MUC1 cytoplasmic tail: a potential therapeutic target for ovarian carcinoma

References

• Agarwal R, Kaye SB. Ovarian cancer: strategies for overcoming resistance to chemotherapy. Nat. Rev. Cancer3, 502–516 (2003).
   PubMed Web of Science ®Google Scholar
• Fleming JS, Beaugie CR, Haviv I, Chenevix-Trench G, Tan OL. Incessant ovulation, inflammation and epithelial ovarian carcinogenesis: revisiting old hypotheses. Mol. Cell Endocrinol.247, 4–21 (2006).
   PubMed Web of Science ®Google Scholar
• Naora H, Montell DJ. Ovarian cancer metastasis: integrating insights from disparate model organisms. Nat. Rev. Cancer5, 355–366 (2005).
   PubMed Web of Science ®Google Scholar
• Hinoda Y, Sasaki S, Ishida T, Imai K. Monoclonal antibodies as effective therapeutic agents for solid tumors. Cancer Sci.95, 621–625 (2004).
   PubMed Web of Science ®Google Scholar
• Cragg MS, French RR, Glennie MJ. Signaling antibodies in cancer therapy. Curr. Opin. Immunol.11, 541–547 (1999).
   PubMed Web of Science ®Google Scholar
• Normanno N, Bianco C, De Luca A, Maiello MR, Salomon DS. Target-based agents against ErbB receptors and their ligands: a novel approach to cancer treatment. Endocr. Rel. Cancer10, 1–21 (2003).
   PubMed Web of Science ®Google Scholar
• Amant F, Vloeberghs V, Woestenborghs H, Moerman P, Vergote I. Transition of epithelial toward mesenchymal differentiation during ovarian carcinosarcoma tumorigenesis. Gynecol. Oncol.90, 372–377 (2003).
   PubMed Web of Science ®Google Scholar
• Sherbet GV, Patil D. Genetic abnormalities of cell proliferation, invasion and metastasis, with special reference to gynaecological cancers. Anticancer Res.23, 1357–1371 (2003).
   PubMed Web of Science ®Google Scholar
• Hollingsworth MA, Swanson BJ. Mucins in cancer: protection and control of the cell surface. Nat. Rev. Cancer4, 45–60 (2004).
   PubMed Web of Science ®Google Scholar
• Lan MS, Batra SK, Qi WN, Metzgar RS, Hollingsworth MA. Cloning and sequencing of a human pancreatic tumor mucin cDNA. J. Biol. Chem.265, 15294–15299 (1990).
   PubMed Web of Science ®Google Scholar
• Wreschner DH, Hareuveni M, Tsarfaty I et al. Human epithelial tumor antigen cDNA sequences. Differential splicing may generate multiple protein forms. Eur. J. Biochem.189, 463–473 (1990).
   PubMedGoogle Scholar
• Hu XF, Xing PX. Discovery and validation of new molecular targets for ovarian cancer. Curr. Opin. Mol. Ther.5, 625–630 (2003).
   PubMedGoogle Scholar
• Acres B, Limacher JM. MUC1 as a target antigen for cancer immunotherapy. Expert Rev. Vaccines4, 493–502 (2005).
   PubMed Web of Science ®Google Scholar
• Rahbarizadeh F, Rasaee MJ, Forouzandeh M et al. The production and characterization of novel heavy-chain antibodies against the tandem repeat region of MUC1 mucin. Immunol. Invest.34, 431–452 (2005).
   PubMed Web of Science ®Google Scholar
• Xing PX. Technology evaluation: R-1549, Antisoma/Roche. Curr. Opin. Mol. Ther.5, 560–565 (2003).
   PubMedGoogle Scholar
• Spicer AP, Duhig T, Chilton BS, Gendler SJ. Analysis of mammalian MUC1 genes reveals potential functionally important domains. Mamm. Genome6, 885–888 (1995).
   PubMed Web of Science ®Google Scholar
• Pemberton LF, Rughetti A, Taylor-Papadimitriou J, Gendler SJ. The epithelial mucin MUC1 contains at least two discrete signals specifying membrane localization in cells. J. Biol. Chem.271, 2332–2340 (1996).
   PubMed Web of Science ®Google Scholar
• Hanisch FG, Stadie TR, Deutzmann F, Peter-Katalinic J. MUC1 glycoforms in breast cancer–cell line T47D as a model for carcinoma-associated alterations of 0-glycosylation. Eur. J. Biochem.236, 318–327 (1996).
