메뉴 건너뛰기




Volumn 586, Issue 13, 2012, Pages 1813-1820

Induction of epithelial-mesenchymal transition with O-glycosylated oncofetal fibronectin

Author keywords

EMT; Non small cell lung cancer; O GalNAc; Oncofetal FN; TGF 1

Indexed keywords

FIBRONECTIN; MONOCLONAL ANTIBODY; N ACETYLGALACTOSAMINE; ONCOFETAL FIBRONECTIN; TRANSFORMING GROWTH FACTOR BETA1; UNCLASSIFIED DRUG;

EID: 84862501413     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.05.020     Document Type: Article
Times cited : (29)

References (34)
  • 1
    • 0030480250 scopus 로고    scopus 로고
    • Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism
    • Hakomori, S. (1996) Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res. 56, 5309-5318.
    • (1996) Cancer Res. , vol.56 , pp. 5309-5318
    • Hakomori, S.1
  • 2
    • 78049507803 scopus 로고    scopus 로고
    • Gangliosides as regulators of cell membrane organization and functions
    • Sonnino, S. and Prinetti, A. (2010) Gangliosides as regulators of cell membrane organization and functions. Adv. Exp. Med. Biol. 688, 165-184.
    • (2010) Adv. Exp. Med. Biol. , vol.688 , pp. 165-184
    • Sonnino, S.1    Prinetti, A.2
  • 4
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: New wine in an old bottle
    • Hakomori, S. (2002) Glycosylation defining cancer malignancy: new wine in an old bottle. Proc. Natl. Acad. Sci. U. S. A. 99, 10231-10233.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 7
    • 78649725167 scopus 로고    scopus 로고
    • Functional role of gangliotetraosylceramide in epithelial-to-mesenchymal transition process induced by hypoxia and by TGF-b
    • Guan, F., Schaffer, L., Handa, K. and Hakomori, S. (2010) Functional role of gangliotetraosylceramide in epithelial-to-mesenchymal transition process induced by hypoxia and by TGF-b. FASEB J. 24, 4889-4903.
    • (2010) FASEB J. , vol.24 , pp. 4889-4903
    • Guan, F.1    Schaffer, L.2    Handa, K.3    Hakomori, S.4
  • 8
    • 66149101390 scopus 로고    scopus 로고
    • Specific glycosphingolipids mediate epithelial-to-mesenchymal transition of human and mouse epithelial cell lines
    • Guan, F., Handa, K. and Hakomori, S. (2009) Specific glycosphingolipids mediate epithelial-to-mesenchymal transition of human and mouse epithelial cell lines. Proc. Natl. Acad. Sci. U. S. A. 106, 7461-7466.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 7461-7466
    • Guan, F.1    Handa, K.2    Hakomori, S.3
  • 9
    • 0020358296 scopus 로고
    • Epithelia suspended in collagen gels can lose polarity and express characteristics of migrating mesenchymal cells
    • DOI 10.1083/jcb.95.1.333
    • Greenburg, G. and Hay, E.D. (1982) Epithelia suspended in collagen gels can lose polarity and express characteristics of migrating mesenchymal cells. J. Cell Biol. 95, 333-339. (Pubitemid 13197104)
    • (1982) Journal of Cell Biology , vol.95 , Issue.1 , pp. 333-339
    • Greenburg, G.1    Hay, E.D.2
  • 10
    • 0029553183 scopus 로고
    • An overview of epithelio-mesenchymal transformation
    • Basel
    • Hay, E.D. (1995) An overview of epithelio-mesenchymal transformation. Acta Anat. (Basel) 154, 8-20.
    • (1995) Acta Anat. , vol.154 , pp. 8-20
    • Hay, E.D.1
  • 11
    • 80052712201 scopus 로고    scopus 로고
    • The ins and outs of the epithelial to mesenchymal transition in health and disease
    • Nieto, M.A. (2011) The ins and outs of the epithelial to mesenchymal transition in health and disease. Annu. Rev. Cell Dev. Biol. 27, 347-376.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 347-376
    • Nieto, M.A.1
  • 12
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan, D. and Weinberg, R.A. (2011) Hallmarks of cancer: the next generation. Cell 144, 646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 13
    • 70450198396 scopus 로고    scopus 로고
    • Epithelialmesenchymal transitions in development and disease
    • Thiery, J.P., Acloque, H., Huang, R.Y. and Nieto, M.A. (2009) Epithelialmesenchymal transitions in development and disease. Cell 139, 871-890.
    • (2009) Cell , vol.139 , pp. 871-890
    • Thiery, J.P.1    Acloque, H.2    Huang, R.Y.3    Nieto, M.A.4
  • 14
    • 33645302628 scopus 로고    scopus 로고
    • The epithelialmesenchymal transition: New insights in signaling, development, and disease
    • Lee, J.M., Dedhar, S., Kalluri, R. and Thompson, E.W. (2006) The epithelialmesenchymal transition: new insights in signaling, development, and disease. J. Cell Biol. 172, 973-981.
