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W1974557118 abstract "Store-operated calcium entry (SOCE) is a key evolutionarily conserved process whereby decreases in endoplasmic reticulum Ca2+ content lead to the influx of Ca2+ across the plasma membrane. How this process is regulated in specific tumor cell types is poorly understood. In an effort to address this concern, we obtained and tested primary Wilms tumor cells, finding no detectable SOCE in this cell type. Analysis of the expression levels of STIM1 and ORAI1 (the molecular mediators of SOC) revealed poor STIM1 expression. Analysis of the STIM1 promoter using the TESS search system (University of Pennsylvania) revealed four putative response elements to the zinc-finger proteins WT1 (Wilms tumor suppressor 1) and EGR1 (early growth response 1). Either overexpression of WT1 or knockdown of EGR1 resulted in loss of STIM1 expression and a resultant decrease in SOCE. Furthermore, examination of Egr1 knock-out animals revealed loss of STIM1 expression in multiple tissues. Finally, using chromatin immunoprecipitation, we reveal direct binding of both WT1 and EGR1 to putative response elements located within 500 bp of the transcriptional start site of STIM1. Considering that WT1 and EGR1 are well described oncogenes and tumor suppressors, these observations may reveal new mechanisms responsible for distinct Ca2+ signals in cancer cells. Store-operated calcium entry (SOCE) is a key evolutionarily conserved process whereby decreases in endoplasmic reticulum Ca2+ content lead to the influx of Ca2+ across the plasma membrane. How this process is regulated in specific tumor cell types is poorly understood. In an effort to address this concern, we obtained and tested primary Wilms tumor cells, finding no detectable SOCE in this cell type. Analysis of the expression levels of STIM1 and ORAI1 (the molecular mediators of SOC) revealed poor STIM1 expression. Analysis of the STIM1 promoter using the TESS search system (University of Pennsylvania) revealed four putative response elements to the zinc-finger proteins WT1 (Wilms tumor suppressor 1) and EGR1 (early growth response 1). Either overexpression of WT1 or knockdown of EGR1 resulted in loss of STIM1 expression and a resultant decrease in SOCE. Furthermore, examination of Egr1 knock-out animals revealed loss of STIM1 expression in multiple tissues. Finally, using chromatin immunoprecipitation, we reveal direct binding of both WT1 and EGR1 to putative response elements located within 500 bp of the transcriptional start site of STIM1. Considering that WT1 and EGR1 are well described oncogenes and tumor suppressors, these observations may reveal new mechanisms responsible for distinct Ca2+ signals in cancer cells. IntroductionChanges in cytosolic Ca2+ levels are a common component of the signal transduction pathways for numerous growth factors and cytokines. Thus, activation of phospholipase C-coupled receptors (primarily via either G protein or tyrosine kinase receptors) results in the generation of the second messenger inositol 1,4,5-trisphosphate (1.Berridge M.J. Bootman M.D. Roderick H.L. Nat. Rev. Mol. Cell Biol. 2003; 4: 517-529Crossref PubMed Scopus (4116) Google Scholar). Inositol 