   PubMedGoogle Scholar
• Li Y, Liu D, Chen D, Kharbanda S, Kufe D. Human DF3/MUC1 carcinoma-associated protein functions as an oncogene. Oncogene22, 6107–6110 (2003).
   PubMed Web of Science ®Google Scholar
• Schroeder JA, Masri AA, Adriance MC et al. MUC1 overexpression results in mammary gland tumorigenesis and prolonged alveolar differentiation. Oncogene23, 5739–5747 (2004).
   PubMed Web of Science ®Google Scholar
• Li Q, Ren J, Kufe D. Interaction of human MUC1 and β-catenin is regulated by Lck and ZAP-70 in activated Jurkat T cells. Biochem. Biophys. Res. Commun.315, 471–476 (2004).
   PubMed Web of Science ®Google Scholar
• Wykes M, MacDonald KP, Tran M et al. MUC1 epithelial mucin (CD227) is expressed by activated dendritic cells. J. Leukocyte Biol.72, 692–701 (2002).
   PubMed Web of Science ®Google Scholar
• Xing PX, Lees C, Lodding J et al. Mouse mucin 1 (MUC1) defined by monoclonal antibodies. Int. J. Cancer76, 875–883 (1998).
   PubMed Web of Science ®Google Scholar
• Rahn JJ, Dabbagh L, Pasdar M, Hugh JC. The importance of MUC1 cellular localization in patients with breast carcinoma: an immunohistologic study of 71 patients and review of the literature. Cancer91, 1973–1982 (2001).
   PubMed Web of Science ®Google Scholar
• Ichige K, Perey L, Vogel CA, Buchegger F, Kufe D. Expression of the DF3-P epitope in human ovarian carcinomas. Clin. Cancer Res.1, 565–571 (1995).
   PubMed Web of Science ®Google Scholar
• Xing PX, Prenzoska J, McKenzie IF. Epitope mapping of anti-breast and anti-ovarian mucin monoclonal antibodies. Mol. Immunol.29, 641–650 (1992).
   PubMed Web of Science ®Google Scholar
• Dong Y, Walsh MD, Cummings MC et al. Expression of MUC1 and MUC2 mucins in epithelial ovarian tumours. J. Pathol.183, 311–317 (1997).
   PubMed Web of Science ®Google Scholar
• Feng H, Ghazizadeh M, Konishi H, Araki T. Expression of MUC1 and MUC2 mucin gene products in human ovarian carcinomas. Jpn J. Clin. Oncol.32, 525–529 (2002).
   PubMed Web of Science ®Google Scholar
• Croce MV, Isla-Larrain M, Remes-Lenicov F et al. MUC1 cytoplasmic tail detection using CT33 polyclonal and CT2 monoclonal antibodies in breast and colorectal tissue. Histol. Histopathol.21, 849–855 (2006).
   PubMed Web of Science ®Google Scholar
• Yamashita K, Yonezawa S, Tanaka S et al. Immunohistochemical study of mucin carbohydrates and core proteins in hepatolithiasis and cholangiocarcinoma. Int. J. Cancer55, 82–91 (1993).
   PubMed Web of Science ®Google Scholar
• Tsutsumida H, Swanson BJ, Singh PK et al. RNA interference suppression of MUC1 reduces the growth rate and metastatic phenotype of human pancreatic cancer cells. Clin. Cancer Res.12, 2976–2987 (2006).
   PubMed Web of Science ®Google Scholar
• Ligtenberg MJ, Buijs F, Vos HL, Hilkens J. Suppression of cellular aggregation by high levels of episialin. Cancer Res.52, 2318–2324 (1992).
   PubMed Web of Science ®Google Scholar
• Jamora C, Fuchs E. Intercellular adhesion, signalling and the cytoskeleton. Nat. Cell Biol.4, E101–E108 (2002).
   PubMed Web of Science ®Google Scholar
• Yamada S, Pokutta S, Drees F, Weis WI, Nelson WJ. Deconstructing the cadherin–catenin–actin complex. Cell123, 889–901 (2005).
   PubMed Web of Science ®Google Scholar
• Takeichi M. Cadherins: a molecular family important in selective cell–cell adhesion. Annu. Rev. Biochem.59, 237–252 (1990).
   PubMed Web of Science ®Google Scholar
• Li Y, Bharti A, Chen D, Gong J, Kufe D. Interaction of glycogen synthase kinase 3β with the DF3/MUC1 carcinoma-associated antigen and β-catenin. Mol. Cell Biol.18, 7216–7224 (1998).