    • (2006) J. Cell Biol. , vol.172 , pp. 973-981
    • Lee, J.M.1    Dedhar, S.2    Kalluri, R.3    Thompson, E.W.4
  • 15
    • 0346724511 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition and its implications for fibrosis
    • DOI 10.1172/JCI200320530
    • Kalluri, R. and Neilson, E.G. (2003) Epithelial-mesenchymal transition and its implications for fibrosis. J. Clin. Invest. 112, 1776-1784. (Pubitemid 38063698)
    • (2003) Journal of Clinical Investigation , vol.112 , Issue.12 , pp. 1776-1784
    • Kalluri, R.1    Neilson, E.G.2
  • 16
    • 0342371891 scopus 로고
    • The oncofetal domain of fibronectin defined by monoclonal antibody FDC-6: Its presence in fibronectins from fetal and tumor tissues and its absence in those from normal adult tissues and plasma
    • DOI 10.1073/pnas.82.19.6517
    • Matsuura, H. and Hakomori, S. (1985) The oncofetal domain of fibronectin defined by monoclonal antibody FDC-6: its presence in fibronectins from fetal and tumor tissues and its absence in those from normal adult tissues and plasma. Proc. Natl. Acad. Sci. U. S. A. 82, 6517-6521. (Pubitemid 16230545)
    • (1985) Proceedings of the National Academy of Sciences of the United States of America , vol.82 , Issue.19 , pp. 6517-6521
    • Matsuura, H.1    Hakomori, S.I.2
  • 17
    • 0023831538 scopus 로고
    • The oncofetal structure of human fibronectin defined by monoclonal antibody FDC-6. Unique structural requirement for the antigenic specificity provided by a glycosylhexapeptide
    • Matsuura, H., Takio, K., Titani, K., Greene, T., Levery, S.B., Salyan, M.E.K. and Hakomori, S. (1988) The oncofetal structure of human fibronectin defined by monoclonal antibody FDC-6: Unique structural requirement for the antigenic specificity provided by a glycosylhexapeptide. J. Biol. Chem. 263, 3314-3322. (Pubitemid 18072789)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.7 , pp. 3314-3322
    • Matsuura, H.1    Takio, K.2    Titani, K.3    Greene, T.4    Levery, S.B.5    Salyan, M.E.K.6    Hakomori, S.7
  • 18
    • 0024316015 scopus 로고
    • An a-N-acetylgalactosaminylation at the threonine residue of a defined peptide sequence creates the oncofetal peptide epitope in human fibronectin
    • Matsuura, H., Greene, T. and Hakomori, S. (1989) An a- Nacetylgalactosaminylation at the threonine residue of a defined peptide sequence creates the oncofetal peptide epitope in human fibronectin. J. Biol. Chem. 264, 10472-10476. (Pubitemid 19161611)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.18 , pp. 10472-10476
    • Matsuura, H.1    Greene, T.2    Hakomori, S.3
  • 19
    • 0033520457 scopus 로고    scopus 로고
    • Cloning and characterization of a close homologue of human UDP-Nacetyl-alpha-D-galactosamine:Polypeptide Nacetylgalactosaminyltransferase- T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy
    • Bennett, E.P., Hassan, H., Mandel, U., Hollingsworth, M.A., Akisawa, N., Ikematsu, Y., Merkx, G., Geurts van Kessel, A., Olofsson, S. and Clausen, H. (1999) Cloning and characterization of a close homologue of human UDP-Nacetyl-alpha-D-galactosamine:Polypeptide Nacetylgalactosaminyltransferase- T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy. J. Biol. Chem. 274, 25362-25370.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25362-25370
    • Bennett, E.P.1    Hassan, H.2    Mandel, U.3    Hollingsworth, M.A.4    Akisawa, N.5    Ikematsu, Y.6    Merkx, G.7    Geurts Van Kessel, A.8    Olofsson, S.9    Clausen, H.10
  • 21
    • 0017375736 scopus 로고
    • Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
    • Engvall, E. and Ruoslahti, E. (1977) Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int. J. Cancer 20, 1-5. (Pubitemid 8139735)
    • (1977) International Journal of Cancer , vol.20 , Issue.1 , pp. 1-5
    • Engvall, E.1    Ruoslahti, E.2
  • 22
    • 34247184670 scopus 로고    scopus 로고
    • Ganglioside GM2-tetraspanin CD82 complex inhibits Met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse
    • DOI 10.1074/jbc.M611407200
    • Todeschini, A.R., Dos Santos, J.N., Handa, K. and Hakomori, S. (2007) Ganglioside GM2-tetraspanin CD82 complex inhibits Met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse. J. Biol. Chem. 282, 8123-8133. (Pubitemid 47093583)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.11 , pp. 8123-8133
    • Todeschini, A.R.1    Dos, S.J.N.2    Handa, K.3    Hakomori, S.-I.4
  • 23
    • 27444438906 scopus 로고    scopus 로고