1,4,5-trisphosphate diffuses rapidly through the cytosol and interacts with its receptor on the endoplasmic reticulum (ER), 2The abbreviations used are: ERendoplasmic reticulumREresponse elementSOCEstore-operated Ca2+ entryChIPchromatin immunoprecipitationsiRNAsmall interfering RNA. resulting in both transient ER Ca2+ release and a lengthy increased influx of Ca2+ across the plasma membrane, a process termed capacitative or store-operated Ca2+ entry (SOCE) (2.Venkatachalam K. van Rossum D.B. Patterson R.L. Ma H.T. Gill D.L. Nat. Cell Biol. 2002; 4: E263-E272Crossref PubMed Scopus (335) Google Scholar). SOCE has been shown to regulate numerous fundamental processes in cell biology, including migration (3.Yang S. Zhang J.J. Huang X.Y. Cancer Cell. 2009; 15: 124-134Abstract Full Text Full Text PDF PubMed Scopus (510) Google Scholar, 4.Potier M. Gonzalez J.C. Motiani R.K. Abdullaev I.F. Bisaillon J.M. Singer H.A. Trebak M. FASEB J. 2009; 23: 2425-2437Crossref PubMed Scopus (237) Google Scholar), proliferation (4.Potier M. Gonzalez J.C. Motiani R.K. Abdullaev I.F. Bisaillon J.M. Singer H.A. Trebak M. FASEB J. 2009; 23: 2425-2437Crossref PubMed Scopus (237) Google Scholar, 5.Abdullaev I.F. Bisaillon J.M. Potier M. Gonzalez J.C. Motiani R.K. Trebak M. Circ. Res. 2008; 103: 1289-1299Crossref PubMed Scopus (313) Google Scholar, 6.El Boustany C. Bidaux G. Enfissi A. Delcourt P. Prevarskaya N. Capiod T. Hepatology. 2008; 47: 2068-2077Crossref PubMed Scopus (178) Google Scholar), and differentiation (7.Darbellay B. Arnaudeau S. König S. Jousset H. Bader C. Demaurex N. Bernheim L. J. Biol. Chem. 2009; 284: 5370-5380Abstract Full Text Full Text PDF PubMed Scopus (116) Google Scholar, 8.Gwack Y. Srikanth S. Oh-Hora M. Hogan P.G. Lamperti E.D. Yamashita M. Gelinas C. Neems D.S. Sasaki Y. Feske S. Prakriya M. Rajewsky K. Rao A. Mol. Cell. Biol. 2008; 28: 5209-5222Crossref PubMed Scopus (246) Google Scholar). Given the impact of these pathways on cancer cell biology, it is not surprising that altered Ca2+ signaling can be observed in numerous classes of cancer cells. Indeed, inhibition of either the phosphatidylinositol pathway (9.Powis G. Gallegos A. Abraham R.T. Ashendel C.L. Zalkow L.H. Grindey G.B. Bonjouklian R. Cancer Chemother. Pharmacol. 1994; 34: 344-350Crossref PubMed Scopus (15) Google Scholar) or calcium influx (10.Cole K. Kohn E. Cancer Metastasis Rev. 1994; 13: 31-44Crossref PubMed Scopus (89) Google Scholar, 11.Soboloff J. Zhang Y. Minden M. Berger S.A. Exp. Hematol. 2002; 30: 1219-1226Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar) can induce either growth arrest or cell death in a variety of tumor cells. Despite these observations, Ca2+ signals remain poorly utilized therapeutic targets. This is in part because these studies were all performed prior to the discovery of the identities of the molecular mediators of SOCE. Without this insight, it was not possible to link changes in Ca2+ signals with changes in the expression and function of oncogenes and tumor suppressors that cause tumor formation.After nearly 20 years of investigations into the mysteries of SOCE, the identities of the key molecular components of this process have finally been revealed (for recent reviews, see Refs. 12.Deng X. Wang