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Volumn 379, Issue 4, 2009, Pages 1091-1096

Role of E-cadherin N-glycosylation profile in a mammary tumor model

Author keywords

Adenoma; Canine; Carcinoma; E cadherin; Mammary gland tumor; N glycosylation

Indexed keywords

MANNOSE; UVOMORULIN;

EID: 58949097354     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.01.024     Document Type: Article
Times cited : (71)

References (21)
  • 1
    • 0033853424 scopus 로고    scopus 로고
    • The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation
    • Beavon I.R.G. The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation. Eur. J. Cancer 36 (2000) 1607-1620
    • (2000) Eur. J. Cancer , vol.36 , pp. 1607-1620
    • Beavon, I.R.G.1
  • 2
    • 33747377812 scopus 로고    scopus 로고
    • N-glycosylation affects the molecular organization and stability of E-cadherin junctions
    • Liwosz A., Lei T., and Kukuruzinska M.A. N-glycosylation affects the molecular organization and stability of E-cadherin junctions. J. Biol. Chem. 281 (2006) 23138-23149
    • (2006) J. Biol. Chem. , vol.281 , pp. 23138-23149
    • Liwosz, A.1    Lei, T.2    Kukuruzinska, M.A.3
  • 3
    • 46449101373 scopus 로고    scopus 로고
    • N-glycosylation affects the adhesive function of E-cadherin through modifying the composition of adherens junctions in human breast carcinoma cell line MDA-MB-435
    • Zhao H., Liang Y., Xu Z., Wang L., Zhou F., Li Z., Jin J., Yang Y., Fang Z., Hu Y., Zhang L., Su J., and Zha X. N-glycosylation affects the adhesive function of E-cadherin through modifying the composition of adherens junctions in human breast carcinoma cell line MDA-MB-435. J. Cell Biochem. 104 (2008) 162-175
    • (2008) J. Cell Biochem. , vol.104 , pp. 162-175
    • Zhao, H.1    Liang, Y.2    Xu, Z.3    Wang, L.4    Zhou, F.5    Li, Z.6    Jin, J.7    Yang, Y.8    Fang, Z.9    Hu, Y.10    Zhang, L.11    Su, J.12    Zha, X.13
  • 4
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: glycans as novel therapeutic targets
    • Fuster M.M., and Esko J.D. The sweet and sour of cancer: glycans as novel therapeutic targets. Nature 5 (2005) 526-542
    • (2005) Nature , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 5
    • 0033655080 scopus 로고    scopus 로고
    • Characterization of Protein Glycosylation by MALDI-TOFMS
    • Mirgorodskaya E., Krogh T.N., and Roepstorff P. Characterization of Protein Glycosylation by MALDI-TOFMS. Methods Mol. Biol. 146 (2000) 273-292
    • (2000) Methods Mol. Biol. , vol.146 , pp. 273-292
    • Mirgorodskaya, E.1    Krogh, T.N.2    Roepstorff, P.3
  • 6
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K., and Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell 126 (2006) 855-867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 7
    • 13544268336 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein N-glycosylation
    • Yan A., and Lennarz W.J. Unraveling the mechanism of protein N-glycosylation. J. Biol. Chem. 280 (2005) 3121-3124
    • (2005) J. Biol. Chem. , vol.280 , pp. 3121-3124
    • Yan, A.1    Lennarz, W.J.2
  • 9
    • 34547799601 scopus 로고    scopus 로고
    • Sialyl lewis × expression in canine malignant mammary tumours: correlation with clinicopathological features and E-cadherin expression
    • Pinho S.S., Matos A.J.F., Lopes C., Marcos N.T., Carvalheira J., Reis C.A., and Gärtner F. Sialyl lewis × expression in canine malignant mammary tumours: correlation with clinicopathological features and E-cadherin expression. BMC Cancer 7 (2007) 124
    • (2007) BMC Cancer , vol.7 , pp. 124
    • Pinho, S.S.1    Matos, A.J.F.2    Lopes, C.3    Marcos, N.T.4    Carvalheira, J.5    Reis, C.A.6    Gärtner, F.7
  • 11
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • Yoshimura M., Ihara Y., Matsuzawa Y., and Taniguchi N. Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis. J. Biol. Chem. 271 (1996) 13811-13815
    • (1996) J. Biol. Chem. , vol.271 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4
  • 12
    • 0347993082 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways
    • Guo H.B., Lee I., Kamar M., and Pierce M. N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways. J. Biol. Chem. 278 (2003) 52412-52424
    • (2003) J. Biol. Chem. , vol.278 , pp. 52412-52424
    • Guo, H.B.1    Lee, I.2    Kamar, M.3    Pierce, M.4
  • 14
    • 38349191968 scopus 로고    scopus 로고
    • Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: contribution of the Na, K-ATPase β1 subunit
    • Vagin O., Tokhtaeva E., Yakubov I., Shevchenko E., and Sachs G. Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: contribution of the Na, K-ATPase β1 subunit. J. Biol. Chem. 283 (2008) 2192-2202
    • (2008) J. Biol. Chem. , vol.283 , pp. 2192-2202
    • Vagin, O.1    Tokhtaeva, E.2    Yakubov, I.3    Shevchenko, E.4    Sachs, G.5
  • 15
    • 0026720235 scopus 로고
    • Characterization of four in vitro established canine mammary carcinoma and one atypical benign mixed tumour cell lines
    • Hellmén E. Characterization of four in vitro established canine mammary carcinoma and one atypical benign mixed tumour cell lines. In Vitro Cell. Dev. Biol. 28A (1992) 309-319
    • (1992) In Vitro Cell. Dev. Biol. , vol.28 A , pp. 309-319
    • Hellmén, E.1
  • 16
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod-A software tool for determining glycosylation compositions from mass spectrometric data
    • Cooper C.A., Gasteiger E., and Packer N. GlycoMod-A software tool for determining glycosylation compositions from mass spectrometric data. Proteomics 1 (2001) 340-349
    • (2001) Proteomics , vol.1 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.3
  • 19
  • 20
    • 17144430928 scopus 로고    scopus 로고
    • β1,6-Branched oligosaccharides are increased in lymph node metastases and predict poor outcome in breast carcinoma
    • Handerson T., Camp R., Harigopal M., Rimm D., and Pawelek J. β1,6-Branched oligosaccharides are increased in lymph node metastases and predict poor outcome in breast carcinoma. Clin. Cancer Res. 11 (2005) 2969-2973
    • (2005) Clin. Cancer Res. , vol.11 , pp. 2969-2973
    • Handerson, T.1    Camp, R.2    Harigopal, M.3    Rimm, D.4    Pawelek, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.