kouskouti A, Scheer E, Staub A, Tora L, Talianidis I: Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol Cell. 2004, 14: 175-182. 10.1016/S1097-2765(04)00182-0.CrossRefPubMed

52.

van de Vijver MJ, He YD, van't Veer LJ, Dai H, Hart AA, Voskuil DW, Schreiber GJ, Peterse JL, Roberts C, Marton MJ, Parrish M, Atsma D, Witteveen A, Glas A, Delahaye L, van der Velde T, Bartelink H, Rodenhuis S, Rutgers ET, Friend SH, Bernards R: A gene-expression signature as a predictor of survival in breast cancer. N Engl J Med. 2002, 347: 1999-2009. 10.1056/NEJMoa021967.CrossRefPubMed

53.

Minn AJ, Gupta GP, Siegel PM, Bos PD, Shu W, Giri DD, Viale A, Olshen AB, Gerald WL, Massague J: Genes that mediate breast cancer metastasis to lung. Nature. 2005, 436: 518-524. 10.1038/nature03799.CrossRefPubMedPubMedCentral

54.

Chin K, DeVries S, Fridlyand J, Spellman PT, Roydasgupta R, Kuo WL, Lapuk A, Neve RM, Qian Z, Ryder T, Chen F, Feiler H, Tokuyasu T, Kingsley C, Dairkee S, Meng Z, Chew K, Pinkel D, Jain A, Ljung BM, Esserman L, Albertson DG, Waldman FM, Gray JW: Genomic and transcriptional aberrations linked to breast cancer pathophysiologies. Cancer Cell. 2006, 10: 529-541. 10.1016/j.ccr.2006.10.009.CrossRefPubMed

55.

Neve RM, Chin K, Fridlyand J, Yeh J, Baehner FL, Fevr T, Clark L, Bayani N, Coppe JP, Tong F, Speed T, Spellman PT, DeVries S, Lapuk A, Wang NJ, Kuo WL, Stilwell JL, Pinkel D, Albertson DG, Waldman FM, McCormick F, Dickson RB, Johnson MD, Lippman M, Ethier S, Gazdar A, Gray JW: A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes. Cancer Cell. 2006, 10: 515-527. 10.1016/j.ccr.2006.10.008.CrossRefPubMedPubMedCentral

56.

Kubota K, Niinuma Y, Kaneko M, Okuma Y, Sugai M, Omura T, Uesugi M, Uehara T, Hosoi T, Nomura Y: Suppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stress. J Neurochem. 2006, 97: 1259-1268. 10.1111/j.1471-4159.2006.03782.x.CrossRefPubMed

57.

Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M, Mori K: ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol. 2000, 20: 6755-6767. 10.1128/MCB.20.18.6755-6767.2000.CrossRefPubMedPubMedCentral

58.

Bi M, Naczki C, Koritzinsky M, Fels D, Blais J, Hu N, Harding H, Novoa I, Varia M, Raleigh J, Scheuner D, Kaufman RJ, Bell J, Ron D, Wouters BG, Koumenis C: ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth. EMBO J. 2005, 24: 3470-3481. 10.1038/sj.emboj.7600777.CrossRefPubMedPubMedCentral

59.

Kazemi S, Mounir Z, Baltzis D, Raven JF, Wang S, Krishnamoorthy JL, Pluquet O, Pelletier J, Koromilas AE: A novel function of eIF2alpha kinases as inducers of the phosphoinositide-3 kinase signaling pathway. Mol Biol Cell. 2007, 18: 3635-3644. 10.1091/mbc.E07-01-0053.CrossRefPubMedPubMedCentral

60.

Puthalakath H, O'Reilly LA, Gunn P, Lee L, Kelly PN, Huntington ND, Hughes PD, Michalak EM, McKimm-Breschkin J, Motoyama N, Gotoh T, Akira S, Bouillet P, Strasser A: ER stress triggers apoptosis by activating BH3-only protein Bim. Cell. 2007, 129: 1337-1349. 10.1016/j.cell.2007.04.027.CrossRefPubMed

61.

Basler K, Oesch B, Scott M, Westaway D, Walchli M, Groth DF, McKinley MP, Prusiner SB, Weissmann C: Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell. 1986, 46: 417-428. 10.1016/0092-8674(86)90662-8.CrossRefPubMed

62.

Funke-Kaiser H, Theis S, Behrouzi T, Thomas A, Scheuch K, Zollmann FS, Paterka M, Paul M, Orzechowski HD: Functional characterization of the human prion protein promoter in neuronal and endothelial cells. J Mol Med. 2001, 79: 529-535. 10.1007/s001090100270.CrossRefPubMed

63.