Y. Zhou Y. Soboloff J. Gill D.L. J. Biol. Chem. 2009; 284: 22501-22505Abstract Full Text Full Text PDF PubMed Scopus (100) Google Scholar and 13.Luik R.M. Lewis R.S. Trends Mol. Med. 2007; 13: 103-107Abstract Full Text Full Text PDF PubMed Scopus (52) Google Scholar). Thus, the type 1A transmembrane protein STIM1 serves a dual role as an ER Ca2+ sensor and activator of SOCE (14.Liou J. Kim M.L. Heo W.D. Jones J.T. Myers J.W. Ferrell Jr., J.E. Meyer T. Curr. Biol. 2005; 15: 1235-1241Abstract Full Text Full Text PDF PubMed Scopus (1726) Google Scholar, 15.Roos J. DiGregorio P.J. Yeromin A.V. Ohlsen K. Lioudyno M. Zhang S. Safrina O. Kozak J.A. Wagner S.L. Cahalan M.D. Veliçelebi G. Stauderman K.A. J. Cell Biol. 2005; 169: 435-445Crossref PubMed Scopus (1497) Google Scholar), whereas the plasma membrane-localized transmembrane protein ORAI1 is the store-operated Ca2+ channel (16.Feske S. Gwack Y. Prakriya M. Srikanth S. Puppel S.H. Tanasa B. Hogan P.G. Lewis R.S. Daly M. Rao A. Nature. 2006; 441: 179-185Crossref PubMed Scopus (1824) Google Scholar, 17.Vig M. Peinelt C. Beck A. Koomoa D.L. Rabah D. Koblan-Huberson M. Kraft S. Turner H. Fleig A. Penner R. Kinet J.P. Science. 2006; 312: 1220-1223Crossref PubMed Scopus (1138) Google Scholar, 18.Zhang S.L. Yeromin A.V. Zhang X.H. Yu Y. Safrina O. Penna A. Roos J. Stauderman K.A. Cahalan M.D. Proc. Natl. Acad. Sci. U.S.A. 2006; 103: 9357-9362Crossref PubMed Scopus (736) Google Scholar). Both of these proteins have mammalian homologues (STIM2, ORAI2, and ORAI3) that do not appear to be required for SOCE (4.Potier M. Gonzalez J.C. Motiani R.K. Abdullaev I.F. Bisaillon J.M. Singer H.A. Trebak M. FASEB J. 2009; 23: 2425-2437Crossref PubMed Scopus (237) Google Scholar, 15.Roos J. DiGregorio P.J. Yeromin A.V. Ohlsen K. Lioudyno M. Zhang S. Safrina O. Kozak J.A. Wagner S.L. Cahalan M.D. Veliçelebi G. Stauderman K.A. J. Cell Biol. 2005; 169: 435-445Crossref PubMed Scopus (1497) Google Scholar, 19.Bird G.S. Hwang S.Y. Smyth J.T. Fukushima M. Boyles R.R. Putney J.W. Curr. Biol. 2009; 19: 1-6PubMed Google Scholar, 20.Soboloff J. Spassova M.A. Hewavitharana T. He L.P. Xu W. Johnstone L.S. Dziadek M.A. Gill D.L. Curr. Biol. 2006; 16: 1465-1470Abstract Full Text Full Text PDF PubMed Scopus (207) Google Scholar) and likely serve modulatory roles in related processes. Despite an exciting recent report that SOCE is a critical and required component of breast tumor cell migration and metastasis (3.Yang S. Zhang J.J. Huang X.Y. Cancer Cell. 2009; 15: 124-134Abstract Full Text Full Text PDF PubMed Scopus (510) Google Scholar), there remains no published insight into the regulation of SOCE components at the level of transcription or their relationship to tumorigenesis.In early investigations performed prior to the discovery of its role in Ca2+ signaling, STIM1 was described as a tumor suppressor because it causes growth arrest in human G401 rhabdoid tumor cells (21.Sabbioni S. Barbanti-Brodano G. Croce C.M. Negrini M. Cancer Res. 1997; 57: 4493-4497PubMed Google Scholar, 22.Sabbioni S. Veronese A. Trubia M. Taramelli R. Barbanti-Brodano G. Croce C.M. Negrini M. Cytogenet. Cell Genet. 