Syndecan-1 is required for Wnt-1-induced mammary tumorigenesis in mice (original) (raw)
References
Bernfield, M. et al. Functions of cell surface heparan sulfate proteoglycans. Annu. Rev. Biochem.68, 729–777 (1999). ArticleCAS Google Scholar
Tsukamoto, A.S., Grosschedl, R., Guzman, R.C., Parslow, T. & Varmus, H.E. Expression of the _int_-1 gene in transgenic mice is associated with mammary gland hyperplasia and adenocarcinomas in male and female mice. Cell55, 619–625 (1988). ArticleCAS Google Scholar
Shackleford, G.M., MacArthur, C.A., Kwan, H.C. & Varmus, H.E. Mouse mammary tumor virus infection accelerates mammary carcinogenesis in Wnt-1 transgenic mice by insertional activation of _int_-2/_Fgf_-3 and hst/_Fgf_-4. Proc. Natl Acad. Sci. USA90, 740–744 (1993). ArticleCAS Google Scholar
Bernfield, M. et al. Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans. Annu. Rev. Cell Biol.8, 365–393 (1992). ArticleCAS Google Scholar
Kato, M., Saunders, S., Nguyen, H. & Bernfield, M. Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells. Mol. Biol. Cell6, 559–576 (1995). ArticleCAS Google Scholar
Cardiff, R.D. & Wellings, S.R. The comparative pathology of human and mouse mammary glands. J. Mammary Gland Biol. Neoplasia4, 105–122 (1999). ArticleCAS Google Scholar
Lee, F.S., Lane, T.F., Kuo, A., Shackleford, G.M. & Leder, P. Insertional mutagenesis identifies a member of the Wnt gene family as a candidate oncogene in the mammary epithelium of int-2/FGF-3 transgenic mice. Proc. Natl Acad. Sci USA92, 2268–2272 (1995). ArticleCAS Google Scholar
Brown, A.M.C., Wildin, R.S., Prendergast, T.J. & Varmus, H.E. A retrovirus vector expressing the putative mammary oncogene _int_-1 causes partial transformation of a mammary epithelial cell line. Cell46, 1001–1009 (1986). ArticleCAS Google Scholar
Shimizu, H. et al. Transformation by Wnt family proteins correlates with regulation of β-catenin. Cell Growth Differ.8, 1349–1358 (1997). CASPubMed Google Scholar
Uren, A. et al. Secreted Frizzled related protein sFRP-1 binds directly to Wingless and is a biphasic modulator of Wnt signaling. J. Biol. Chem.275, 4374–4382 (2000). ArticleCAS Google Scholar
Reichsman, F., Smith, L. & Cumberledge, S. Glycosaminoglycans can modulate extracellular localization of the wingless protein and promote signal transduction. J. Cell Biol.135, 819–827 (1996). ArticleCAS Google Scholar
Bradley, R.S. & Brown, A.M.C. The proto-oncogene _int_-1 encodes a secreted protein associated with the extracellular matrix. EMBO J.9, 1569–1575 (1990). ArticleCAS Google Scholar
Burrus, L.W. & McMahon, A.P. Biochemical analysis of murine Wnt proteins reveals both shared and distinct properties. Exp. Cell Res.220, 363–373 (1995). ArticleCAS Google Scholar
Jue, S.F., Bradley, R.S., Rudnicki, J.A., Varmus, H.E. & Brown, A.M.C. The mouse Wnt-1 gene can act via a paracrine mechanism in transformation of mammary epithelial cells. Mol. Cell. Biol.12, 321–328 (1992). ArticleCAS Google Scholar
Haerry, T.E., Heslip, T.R., Marsh, J.L. & O'Connor, M.B. Defects in glucuronate biosynthesis disrupt Wingless signaling in Drosophila. Development124, 3055–3064 (1997). CASPubMed Google Scholar
Hacker, U., Lin, X. & Perrimon, N. The Drosophila sugarless gene modulates Wingless signaling and encodes an enzyme involved in polysaccharide biosynthesis. Development124, 3565–3573 (1997). CAS Google Scholar
Binari, R.C. et al. Genetic evidence that heparin-like glycosaminoglycans are involved in wingless signaling. Development124, 2623–2632 (1997). CASPubMed Google Scholar
Tsuda, M. et al. The cell surface proteoglycan Dally regulates Wingless signalling in Drosophila. Nature400, 276–280 (1999). ArticleCAS Google Scholar
Lin, X. & Perrimon, N. Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling. Nature400, 281–284 (1999). ArticleCAS Google Scholar
Jackson, S.M. et al. dally, a Drosophila glypican, controls cellular responses to the TGF—related morphogen, Dpp. Development124, 4113–4120 (1997). CASPubMed Google Scholar
Bellaiche, Y., The, I. & Perrimon, N. Tout-velu is a Drosophila homolog of the putative tumor suppressor EXT-1 and is needed for Hh diffusion. Nature394, 85–88 (1998). ArticleCAS Google Scholar
Ramakrishna, N.R. & Brown, A.T. Wingless, the Drosophila homolog of the proto-oncogene Wnt-1, can transform mouse mammary epithelial cells. Development119 (suppl.), 95–103 (1993). Google Scholar
Rapraeger, A.C. In the clutches of proteoglycans: how does heparan sulfate regulate FGF binding? Chem. Biol.2, 645–649 (1995). ArticleCAS Google Scholar
Lin, X., Buff, E.M., Perrimon, N. & Michelson, A.M. Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development. Development126, 3715–3723 (1999). CASPubMed Google Scholar
Jackson, D., Bresnick, J. & Dickson, C. A role for fibroblast growth factor signaling in the lobuloalveolar development of the mammary gland. J. Mammary Gland Biol. Neoplasia2, 385–392 (1997). ArticleCAS Google Scholar
Guimond, S., Maccarana, M., Olwin, B.B., Lindahl, U. & Rapraeger, A.C. Activating and inhibitory heparin sequences for FGF-2 (b-FGF). Distinct requirements for FGF-1, FGF-2 and FGF-4. J. Biol. Chem.268, 23906–23914 (1993). CASPubMed Google Scholar
Thomas, K.R., Musci, T.S., Neumann, P.E. & Capecchi, M.R. Swaying is a mutant allele of the proto-oncogene Wnt-1. Cell67, 969–976 (1991). ArticleCAS Google Scholar
Ugolini, F. et al. Differential expression assay of chromosome 8 genes identifies Frizzled-related protein (FRP-1/FRZB) and fibroblast growth factor receptor-1 (FGFR-1) as candidate breast cancer genes. Oncogene18, 1903–1910 (1999). ArticleCAS Google Scholar
Pennica, D. et al. WISP genes are members of the connective tissue growth factor family that are up-regulated in Wnt-1 transformed cells and aberrantly expressed in human colon tumors. Proc. Natl Acad. Sci. USA95, 14717–14722 (1998). ArticleCAS Google Scholar
Jalkanen, M., Rapraeger, A., Saunders, S. & Bernfield, M. Cell surface proteoglycan of mouse mammary epithelial cells is shed by cleavage of its matrix-binding ectodomain from its membrane-associated domain. J. Cell Biol.105, 3087–3096 (1987). ArticleCAS Google Scholar
Bhanot, P. et al. A new member of the frizzled family from Drosophila functions as a Wingless receptor. Nature382, 225–230 (1996). ArticleCAS Google Scholar