메뉴 건너뛰기




Volumn 72, Issue 10, 2012, Pages 2578-2588

Loss of cell-surface laminin anchoring promotes tumor growth and is associated with poor clinical outcomes

Author keywords

[No Author keywords available]

Indexed keywords

DYSTROGLYCAN; GLYCOSYLTRANSFERASE; LAMININ; LIKE ACETYLGLUCOSAMINYLTRANSFERASE; N ACETYLGLUCOSAMINYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84861137691     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-11-3732     Document Type: Article
Times cited : (48)

References (49)
  • 1
    • 43649085395 scopus 로고    scopus 로고
    • Microenvironmental regulation of cancer development
    • DOI 10.1016/j.gde.2007.12.006, PII S0959437X0800004X
    • Hu M, Polyak K. Microenvironmental regulation of cancer development. Curr Opin Genet Dev 2008;18:27-34. (Pubitemid 351694443)
    • (2008) Current Opinion in Genetics and Development , vol.18 , Issue.1 , pp. 27-34
    • Hu, M.1    Polyak, K.2
  • 2
    • 33751217466 scopus 로고    scopus 로고
    • Tumor Morphology and Phenotypic Evolution Driven by Selective Pressure from the Microenvironment
    • DOI 10.1016/j.cell.2006.09.042, PII S0092867406013481
    • Anderson AR, Weaver AM, Cummings PT, Quaranta V. Tumor morphology and phenotypic evolution driven by selective pressure from the microenvironment. Cell 2006; 127:905-15. (Pubitemid 44792251)
    • (2006) Cell , vol.127 , Issue.5 , pp. 905-915
    • Anderson, A.R.A.1    Weaver, A.M.2    Cummings, P.T.3    Quaranta, V.4
  • 3
    • 69949101473 scopus 로고    scopus 로고
    • Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment
    • Schafer ZT, Grassian AR, Song L, Jiang Z, Gerhart-Hines Z, Irie HY, et al. Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment. Nature 2009;461: 109-13.
    • (2009) Nature , vol.461 , pp. 109-113
    • Schafer, Z.T.1    Grassian, A.R.2    Song, L.3    Jiang, Z.4    Gerhart-Hines, Z.5    Irie, H.Y.6
  • 4
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • Levental KR, Yu H, Kass L, Lakins JN, Egeblad M, Erler JT, et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell 2009;139:891-906.
    • (2009) Cell , vol.139 , pp. 891-906
    • Levental, K.R.1    Yu, H.2    Kass, L.3    Lakins, J.N.4    Egeblad, M.5    Erler, J.T.6
  • 5
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002;2:161-74. (Pubitemid 37328786)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 7
    • 65649130436 scopus 로고    scopus 로고
    • Developmental and pathogenic mechanisms of basement membrane assembly
    • Yurchenco PD, Patton BL. Developmental and pathogenic mechanisms of basement membrane assembly. Curr Pharm Des 2009;15: 1277-94.
    • (2009) Curr Pharm Des , vol.15 , pp. 1277-1294
    • Yurchenco, P.D.1    Patton, B.L.2
  • 8
    • 50849145156 scopus 로고    scopus 로고
    • Collagen fibrillogenesis: Fibronectin, integrins, and minor collagens as organizers and nucleators
    • Kadler KE, Hill A, Canty-Laird EG. Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators. Curr Opin Cell Biol 2008;20:495-501.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 495-501
    • Kadler, K.E.1    Hill, A.2    Canty-Laird, E.G.3
  • 9
    • 1842509188 scopus 로고    scopus 로고
    • Laminin: The crux of basement membrane assembly
    • DOI 10.1083/jcb.200401058
    • Sasaki T, Fassler R, Hohenester E. Laminin: the crux of basement membrane assembly. J Cell Biol 2004;164:959-63. (Pubitemid 38429121)
    • (2004) Journal of Cell Biology , vol.164 , Issue.7 , pp. 959-963
    • Sasaki, T.1    Fassler, R.2    Hohenester, E.3
  • 10
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • DOI 10.1083/jcb.145.3.619
    • Colognato H, Winkelmann DA, Yurchenco PD. Laminin polymerization induces a receptor-cytoskeleton network. J Cell Biol 1999;145: 619-31. (Pubitemid 29215724)
    • (1999) Journal of Cell Biology , vol.145 , Issue.3 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 11
    • 0035870134 scopus 로고    scopus 로고
    • Assembly of laminin polymers is dependent on beta1-integrins
    • DOI 10.1006/excr.2001.5170