1999; 86: 214-218Crossref PubMed Scopus (44) Google Scholar), a kidney-derived rhabdoid cell line often used to study chromosomal changes in Wilms tumor (23.Garvin A.J. Re G.G. Tarnowski B.I. Hazen-Martin D.J. Sens D.A. Am. J. Pathol. 1993; 142: 375-380PubMed Google Scholar) due to the fact that they lack expression of WT1 (Wilms tumor suppressor 1). WT1 is a zinc-finger transcription factor that regulates the expression of multiple growth factors such as colony-stimulating factor (24.Harrington M.A. Konicek B. Song A. Xia X.L. Fredericks W.J. Rauscher 3rd, F.J. J. Biol. Chem. 1993; 268: 21271-21275Abstract Full Text PDF PubMed Google Scholar), insulin-like growth factor I (25.Sarfstein R. Werner H. J. Neurochem. 2006; 99: 818-826Crossref PubMed Scopus (11) Google Scholar), and platelet-derived growth factor (26.Wang Z.Y. Madden S.L. Deuel T.F. Rauscher 3rd, F.J. J. Biol. Chem. 1992; 267: 21999-22002Abstract Full Text PDF PubMed Google Scholar). Thus, loss of WT1 leads to up-regulation of these growth factors and the formation of Wilms tumor, leading to its original classification as a tumor suppressor (27.Little M. Wells C. Hum. Mutat. 1997; 9: 209-225Crossref PubMed Scopus (324) Google Scholar). However, subsequent studies have revealed a potential role for WT1 as an oncogene because it is up-regulated in a variety of human cancers such as astrocytic tumors (28.Oji Y. Suzuki T. Nakano Y. Maruno M. Nakatsuka S. Jomgeow T. Abeno S. Tatsumi N. Yokota A. Aoyagi S. Nakazawa T. Ito K. Kanato K. Shirakata T. Nishida S. Hosen N. Kawakami M. Tsuboi A. Oka Y. Aozasa K. Yoshimine T. Sugiyama H. Cancer Sci. 2004; 95: 822-827Crossref PubMed Scopus (104) Google Scholar), breast cancer (29.Loeb D.M. Evron E. Patel C.B. Sharma P.M. Niranjan B. Buluwela L. Weitzman S.A. Korz D. Sukumar S. Cancer Res. 2001; 61: 921-925PubMed Google Scholar), leukemia (30.Miwa H. Beran M. Saunders G.F. Leukemia. 1992; 6: 405-409PubMed Google Scholar), and sporadic Wilms tumor (31.Grubb G.R. Yun K. Williams B.R. Eccles M.R. Reeve A.E. Lab. Invest. 1994; 71: 472-479PubMed Google Scholar, 32.Ghanem M.A. Van der Kwast T.H. Den Hollander J.C. Sudaryo M.K. Oomen M.H. Noordzij M.A. Van den Heuvel M.M. Nassef S.M. Nijman R.M. Van Steenbrugge G.J. Clin. Cancer Res. 2000; 6: 4265-4271PubMed Google Scholar), which accounts for ∼85% of all Wilms tumors. WT1 is a member of the EGR (early growth response) family, primarily due to similarities in the consensus sequences of WT1 and EGR1. However, the consequences of binding are most often mutually opposing; EGR1 activates the transcription of genes that WT1 represses (33.Sukhatme V.P. Cao X. Chang L.C. Tsai-Morris C.H. Stamenkovich D. Ferreira P.C. Cohen D.R. Edwards S.A. Shows T.B. Curran T. Le Beau M.M. Adamson E.D. Cell. 1988; 53: 37-43Abstract Full Text PDF PubMed Scopus (1019) Google Scholar, 34.Dey B.R. Sukhatme V.P. Roberts A.B. Sporn M.B. Rauscher 3rd, F.J. Kim S.J. Mol. Endocrinol. 1994; 8: 595-602Crossref PubMed Scopus (194) Google Scholar). Like WT1, EGR1 expression levels are atypical in multiple neoplastic cell types such as prostate cancer (35.Baron V. De Gregorio G. Krones-Herzig A. Virolle T. Calogero A. Urcis R. Mercola D. Oncogene. 