   PubMed Web of Science ®Google Scholar
• Sastry SK, Burridge K. Focal adhesions: a nexus for intracellular signaling and cytoskeletal dynamics. Exp. Cell Res.261, 25–36 (2000).
   PubMed Web of Science ®Google Scholar
• Wesseling J, van der Valk SW, Hilkens J. A mechanism for inhibition of E-cadherin-mediated cell–cell adhesion by the membrane-associated mucin episialin/MUC1. Mol. Biol. Cell7, 565–577 (1996).
   PubMed Web of Science ®Google Scholar
• Wesseling J, van der Valk SW, Vos HL, Sonnenberg A, Hilkens J. Episialin (MUC1) overexpression inhibits integrin-mediated cell adhesion to extracellular matrix components. J. Cell Biol.129, 255–265 (1995).
   PubMed Web of Science ®Google Scholar
• McDermott KM, Crocker PR, Harris A et al. Overexpression of MUC1 reconfigures the binding properties of tumor cells. Int. J. Cancer94, 783–791 (2001).
   PubMed Web of Science ®Google Scholar
• Chang JH, Gill S, Settleman J, Parsons SJ. c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation. J. Cell Biol.130, 355–368 (1995).
   PubMed Web of Science ®Google Scholar
• Zou JX, Liu Y, Pasquale EB, Ruoslahti, E. Activated SRC oncogene phosphorylates R-ras and suppresses integrin activity. J. Biol. Chem.277, 1824–1827 (2002).
   PubMed Web of Science ®Google Scholar
• Kaplan KB, Bibbins KB, Swedlow JR, Arnaud M, Morgan DO, Varmus HE. Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. Embo. J.13, 4745–4756 (1994).
   PubMed Web of Science ®Google Scholar
• Zrihan-Licht S, Baruch A, Elroy-Stein O, Keydar I, Wreschner DH. Tyrosine phosphorylation of the MUC1 breast cancer membrane proteins. Cytokine receptor-like molecules. FEBS Lett.356, 130–136 (1994).
   PubMed Web of Science ®Google Scholar
• Schroeder JA, Thompson MC, Gardner MM, Gendler SJ. Transgenic MUC1 interacts with epidermal growth factor receptor and correlates with mitogen-activated protein kinase activation in the mouse mammary gland. J. Biol. Chem.276, 13057–13064 (2001).
   PubMed Web of Science ®Google Scholar
• Li Y, Kuwahara H, Ren J, Wen G, Kufe D. The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 β and β-catenin. J. Biol. Chem.276, 6061–6064 (2001).
   PubMed Web of Science ®Google Scholar
• Yamamoto M, Bharti A, Li Y, Kufe D. Interaction of the DF3/MUC1 breast carcinoma-associated antigen and β-catenin in cell adhesion. J. Biol. Chem.272, 12492–12494 (1997).
   PubMed Web of Science ®Google Scholar
• Su LK, Vogelstein B, Kinzler KW. Association of the APC tumor suppressor protein with catenins. Science262, 1734–1737 (1993).
   PubMed Web of Science ®Google Scholar
• Rubinfeld B, Albert I, Porfiri E, Fiol C, Munemitsu S, Polakis P. Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly. Science272, 1023–1026 (1996).
   PubMed Web of Science ®Google Scholar
• Jones RJ, Brunton VG, Frame MC. Adhesion-linked kinases in cancer; emphasis on src, focal adhesion kinase and PI 3-kinase. Eur. J. Cancer36, 1595–1606 (2000).
   PubMed Web of Science ®Google Scholar
• Yeatman TJ. A renaissance for SRC. Nat. Rev. Cancer4, 470–480 (2004).
   PubMed Web of Science ®Google Scholar
• Ren R, Mayer BJ, Cicchetti P, Baltimore D. Identification of a ten-amino acid proline-rich SH3 binding site. Science259, 1157–1161 (1993).
   PubMed Web of Science ®Google Scholar
• Li Y, Ren J, Yu W et al. The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and β-catenin. J. Biol. Chem.276, 35239–35242 (2001).
   PubMed Web of Science ®Google Scholar
• Ottenhoff-Kalff AE, Rijksen G, van Beurden EA, Hennipman A, Michels AA, Staal GE. Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product. Cancer Res.52, 4773–4778 (1992).