    • A specific microdomain ("glycosynapse 3") controls phenotypic conversion and reversion of bladder cancer cells through GM3-mediated interaction of alpha3beta1 integrin with CD9
    • DOI 10.1074/jbc.M505630200
    • Mitsuzuka, K., Handa, K., Satoh, M., Arai, Y. and Hakomori, S. (2005) A specific microdomain ("glycosynapse 3") controls phenotypic conversion and reversion of bladder cancer cells through GM3-mediated interaction of alpha3beta1 integrin with CD9. J. Biol. Chem. 280, 35545-35553. (Pubitemid 41532746)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35545-35553
    • Mitsuzuka, K.1    Handa, K.2    Satoh, M.3    Arai, Y.4    Hakomori, S.5
  • 24
    • 4544250815 scopus 로고    scopus 로고
    • Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13
    • DOI 10.1074/jbc.M403857200
    • Toledo, M.S., Suzuki, E., Handa, K. and Hakomori, S. (2004) Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13. J. Biol. Chem. 279, 34655-34664. (Pubitemid 39318095)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34655-34664
    • Toledo, M.S.1    Suzuki, E.2    Handa, K.3    Hakomori, S.4
  • 25
    • 79952106660 scopus 로고    scopus 로고
    • Location, location, location: New insights into O-GalNAc protein glycosylation
    • Gill, D.J., Clausen, H. and Bard, F. (2011) Location, location, location: new insights into O-GalNAc protein glycosylation. Trends Cell Biol. 21, 149-158.
    • (2011) Trends Cell Biol. , vol.21 , pp. 149-158
    • Gill, D.J.1    Clausen, H.2    Bard, F.3
  • 26
    • 84857445346 scopus 로고    scopus 로고
    • Control of Mucin-Type O-Glycosylation - A Classification of the Polypeptide GalNAc-transferase Gene Family
    • Epub ahead of print
    • Bennett, E.P., Mandel, U., Clausen, H., Gerken, T.A., Fritz, T.A. and Tabak, L.A. (2011) Control of Mucin-Type O-Glycosylation - A Classification of the Polypeptide GalNAc-transferase Gene Family. Glycobiology [Epub ahead of print].
    • (2011) Glycobiology
    • Bennett, E.P.1    Mandel, U.2    Clausen, H.3    Gerken, T.A.4    Fritz, T.A.5    Tabak, L.A.6
  • 27
  • 29
    • 79959596406 scopus 로고    scopus 로고
    • Fibronectin splice variants: Understanding their multiple roles in health and disease using engineered mouse models
    • White, E.S. and Muro, A.F. (2011) Fibronectin splice variants: understanding their multiple roles in health and disease using engineered mouse models. IUBMB. Life 63, 538-546.
    • (2011) IUBMB. Life , vol.63 , pp. 538-546
    • White, E.S.1    Muro, A.F.2
  • 30
    • 50249176028 scopus 로고    scopus 로고
    • New insights into form and function of fibronectin splice variants
    • White, E.S., Baralle, F.E. and Muro, A.F. (2008) New insights into form and function of fibronectin splice variants. J. Pathol. 216, 1-14.
    • (2008) J. Pathol. , vol.216 , pp. 1-14
    • White, E.S.1    Baralle, F.E.2    Muro, A.F.3
  • 31
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • DOI 10.1242/jcs.00059
    • Pankov, R. and Yamada, K.M. (2002) Fibronectin at a glance. J. Cell Sci. 115, 3861-3863. (Pubitemid 35256486)
    • (2002) Journal of Cell Science , vol.115 , Issue.20 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 32
    • 0023392493 scopus 로고
    • Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon
    • Zardi, L., Carnemolla, B., Siri, A., Petersen, T.E., Paolella, G., Sebastio, G. and Baralle, F.E. (1987) Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon. EMBO J. 6, 2337-2342.
    • (1987) EMBO J. , vol.6 , pp. 2337-2342
    • Zardi, L.1    Carnemolla, B.2    Siri, A.3    Petersen, T.E.4    Paolella, G.5    Sebastio, G.6    Baralle, F.E.7
  • 33
    • 79953708277 scopus 로고    scopus 로고
    • Polypeptide N-acetylgalactosaminyltransferase 6 disrupts mammary acinar morphogenesis through O-glycosylation of fibronectin
    • Park, J.H., Katagiri, T., Chung, S., Kijima, K. and Nakamura, Y. (2011) Polypeptide N-acetylgalactosaminyltransferase 6 disrupts mammary acinar morphogenesis through O-glycosylation of fibronectin. Neoplasia 13, 320-326.
    • (2011) Neoplasia , vol.13 , pp. 320-326
    • Park, J.H.1    Katagiri, T.2    Chung, S.3    Kijima, K.4    Nakamura, Y.5
  • 34
    • 79954570719 scopus 로고    scopus 로고
    • Myofibroblast differentiation during fibrosis: Role of NAD(P)H oxidases
    • Barnes, J.L. and Gorin, Y. (2011) Myofibroblast differentiation during fibrosis: role of NAD(P)H oxidases. Kidney Int. 79, 944-956.
    • (2011) Kidney Int. , vol.79 , pp. 944-956
    • Barnes, J.L.1    Gorin, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.