2003; 22: 4194-4204Crossref PubMed Scopus (99) Google Scholar), glioblastoma (36.Ahn B.H. Park M.H. Lee Y.H. Min do S. FEBS Lett. 2007; 581: 5940-5944Crossref PubMed Scopus (6) Google Scholar), and Wilms tumor (32.Ghanem M.A. Van der Kwast T.H. Den Hollander J.C. Sudaryo M.K. Oomen M.H. Noordzij M.A. Van den Heuvel M.M. Nassef S.M. Nijman R.M. Van Steenbrugge G.J. Clin. Cancer Res. 2000; 6: 4265-4271PubMed Google Scholar). Furthermore, EGR1 can also act as either an oncogene (35.Baron V. De Gregorio G. Krones-Herzig A. Virolle T. Calogero A. Urcis R. Mercola D. Oncogene. 2003; 22: 4194-4204Crossref PubMed Scopus (99) Google Scholar) or a tumor suppressor (37.Krones-Herzig A. Mittal S. Yule K. Liang H. English C. Urcis R. Soni T. Adamson E.D. Mercola D. Cancer Res. 2005; 65: 5133-5143Crossref PubMed Scopus (120) Google Scholar) in different cell types. In this work, we reveal that STIM1 expression is directly regulated by EGR1 and WT1, with EGR1 driving STIM1 expression and WT1 antagonizing this effect. Given the well described impact of these oncogenes/tumor suppressors on tumorigenesis, these findings provide important new insight into differential Ca2+ signaling in cancer cells. IntroductionChanges in cytosolic Ca2+ levels are a common component of the signal transduction pathways for numerous growth factors and cytokines. Thus, activation of phospholipase C-coupled receptors (primarily via either G protein or tyrosine kinase receptors) results in the generation of the second messenger inositol 1,4,5-trisphosphate (1.Berridge M.J. Bootman M.D. Roderick H.L. Nat. Rev. Mol. Cell Biol. 2003; 4: 517-529Crossref PubMed Scopus (4116) Google Scholar). Inositol 1,4,5-trisphosphate diffuses rapidly through the cytosol and interacts with its receptor on the endoplasmic reticulum (ER), 2The abbreviations used are: ERendoplasmic reticulumREresponse elementSOCEstore-operated Ca2+ entryChIPchromatin immunoprecipitationsiRNAsmall interfering RNA. resulting in both transient ER Ca2+ release and a lengthy increased influx of Ca2+ across the plasma membrane, a process termed capacitative or store-operated Ca2+ entry (SOCE) (2.Venkatachalam K. van Rossum D.B. Patterson R.L. Ma H.T. Gill D.L. Nat. Cell Biol. 2002; 4: E263-E272Crossref PubMed Scopus (335) Google Scholar). SOCE has been shown to regulate numerous fundamental processes in cell biology, including migration (3.Yang S. Zhang J.J. Huang X.Y. Cancer Cell. 2009; 15: 124-134Abstract Full Text Full Text PDF PubMed Scopus (510) Google Scholar, 4.Potier M. Gonzalez J.C. Motiani R.K. Abdullaev I.F. Bisaillon J.M. Singer H.A. Trebak M. FASEB J. 2009; 23: 2425-2437Crossref PubMed Scopus (237) Google Scholar), proliferation (4.Potier M. Gonzalez J.C. Motiani R.K. Abdullaev I.F. Bisaillon J.M. Singer H.A. Trebak M. FASEB J. 2009; 23: 2425-2437Crossref PubMed Scopus (237) Google Scholar, 5.Abdullaev I.F. Bisaillon J.M. Potier M. Gonzalez J.C. Motiani R.K. Trebak M. Circ. Res. 2008; 103: 1289-1299Crossref PubMed Scopus (313) Google Scholar, 6.El Boustany C. Bidaux G. Enfissi A. Delcourt P. Prevarskaya N. Capiod T. Hepatology. 