   PubMed Web of Science ®Google Scholar
• Wiener JR, Windham TC, Estrella VC et al. Activated SRC protein tyrosine kinase is overexpressed in late-stage human ovarian cancers. Gynecol. Oncol.88, 73–79 (2003).
   PubMed Web of Science ®Google Scholar
• Bjorge JD, Pang A, Fujita DJ. Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem.275, 41439–41446 (2000).
   PubMed Web of Science ®Google Scholar
• Pengetnze Y, Steed M, Roby KF, Terranova PF, Taylor CC. Src tyrosine kinase promotes survival and resistance to chemotherapeutics in a mouse ovarian cancer cell line. Biochem. Biophys. Res. Commun.309, 377–383 (2003).
   PubMed Web of Science ®Google Scholar
• Chen T, Pengetnze Y, Taylor CC. Src inhibition enhances paclitaxel cytotoxicity in ovarian cancer cells by caspase-9-independent activation of caspase-3. Mol. Cancer Ther.4, 217–224 (2005).
   PubMed Web of Science ®Google Scholar
• George JA, Chen T, Taylor CC. SRC tyrosine kinase and multidrug resistance protein-1 inhibitions act independently but cooperatively to restore paclitaxel sensitivity to paclitaxel-resistant ovarian cancer cells. Cancer Res.65, 10381–10388 (2005).
   PubMed Web of Science ®Google Scholar
• Pandey P, Kharbanda S, Kufe D. Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein. Cancer Res.55, 4000–4003 (1995).
   PubMed Web of Science ®Google Scholar
• Penuel E, Martin GS. Transformation by v-Src: Ras-MAPK and PI3K-mTOR mediate parallel pathways. Mol. Biol. Cell10, 1693–1703 (1999).
   PubMed Web of Science ®Google Scholar
• Meerzaman D, Shapiron PS, Kim KC. Involvement of the MAP kinase ERK2 in MUC1 mucin signaling. Am. J. Physiol. Lung Cell Mol. Physiol.281, L86–L91 (2001).
   Google Scholar
• Guy CT, Cardiff RD, Muller WJ. Induction of mammary tumors by expression of polyomavirus middle T oncogene: a transgenic mouse model for metastatic disease. Mol. Cell Biol.12, 954–961 (1992).
   PubMed Web of Science ®Google Scholar
• Guy CT, Muthuswamy SK, Cardiff RD, Soriano P, Muller WJ. Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice. Genes Dev.8, 23–32 (1994).
   PubMed Web of Science ®Google Scholar
• Spicer AP, Rowse GJ, Lidner TK, Gendler SJ. Delayed mammary tumor progression in Muc-1 null mice. J. Biol. Chem.270, 30093–30101 (1995).
   PubMed Web of Science ®Google Scholar
• Al Masri A, Gendler SJ. Muc1 affects c-Src signaling in PyV MT-induced mammary tumorigenesis. Oncogene24, 5799–5808 (2005).
   PubMed Web of Science ®Google Scholar
• Nigg EA, Sefton BM, Hunter T, Walter G, Singer SJ. Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. Proc. Natl Acad. Sci. USA79, 5322–5326 (1982).
   PubMed Web of Science ®Google Scholar
• Johnson LN, Noble ME, Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell85, 149–158 (1996).
   PubMed Web of Science ®Google Scholar
• Sefton BM, Trowbridge IS, Cooper JA, Scolnick EM. The transforming proteins of Rous sarcoma virus, Harvey sarcoma virus and Abelson virus contain tightly bound lipid. Cell31, 465–474 (1982).
   PubMed Web of Science ®Google Scholar
• Hanks SK, Ryzhova L, Shin NY, Brabek J. Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front. Biosci.8, D982–D996 (2003).
   PubMed Web of Science ®Google Scholar
• Schlaepfer DD, Hauck CR, Sieg DJ. Signaling through focal adhesion kinase. Prog. Biophys. Mol. Biol.71, 435–478 (1999).
   PubMed Web of Science ®Google Scholar
• Talmage DA, Freund R, Young AT, Dahl J, Dawe CJ, Benjamin TL. Phosphorylation of middle T by pp60c-src: a switch for binding of phosphatidylinositol 3-kinase and optimal tumorigenesis. Cell59, 55–65 (1989).
   PubMed Web of Science ®Google Scholar
• Cantley LC. The phosphoinositide 3-kinase pathway. Science296, 1655–1657 (2002).