    • Lohikangas L, Gullberg D, Johansson S. Assembly of laminin polymers is dependent on beta1-integrins. Exp Cell Res 2001;265:135-44. (Pubitemid 32989071)
    • (2001) Experimental Cell Research , vol.265 , Issue.1 , pp. 135-144
    • Lohikangas, L.1    Gullberg, D.2    Johansson, S.3
  • 12
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • DOI 10.1016/S0092-8674(00)81708-0
    • Henry MD, Campbell KP. A role for dystroglycan in basement membrane assembly. Cell 1998;95:859-70. (Pubitemid 29014465)
    • (1998) Cell , vol.95 , Issue.6 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 13
    • 33750436537 scopus 로고    scopus 로고
    • Dystroglycan loss disrupts polarity and beta-casein induction in mammary epithelial cells by perturbing laminin anchoring
    • DOI 10.1242/jcs.03103
    • Weir ML, Oppizzi ML, Henry MD, Onishi A, Campbell KP, Bissell MJ, et al. Dystroglycan loss disrupts polarity and {beta}-casein induction in mammary epithelial cells by perturbing laminin anchoring. J Cell Sci 2006;119:4047-58. (Pubitemid 44650877)
    • (2006) Journal of Cell Science , vol.119 , Issue.19 , pp. 4047-4058
    • Weir, M.L.1    Oppizzi, M.L.2    Henry, M.D.3    Onishi, A.4    Campbell, K.P.5    Bissell, M.J.6    Muschler, J.L.7
  • 14
    • 17644375191 scopus 로고    scopus 로고
    • Laminin-sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
    • DOI 10.1083/jcb.200501098
    • Li S, Liquari P, McKee KK, Harrison D, Patel R, Lee S, et al. Lamininsulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts. J Cell Biol 2005;169:179-89. (Pubitemid 40562924)
    • (2005) Journal of Cell Biology , vol.169 , Issue.1 , pp. 179-189
    • Li, S.1    Liquari, P.2    McKee, K.K.3    Harrison, D.4    Patel, R.5    Lee, S.6    Yurchenco, P.D.7
  • 16
    • 0035988822 scopus 로고    scopus 로고
    • Laminin isoforms in tumor invasion, angiogenesis and metastasis
    • DOI 10.1016/S1044-579X(02)00023-8
    • Patarroyo M, Tryggvason K, Virtanen I. Laminin isoforms in tumor invasion, angiogenesis and metastasis. Semin Cancer Biol 2002;12: 197-207. (Pubitemid 34833063)
    • (2002) Seminars in Cancer Biology , vol.12 , Issue.3 , pp. 197-207
    • Patarroyo, M.1    Tryggvason, K.2    Virtanen, I.3
  • 17
    • 0036990109 scopus 로고    scopus 로고
    • The organizing principle: Microenvironmental influences in the normal and malignant breast
    • DOI 10.1046/j.1432-0436.2002.700907.x
    • Bissell MJ, Radisky DC, Rizki A, Weaver VM, Petersen OW. The organizing principle: microenvironmental influences in the normal and malignant breast. Differentiation 2002;70:537-46. (Pubitemid 36194318)
    • (2002) Differentiation , vol.70 , Issue.9-10 , pp. 537-546
    • Bissell, M.J.1    Radisky, D.C.2    Rizki, A.3    Weaver, V.M.4    Petersen, O.W.5
  • 18
    • 0036153330 scopus 로고    scopus 로고
    • Normal and tumor-derived myoepithelial cells differ in their ability to interact with luminal breast epithelial cells for polarity and basement membrane deposition
    • Gudjonsson T, Ronnov-Jessen L, Villadsen R, Rank F, Bissell MJ, Petersen OW. Normal and tumor-derived myoepithelial cells differ in their ability to interact with luminal breast epithelial cells for polarity and basement membrane deposition. J Cell Sci 2002; 115:39-50. (Pubitemid 34105527)
    • (2002) Journal of Cell Science , vol.115 , Issue.1 , pp. 39-50
    • Gudjonsson, T.1    Ronnov-Jessen, L.2    Villadsen, R.3    Rank, F.4    Bissell, M.J.5    Petersen, O.W.6
  • 19
    • 77950257304 scopus 로고    scopus 로고
    • Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists
    • Yang XH, Flores LM, Li Q, Zhou P, Xu F, Krop IE, et al. Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists. Cancer Res 2010;70: 2256-63.
    • (2010) Cancer Res , vol.70 , pp. 2256-2263
    • Yang, X.H.1    Flores, L.M.2    Li, Q.3    Zhou, P.4    Xu, F.5    Krop, I.E.6
  • 20
    • 0036726312 scopus 로고    scopus 로고
    • beta4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium
    • DOI 10.1016/S1535-6108(02)00125-3