2008; 47: 2068-2077Crossref PubMed Scopus (178) Google Scholar), and differentiation (7.Darbellay B. Arnaudeau S. König S. Jousset H. Bader C. Demaurex N. Bernheim L. J. Biol. Chem. 2009; 284: 5370-5380Abstract Full Text Full Text PDF PubMed Scopus (116) Google Scholar, 8.Gwack Y. Srikanth S. Oh-Hora M. Hogan P.G. Lamperti E.D. Yamashita M. Gelinas C. Neems D.S. Sasaki Y. Feske S. Prakriya M. Rajewsky K. Rao A. Mol. Cell. Biol. 2008; 28: 5209-5222Crossref PubMed Scopus (246) Google Scholar). Given the impact of these pathways on cancer cell biology, it is not surprising that altered Ca2+ signaling can be observed in numerous classes of cancer cells. Indeed, inhibition of either the phosphatidylinositol pathway (9.Powis G. Gallegos A. Abraham R.T. Ashendel C.L. Zalkow L.H. Grindey G.B. Bonjouklian R. Cancer Chemother. Pharmacol. 1994; 34: 344-350Crossref PubMed Scopus (15) Google Scholar) or calcium influx (10.Cole K. Kohn E. Cancer Metastasis Rev. 1994; 13: 31-44Crossref PubMed Scopus (89) Google Scholar, 11.Soboloff J. Zhang Y. Minden M. Berger S.A. Exp. Hematol. 2002; 30: 1219-1226Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar) can induce either growth arrest or cell death in a variety of tumor cells. Despite these observations, Ca2+ signals remain poorly utilized therapeutic targets. This is in part because these studies were all performed prior to the discovery of the identities of the molecular mediators of SOCE. Without this insight, it was not possible to link changes in Ca2+ signals with changes in the expression and function of oncogenes and tumor suppressors that cause tumor formation.After nearly 20 years of investigations into the mysteries of SOCE, the identities of the key molecular components of this process have finally been revealed (for recent reviews, see Refs. 12.Deng X. Wang Y. Zhou Y. Soboloff J. Gill D.L. J. Biol. Chem. 2009; 284: 22501-22505Abstract Full Text Full Text PDF PubMed Scopus (100) Google Scholar and 13.Luik R.M. Lewis R.S. Trends Mol. Med. 2007; 13: 103-107Abstract Full Text Full Text PDF PubMed Scopus (52) Google Scholar). Thus, the type 1A transmembrane protein STIM1 serves a dual role as an ER Ca2+ sensor and activator of SOCE (14.Liou J. Kim M.L. Heo W.D. Jones J.T. Myers J.W. Ferrell Jr., J.E. Meyer T. Curr. Biol. 2005; 15: 1235-1241Abstract Full Text Full Text PDF PubMed Scopus (1726) Google Scholar, 15.Roos J. DiGregorio P.J. Yeromin A.V. Ohlsen K. Lioudyno M. Zhang S. Safrina O. Kozak J.A. Wagner S.L. Cahalan M.D. Veliçelebi G. Stauderman K.A. J. Cell Biol. 2005; 169: 435-445Crossref PubMed Scopus (1497) Google Scholar), whereas the plasma membrane-localized transmembrane protein ORAI1 is the store-operated Ca2+ channel (16.Feske S. Gwack Y. Prakriya M. Srikanth S. Puppel S.H. Tanasa B. Hogan P.G. Lewis R.S. Daly M. Rao A. Nature. 2006; 441: 179-185Crossref PubMed Scopus (1824) Google Scholar, 17.Vig M. Peinelt C. Beck A. Koomoa D.L. Rabah D. Koblan-Huberson M. Kraft S. Turner H. Fleig A. Penner R. Kinet J.P. Science. 2006; 312: 1220-1223Crossref PubMed Scopus (1138) Google Scholar, 18.Zhang S.L. Yeromin A.V. Zhang X.H. Yu Y. Safrina O. Penna A. Roos J. Stauderman K.A. Cahalan M.D. Proc. Natl. Acad. Sci. U.S.A. 2006; 103: 9357-9362Crossref PubMed Scopus (736) Google Scholar). Both of these proteins have mammalian homologues (STIM2, ORAI2, and ORAI3) that do not appear to be required for SOCE (4.Potier M. Gonzalez J.C. Motiani R.K. Abdullaev I.F. Bisaillon J.M. Singer H.A. Trebak M. FASEB J. 2009; 23: 2425-2437Crossref PubMed Scopus (237) Google Scholar, 15.Roos J. DiGregorio P.J. Yeromin A.V. Ohlsen K. Lioudyno M. Zhang S. Safrina O. Kozak J.A. Wagner S.L. Cahalan M.D. Veliçelebi G. Stauderman K.A. J. Cell Biol. 2005; 169: 435-445Crossref PubMed Scopus (1497) Google Scholar, 19.Bird G.S. Hwang S.Y. Smyth J.T. Fukushima M. Boyles R.R. Putney J.W. Curr. Biol. 2009; 19: 1-6PubMed Google Scholar, 20.Soboloff J. Spassova M.A. Hewavitharana T. He L.P. Xu W. Johnstone L.S. Dziadek M.A. Gill D.L. Curr. Biol. 2006; 16: 1465-1470Abstract Full Text Full Text PDF PubMed Scopus (207) Google Scholar) and likely serve modulatory roles in related processes. Despite an exciting recent report that SOCE is a critical and required component of breast tumor cell migration and metastasis (3.Yang S. Zhang J.J. Huang X.Y. Cancer Cell. 2009; 15: 124-134Abstract Full Text Full Text PDF PubMed Scopus (510) Google Scholar), there remains no published insight into the regulation of SOCE components at the level of transcription or their relationship to tumorigenesis.In early investigations performed prior to the discovery of its role in Ca2+ signaling, STIM1 was described as a tumor suppressor because it causes growth arrest in human G401 rhabdoid tumor cells (21.Sabbioni S. Barbanti-Brodano G. Croce C.M. Negrini M. Cancer Res. 1997; 57: 4493-4497PubMed Google Scholar, 22.Sabbioni S. Veronese A. Trubia M. Taramelli R. Barbanti-Brodano G. Croce C.M. Negrini M. Cytogenet. Cell Genet. 1999; 86: 214-218Crossref PubMed Scopus (44) Google Scholar), a kidney-derived rhabdoid cell line often used to study chromosomal changes in Wilms tumor (23.Garvin A.J. Re G.G. Tarnowski B.I. Hazen-Martin D.J. Sens D.A. Am. J. Pathol. 1993; 142: 375-380PubMed Google Scholar) due to the fact that they lack expression of WT1 (Wilms tumor suppressor 1). WT1 is a zinc-finger transcription factor that regulates the expression of multiple growth factors such as colony-stimulating factor (24.Harrington M.A. Konicek B. Song A. Xia X.L. Fredericks W.J. Rauscher 3rd, F.J. J. Biol. Chem. 1993; 268: 21271-21275Abstract Full Text PDF PubMed Google Scholar), insulin-like growth factor I (25.Sarfstein R. Werner H. J. Neurochem. 2006; 99: 818-826Crossref PubMed Scopus (11) Google Scholar), and platelet-derived growth factor (26.Wang Z.Y. Madden S.L. Deuel T.F. Rauscher 3rd, F.J. J. Biol. Chem. 1992; 267: 21999-22002Abstract Full Text PDF PubMed Google Scholar). Thus, loss of WT1 leads to up-regulation of these growth factors and the formation of Wilms tumor, leading to its original classification as a tumor suppressor (27.Little M. Wells C. Hum. Mutat. 1997; 9: 209-225Crossref PubMed Scopus (324) Google Scholar). However, subsequent studies have revealed a potential role for WT1 as an oncogene because it is up-regulated in a variety of human cancers such as astrocytic tumors (28.Oji Y. Suzuki T. Nakano Y. Maruno M. Nakatsuka S. Jomgeow T. Abeno S. Tatsumi N. Yokota A. Aoyagi S. Nakazawa T. Ito K. Kanato K. Shirakata T. Nishida S. Hosen N. Kawakami M. Tsuboi A. Oka Y. Aozasa K. Yoshimine T. Sugiyama H. Cancer Sci. 2004; 95: 822-827Crossref PubMed Scopus (104) Google Scholar), breast cancer (29.Loeb D.M. Evron E. Patel C.B. Sharma P.M. Niranjan B. Buluwela L. Weitzman S.A. Korz D. Sukumar S. Cancer Res. 2001; 61: 921-925PubMed Google Scholar), leukemia (30.Miwa H. Beran M. Saunders G.F. Leukemia. 