   PubMed Web of Science ®Google Scholar
• Webster MA, Hutchinson JN, Rauh MJ et al. Requirement for both Shc and phosphatidylinositol 3´ kinase signaling pathways in polyomavirus middle T-mediated mammary tumorigenesis. Mol. Cell Biol.18, 2344–2359 (1998).
   PubMed Web of Science ®Google Scholar
• Calo V, Migliavacca M, Bazan V et al. STAT proteins: from normal control of cellular events to tumorigenesis. J. Cell Physiol.197, 157–168 (2003).
   PubMed Web of Science ®Google Scholar
• Yuan ZL, Guan YJ, Wang L, Wei W, Kane AB, Chin YE. Central role of the threonine residue within the p+1 loop of receptor tyrosine kinase in STAT3 constitutive phosphorylation in metastatic cancer cells. Mol. Cell Biol.24, 9390–9400 (2004).
   PubMed Web of Science ®Google Scholar
• Dann CE, Hsieh JC, Rattner A et al. Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains. Nature412, 86–90 (2001).
   PubMed Web of Science ®Google Scholar
• Henderson BR, Fagotto F. The ins and outs of APC and β-catenin nuclear transport. EMBO Rep.3, 834–839 (2002).
   PubMed Web of Science ®Google Scholar
• Seidensticker MJ, Behrens J. Biochemical interactions in the wnt pathway. Biochim. Biophys. Acta1495, 168–182 (2000).
   PubMed Web of Science ®Google Scholar
• Uthoff SM, Eichenberger MR, McAuliffe TL, Hamilton CJ, Galandiuk S. Wingless-type frizzled protein receptor signaling and its putative role in human colon cancer. Mol. Carcinog.31, 56–62 (2001).
   PubMed Web of Science ®Google Scholar
• Liu C, Li Y, Semenov M et al. Control of β-catenin phosphorylation/degradation by a dual-kinase mechanism. Cell108, 837–847 (2002).
   PubMed Web of Science ®Google Scholar
• Orford K, Crockett C, Jensen JP, Weissman AM, Bayers SW. Serine phosphorylation-regulated ubiquitination and degradation of β-catenin. J. Biol. Chem.272, 24735–24738 (1997).
   PubMed Web of Science ®Google Scholar
• Rubinfeld B, Souza B, Albert I, Munemitsu S, Polakis P. The APC protein and E-cadherin form similar but independent complexes with α-catenin, β-catenin, and plakoglobin. J. Biol. Chem.270, 5549–5555 (1995).
   PubMed Web of Science ®Google Scholar
• Hattrup CL, Fernandez-Rodriguez J, Schroeder JA, Hansson GC, Gendler SJ. MUC1 can interact with adenomatous polyposis coli in breast cancer. Biochem. Biophys. Res. Commun.316, 364–369 (2004).
   PubMed Web of Science ®Google Scholar
• Huang L, Chen D, Liu D, Yin L, Kharbanda S, Kufe D. MUC1 oncoprotein blocks glycogen synthase kinase 3 β-mediated phosphorylation and degradation of β-catenin. Cancer Res.65, 10413–10422 (2005).
   PubMed Web of Science ®Google Scholar
• Huang L, Ren J, Chen D, Li Y, Kharbanda S, Kufe D. MUC1 cytoplasmic domain coactivates Wnt target gene transcription and confers transformation. Cancer Biol. Ther.2, 702–706 (2003).
   PubMed Web of Science ®Google Scholar
• Roura S, Miravet S, Piedra J, Garcia de Herreros A, Dunach M. Regulation of E-cadherin/catenin association by tyrosine phosphorylation. J. Biol. Chem.274, 36734–36740 (1999).
   PubMed Web of Science ®Google Scholar
• Wen Y, Caffrey TC, Wheelock MJ, Johnson KR, Hollingsworth MA. Nuclear association of the cytoplasmic tail of MUC1 and β-catenin. J. Biol. Chem.278, 38029–38039 (2003).
   PubMed Web of Science ®Google Scholar
• Li Y, Hively WP, Varmus HE. Use of MMTV-Wnt-1 transgenic mice for studying the genetic basis of breast cancer. Oncogene19, 1002–1009 (2000).
   PubMed Web of Science ®Google Scholar
• Schroeder JA, Adriance MC, Thompson MC, Camenisch TD, Gendler SJ. MUC1 alters β-catenin-dependent tumor formation and promotes cellular invasion. Oncogene22, 1324–1332 (2003).