    • Weaver VM, Lelievre S, Lakins JN, Chrenek MA, Jones JC, Giancotti F, et al. beta4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium. Cancer Cell 2002;2:205-16. (Pubitemid 41043976)
    • (2002) Cancer Cell , vol.2 , Issue.3 , pp. 205-216
    • Weaver, V.M.1    Lelievre, S.2    Lakins, J.N.3    Chrenek, M.A.4    Jones, J.C.R.5    Giancotti, F.6    Werb, Z.7    Bissell, M.J.8
  • 23
    • 46249106990 scopus 로고    scopus 로고
    • Mapping and quantifying mammalian transcriptomes by RNA-Seq
    • DOI 10.1038/nmeth.1226, PII NMETH.1226
    • Mortazavi A, WilliamsBA, McCue K, Schaeffer L, Wold B. Mapping and quantifying mammalian transcriptomes by RNA-Seq. Nat Methods 2008;5:621-8. (Pubitemid 351911867)
    • (2008) Nature Methods , vol.5 , Issue.7 , pp. 621-628
    • Mortazavi, A.1    Williams, B.A.2    McCue, K.3    Schaeffer, L.4    Wold, B.5
  • 26
    • 78149370128 scopus 로고    scopus 로고
    • Dystroglycan controls signaling of multiple hormones through modulation of STAT5 activity
    • Leonoudakis D, Singh M, Mohajer R, Mohajer P, Fata JE, Campbell KP, et al. Dystroglycan controls signaling of multiple hormones through modulation of STAT5 activity. J Cell Sci 2010;123: 3683-92.
    • (2010) J Cell Sci , vol.123 , pp. 3683-3692
    • Leonoudakis, D.1    Singh, M.2    Mohajer, R.3    Mohajer, P.4    Fata, J.E.5    Campbell, K.P.6
  • 29
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: From biosynthesis to pathogenesis of human disease
    • DOI 10.1242/jcs.02814
    • Barresi R, Campbell KP. Dystroglycan: from biosynthesis to pathogenesis of human disease. J Cell Sci 2006;119:199-207. (Pubitemid 43210689)
    • (2006) Journal of Cell Science , vol.119 , Issue.2 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 30
    • 35348891997 scopus 로고    scopus 로고
    • Altered expression of natively glycosylated alpha dystroglycan in pediatric solid tumors
    • DOI 10.1016/j.humpath.2007.03.025, PII S0046817707001621
    • Martin LT, Glass M, Dosunmu E, Martin PT. Altered expression of natively glycosylated alpha dystroglycan in pediatric solid tumors. Hum Pathol 2007;38:1657-68. (Pubitemid 47589088)
    • (2007) Human Pathology , vol.38 , Issue.11 , pp. 1657-1668
    • Martin, L.T.1    Glass, M.2    Dosunmu, E.3    Martin, P.T.4
  • 31
    • 67749098053 scopus 로고    scopus 로고
    • Tumor suppressor function of lamininbinding alpha-dystroglycan requires a distinct beta3-N-acetylglucosaminyltransferase
    • Bao X, Kobayashi M, Hatakeyama S, Angata K, Gullberg D, Nakayama J, et al. Tumor suppressor function of lamininbinding alpha-dystroglycan requires a distinct beta3-N-acetylglucosaminyltransferase. Proc Natl Acad Sci U S A 2009;106: 12109-14.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 12109-12114
    • Bao, X.1    Kobayashi, M.2    Hatakeyama, S.3    Angata, K.4    Gullberg, D.5    Nakayama, J.6
  • 33
  • 34
    • 70349101617 scopus 로고    scopus 로고
    • Abnormal glycosylation of dystroglycan in human genetic disease
    • Hewitt JE. Abnormal glycosylation of dystroglycan in human genetic disease. Biochim Biophys Acta 2009;1792:853-61.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 853-861
    • Hewitt, J.E.1
  • 35
  • 36
    • 33644867290 scopus 로고    scopus 로고
    • Defining molecular profiles of poor outcome in patients with invasive bladder cancer using oligonucleotide microarrays
    • DOI 10.1200/JCO.2005.03.2375
    • Sanchez-Carbayo M, Socci ND, Lozano J, Saint F, Cordon-Cardo C. Defining molecular profiles of poor outcome in patients with invasive bladder cancer using oligonucleotide microarrays. J Clin Oncol 2006;24:778-89. (Pubitemid 46622045)
    • (2006) Journal of Clinical Oncology , vol.24 , Issue.5 , pp. 778-789
    • Sanchez-Carbayo, M.1    Socci, N.D.2    Lozano, J.3    Saint, F.4    Cordon-Cardo, C.5
  • 37
    • 39749137048 scopus 로고    scopus 로고
    • Transcriptional recapitulation and subversion of embryonic colon development by mouse colon tumor models and human colon cancer