Puckett C, Concannon P, Casey C, Hood L: Genomic structure of the human prion protein gene. Am J Hum Genet. 1991, 49: 320-329.PubMedPubMedCentral

64.

Bellingham SA, Coleman LA, Masters CL, Camakaris J, Hill AF: Regulation of prion gene expression by transcription factors SP1 and metal transcription factor-1. J Biol Chem. 2009, 284: 1291-1301.CrossRefPubMed

65.

Qin K, Zhao L, Ash RD, McDonough WF, Zhao RY: ATM-mediated transcriptional elevation of prion in response to copper-induced oxidative stress. J Biol Chem. 2009, 284: 4582-4593.CrossRefPubMed

66.

Vincent B, Sunyach C, Orzechowski HD, St George-Hyslop P, Checler F: p53-Dependent transcriptional control of cellular prion by presenilins. J Neurosci. 2009, 29: 6752-6760. 10.1523/JNEUROSCI.0789-09.2009.CrossRefPubMed

67.

Westaway D, Cooper C, Turner S, Da Costa M, Carlson GA, Prusiner SB: Structure and polymorphism of the mouse prion protein gene. Proc Natl Acad Sci USA. 1994, 91: 6418-6422. 10.1073/pnas.91.14.6418.CrossRefPubMedPubMedCentral

68.

Davies MP, Barraclough DL, Stewart C, Joyce KA, Eccles RM, Barraclough R, Rudland PS, Sibson DR: Expression and splicing of the unfolded protein response gene XBP-1 are significantly associated with clinical outcome of endocrine-treated breast cancer. Int J Cancer. 2008, 123: 85-88. 10.1002/ijc.23479.CrossRefPubMed

69.

Mehrpour M, Codogno P: Prion protein: from physiology to cancer biology. Cancer Lett. 2010, 290: 1-23. 10.1016/j.canlet.2009.07.009.CrossRefPubMed

70.

Hetz C, Castilla J, Soto C: Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. J Biol Chem. 2007, 282: 12725-12733. 10.1074/jbc.M611909200.CrossRefPubMedPubMedCentral

71.

Orsi A, Fioriti L, Chiesa R, Sitia R: Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. J Biol Chem. 2006, 281: 30431-30438. 10.1074/jbc.M605320200.CrossRefPubMed

72.

Rane NS, Kang SW, Chakrabarti O, Feigenbaum L, Hegde RS: Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration. Dev Cell. 2008, 15: 359-370. 10.1016/j.devcel.2008.06.015.CrossRefPubMedPubMedCentral

73.

Zhou H, Zhang Y, Fu Y, Chan L, Lee AS: Novel mechanism of anti-apoptotic function of 78-kDa glucose-regulated protein (GRP78): endocrine resistance factor in breast cancer, through release of B-cell lymphoma 2 (BCL-2) from BCL-2-interacting killer (BIK). J Biol Chem. 2011, 286: 25687-25696. 10.1074/jbc.M110.212944.CrossRefPubMedPubMedCentral

74.

Cook KL, Shajahan AN, Warri A, Jin L, Hilakivi-Clarke LA, Clarke R: Glucose-regulated protein 78 controls cross-talk between apoptosis and autophagy to determine antiestrogen responsiveness. Cancer Res. 2012, 72: 3337-3349. 10.1158/0008-5472.CAN-12-0269.CrossRefPubMedPubMedCentral

75.

Grkovic S, O'Reilly VC, Han S, Hong M, Baxter RC, Firth SM: IGFBP-3 binds GRP78, stimulates autophagy and promotes the survival of breast cancer cells exposed to adverse microenvironments. Oncogene. 2012

76.

Li C, Harada A, Oh Y: IGFBP-3 sensitizes antiestrogen-resistant breast cancer cells through interaction with GRP78. Cancer Lett. 2012, 325: 200-206. 10.1016/j.canlet.2012.07.004.CrossRefPubMed

Title: Endoplasmic reticulum stress induces PRNP prion protein gene expression in breast cancer
Authors: Marc-André Déry
Julie Jodoin
Josie Ursini-Siegel
Olga Aleynikova
Cristiano Ferrario
Saima Hassan
Mark Basik
Andréa C LeBlanc
Publication date: 01-04-2013
Publisher: BioMed Central
Published in: Breast Cancer Research / Issue 2/2013
Electronic ISSN: 1465-542X
DOI: https://doi.org/10.1186/bcr3398

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