   PubMed Web of Science ®Google Scholar
• Ren J, Li Y, Kufe D. Protein kinase C δ regulates function of the DF3/MUC1 carcinoma antigen in β-catenin signaling. J. Biol. Chem.277, 17616–17622 (2002).
   PubMed Web of Science ®Google Scholar
• Lin SY, Xia W, Wang JC et al. β-catenin, a novel prognostic marker for breast cancer: its roles in cyclin D1 expression and cancer progression. Proc. Natl Acad. Sci. USA97, 4262–4266 (2000).
   PubMed Web of Science ®Google Scholar
• Yamashiro S, Yamakita Y, Ono S, Matsumura F. Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells. Mol. Biol. Cell9, 993–1006 (1998).
   PubMed Web of Science ®Google Scholar
• Tao YS, Edwards RA, Tubb B, Wang S, Bryan J, McCrea PD. β-catenin associates with the actin-bundling protein fascin in a noncadherin complex. J. Cell Biol.134, 1271–1281 (1996).
   PubMed Web of Science ®Google Scholar
• Kohlgraf KG, Gawron AJ, Higashi M et al. Tumor-specific immunity in MUC1.Tg mice induced by immunization with peptide vaccines from the cytoplasmic tail of CD227 (MUC1). Cancer Immunol. Immunother.53, 1068–1084 (2004).
   PubMed Web of Science ®Google Scholar
• Croce MV, Isla-Larrain MT, Rua CE, Rabassa ME, Gendler SJ, Segal-Eiras A. Patterns of MUC1 tissue expression defined by an anti-MUC1 cytoplasmic tail monoclonal antibody in breast cancer. J. Histochem. Cytochem.51, 781–788 (2003).
   PubMed Web of Science ®Google Scholar
• Carragher NO, Westhoff MA, Fincham VJ, Schaller MD, Frame MC. A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src. Curr. Biol.13, 1442–1450 (2003).
   PubMed Web of Science ®Google Scholar
• Morkel M, Huelsken J, Wakamiya M et al. β-catenin regulates Cripto- and Wnt3-dependent gene expression programs in mouse axis and mesoderm formation. Development130, 6283–6294 (2003).
   PubMed Web of Science ®Google Scholar
• van de Wetering M, Sancho E, Verweij C et al. The β-catenin/TCF-4 complex imposes a crypt progenitor phenotype on colorectal cancer cells. Cell111, 241–250 (2002).
   PubMed Web of Science ®Google Scholar
• D’Antonio A, Losito S, Pignata S et al. Transforming growth factor α, amphiregulin and cripto-1 are frequently expressed in advanced human ovarian carcinomas. Int. J. Oncol.21, 941–948 (2002).
   PubMed Web of Science ®Google Scholar
• Stromberg K, Johnson GR, O’Connor DM, Sorensen CM, Gullick WJ, Kannan B. Frequent immunohistochemical detection of EGF supergene family members in ovarian carcinogenesis. Int. J. Gynecol. Pathol.13, 342–347 (1994).
   PubMed Web of Science ®Google Scholar
• Saloman DS, Bianco C, Ebert AD et al. The EGF-CFC family: novel epidermal growth factor-related proteins in development and cancer. Endocr. Rel. Cancer7, 199–226 (2000).
   PubMed Web of Science ®Google Scholar
• Strizzi L, Bianco C, Normanno N et al. Epithelial mesenchymal transition is a characteristic of hyperplasias and tumors in mammary gland from MMTV-Cripto-1 transgenic mice. J. Cell Physiol.201, 266–276 (2004).
   PubMed Web of Science ®Google Scholar
• Hu XF, Xing PX. Cripto monoclonal antibodies. Drug News Perspect18, 293–303 (2005).
   PubMedGoogle Scholar
• Hu XF, Xing PX. Cripto as a target for cancer immunotherapy. Expert Opin. Ther. Targets9, 383–394 (2005).
   PubMed Web of Science ®Google Scholar
• Xing PX, Hu XF, Pietersz GA, Hosick HL, McKenzie IF. Cripto: a novel target for antibody-based cancer immunotherapy. Cancer Res.64, 4018–4023 (2004).
   PubMed Web of Science ®Google Scholar
• Casamassimi A, De Luca A, Agrawal S, Stromberg K, Salomon DS, Normanno N. EGF-related antisense oligonucleotides inhibit the proliferation of human ovarian carcinoma cells. Ann. Oncol.11, 319–325 (2000).
   PubMed Web of Science ®Google Scholar