    • Kaiser S, Park YK, Franklin JL, Halberg RB, Yu M, Jessen WJ, et al. Transcriptional recapitulation and subversion of embryonic colon development by mouse colon tumor models and human colon cancer. Genome Biol 2007;8:R131.
    • (2007) Genome Biol , vol.8
    • Kaiser, S.1    Park, Y.K.2    Franklin, J.L.3    Halberg, R.B.4    Yu, M.5    Jessen, W.J.6
  • 38
    • 66349100709 scopus 로고    scopus 로고
    • Patterns of gene expression and copy-number alterations in von- Hippel Lindau disease-associated and sporadic clear cell carcinoma of the kidney
    • Beroukhim R, Brunet JP, Di Napoli A, Mertz KD, Seeley A, Pires MM, et al. Patterns of gene expression and copy-number alterations in von- Hippel Lindau disease-associated and sporadic clear cell carcinoma of the kidney. Cancer Res 2009;69:4674-81.
    • (2009) Cancer Res , vol.69 , pp. 4674-4681
    • Beroukhim, R.1    Brunet, J.P.2    Di Napoli, A.3    Mertz, K.D.4    Seeley, A.5    Pires, M.M.6
  • 39
    • 0043244946 scopus 로고    scopus 로고
    • Transcriptional silencing of zinc finger protein 185 identified by expression profiling is associated with prostate cancer progression
    • Vanaja DK, Cheville JC, Iturria SJ, Young CY. Transcriptional silencing of zinc finger protein 185 identified by expression profiling is associated with prostate cancer progression. Cancer Res 2003;63: 3877-82. (Pubitemid 36917897)
    • (2003) Cancer Research , vol.63 , Issue.14 , pp. 3877-3882
    • Vanaja, D.K.1    Cheville, J.C.2    Iturria, S.J.3    Young, C.Y.F.4
  • 40
    • 49649103221 scopus 로고    scopus 로고
    • The gene expression profiles of primary and metastatic melanoma yields a transition point of tumor progression and metastasis
    • Riker AI, Enkemann SA, Fodstad O, Liu S, Ren S, Morris C, et al. The gene expression profiles of primary and metastatic melanoma yields a transition point of tumor progression and metastasis. BMC Med Genomics 2008;1:13.
    • (2008) BMC Med Genomics , vol.1 , pp. 13
    • Riker, A.I.1    Enkemann, S.A.2    Fodstad, O.3    Liu, S.4    Ren, S.5    Morris, C.6
  • 41
    • 33645772227 scopus 로고    scopus 로고
    • Neuronal and glioma-derived stem cell factor induces angiogenesis within the brain
    • Sun L, Hui AM, Su Q, Vortmeyer A, Kotliarov Y, Pastorino S, et al. Neuronal and glioma-derived stem cell factor induces angiogenesis within the brain. Cancer Cell 2006;9:287-300.
    • (2006) Cancer Cell , vol.9 , pp. 287-300
    • Sun, L.1    Hui, A.M.2    Su, Q.3    Vortmeyer, A.4    Kotliarov, Y.5    Pastorino, S.6
  • 46
    • 76049106434 scopus 로고    scopus 로고
    • Polarity protein alterations in carcinoma: A focus on emerging roles for polarity regulators
    • Huang L, Muthuswamy SK. Polarity protein alterations in carcinoma: a focus on emerging roles for polarity regulators. Curr Opin Genet Dev 2010;20:41-50.
    • (2010) Curr Opin Genet Dev , vol.20 , pp. 41-50
    • Huang, L.1    Muthuswamy, S.K.2
  • 48
    • 80053356357 scopus 로고    scopus 로고
    • Genome-wide methylation analysis identifies genes specific to breast cancer hormone receptor status and risk of recurrence
    • Fackler MJ, Umbricht C, Williams D, Argani P, Cruz LA, Merino VF, et al. Genome-wide methylation analysis identifies genes specific to breast cancer hormone receptor status and risk of recurrence. Cancer Res 2011;71:6195-207.
    • (2011) Cancer Res , vol.71 , pp. 6195-6207
    • Fackler, M.J.1    Umbricht, C.2    Williams, D.3    Argani, P.4    Cruz, L.A.5    Merino, V.F.6
  • 49
    • 0026738947 scopus 로고
    • Interaction with basement membrane serves to rapidly distinguish growth and differentiation pattern of normal and malignant human breast epithelial cells
    • Petersen OW, Ronnov JL, Howlett AR, Bissell MJ. Interaction with basement membrane serves to rapidly distinguish growth and differentiation pattern of normal and malignant human breast epithelial cells. Proc Natl Acad Sci U S A 1992;89:9064-8.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 9064-9068
    • Petersen, O.W.1    Ronnov, J.L.2    Howlett, A.R.3    Bissell, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.