1992; 6: 405-409PubMed Google Scholar), and sporadic Wilms tumor (31.Grubb G.R. Yun K. Williams B.R. Eccles M.R. Reeve A.E. Lab. Invest. 1994; 71: 472-479PubMed Google Scholar, 32.Ghanem M.A. Van der Kwast T.H. Den Hollander J.C. Sudaryo M.K. Oomen M.H. Noordzij M.A. Van den Heuvel M.M. Nassef S.M. Nijman R.M. Van Steenbrugge G.J. Clin. Cancer Res. 2000; 6: 4265-4271PubMed Google Scholar), which accounts for ∼85% of all Wilms tumors. WT1 is a member of the EGR (early growth response) family, primarily due to similarities in the consensus sequences of WT1 and EGR1. However, the consequences of binding are most often mutually opposing; EGR1 activates the transcription of genes that WT1 represses (33.Sukhatme V.P. Cao X. Chang L.C. Tsai-Morris C.H. Stamenkovich D. Ferreira P.C. Cohen D.R. Edwards S.A. Shows T.B. Curran T. Le Beau M.M. Adamson E.D. Cell. 1988; 53: 37-43Abstract Full Text PDF PubMed Scopus (1019) Google Scholar, 34.Dey B.R. Sukhatme V.P. Roberts A.B. Sporn M.B. Rauscher 3rd, F.J. Kim S.J. Mol. Endocrinol. 1994; 8: 595-602Crossref PubMed Scopus (194) Google Scholar). Like WT1, EGR1 expression levels are atypical in multiple neoplastic cell types such as prostate cancer (35.Baron V. De Gregorio G. Krones-Herzig A. Virolle T. Calogero A. Urcis R. Mercola D. Oncogene. 2003; 22: 4194-4204Crossref PubMed Scopus (99) Google Scholar), glioblastoma (36.Ahn B.H. Park M.H. Lee Y.H. Min do S. FEBS Lett. 2007; 581: 5940-5944Crossref PubMed Scopus (6) Google Scholar), and Wilms tumor (32.Ghanem M.A. Van der Kwast T.H. Den Hollander J.C. Sudaryo M.K. Oomen M.H. Noordzij M.A. Van den Heuvel M.M. Nassef S.M. Nijman R.M. Van Steenbrugge G.J. Clin. Cancer Res. 2000; 6: 4265-4271PubMed Google Scholar). Furthermore, EGR1 can also act as either an oncogene (35.Baron V. De Gregorio G. Krones-Herzig A. Virolle T. Calogero A. Urcis R. Mercola D. Oncogene. 2003; 22: 4194-4204Crossref PubMed Scopus (99) Google Scholar) or a tumor suppressor (37.Krones-Herzig A. Mittal S. Yule K. Liang H. English C. Urcis R. Soni T. Adamson E.D. Mercola D. Cancer Res. 2005; 65: 5133-5143Crossref PubMed Scopus (120) Google Scholar) in different cell types. In this work, we reveal that STIM1 expression is directly regulated by EGR1 and WT1, with EGR1 driving STIM1 expression and WT1 antagonizing this effect. Given the well described impact of these oncogenes/tumor suppressors on tumorigenesis, these findings provide important new insight into differential Ca2+ signaling in cancer cells." @default.
W1974557118 created "2016-06-24" @default.
W1974557118 creator A5027391949 @default.
W1974557118 creator A5030342211 @default.
W1974557118 creator A5043149943 @default.
W1974557118 creator A5073277560 @default.
W1974557118 creator A5076785173 @default.
W1974557118 date "2010-04-01" @default.
W1974557118 modified "2023-10-07" @default.
W1974557118 title "Wilms Tumor Suppressor 1 (WT1) and Early Growth Response 1 (EGR1) Are Regulators of STIM1 Expression" @default.
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W1974557118 doi "https://doi.org/10.1074/jbc.m109.083493" @default.
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