메뉴 건너뛰기




Volumn 19, Issue 12, 2014, Pages 20073-20090

Alteration of N-glycans and expression of their related glycogenes in the epithelial-mesenchymal transition of HCV29 bladder epithelial cells

Author keywords

Epithelial mesenchymal transition; Glycogene; Mass spectrometry; Microarray; N glycan

Indexed keywords

BIOLOGICAL MARKER; LECTIN; POLYSACCHARIDE; TRANSFORMING GROWTH FACTOR BETA;

EID: 84919779591     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules191220073     Document Type: Article
Times cited : (37)

References (49)
  • 1
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings, R.D. The repertoire of glycan determinants in the human glycome. Mol. Biosyst. 2009, 5, 1087-1104.
    • (2009) Mol. Biosyst. , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 2
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • Zaia, J. Mass spectrometry and the emerging field of glycomics. Chem. Biol. 2008, 15, 881-892.
    • (2008) Chem. Biol. , vol.15 , pp. 881-892
    • Zaia, J.1
  • 3
  • 4
    • 70349286075 scopus 로고    scopus 로고
    • Glycomic analysis: An array of technologies
    • Krishnamoorthy, L.; Mahal, L.K. Glycomic analysis: An array of technologies. ACS Chem. Biol. 2009, 4, 715-732.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 715-732
    • Krishnamoorthy, L.1    Mahal, L.K.2
  • 5
    • 33750620940 scopus 로고    scopus 로고
    • Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers
    • Drake, R.R.; Schwegler, E.E.; Malik, G.; Diaz, J.; Block, T.; Mehta, A.; Semmes, O.J. Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers. Mol. Cell. Proteomics 2006, 5, 1957-1967.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1957-1967
    • Drake, R.R.1    Schwegler, E.E.2    Malik, G.3    Diaz, J.4    Block, T.5    Mehta, A.6    Semmes, O.J.7
  • 9
    • 23944510667 scopus 로고    scopus 로고
    • Direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification of proteins on membrane detected by western blotting and lectin blotting
    • Ohtsu, I.; Nakanisi, T.; Furuta, M.; Ando, E.; Nishimura, O. Direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification of proteins on membrane detected by western blotting and lectin blotting. J. Proteome Res. 2005, 4, 1391-1396.
    • (2005) J. Proteome Res. , vol.4 , pp. 1391-1396
    • Ohtsu, I.1    Nakanisi, T.2    Furuta, M.3    Ando, E.4    Nishimura, O.5
  • 10
    • 84866487628 scopus 로고    scopus 로고
    • Improved lectin ELISA for glycosylation analysis of biomarkers using ps-tag-fused single-chain fv
    • Kumada, Y.; Ohigashi, Y.; Emori, Y.; Imamura, K.; Omura, Y.; Kishimoto, M. Improved lectin ELISA for glycosylation analysis of biomarkers using Ps-tag-fused single-chain Fv. J. Immunol. Methods 2012, 385, 15-22.
    • (2012) J. Immunol. Methods , vol.385 , pp. 15-22
    • Kumada, Y.1    Ohigashi, Y.2    Emori, Y.3    Imamura, K.4    Omura, Y.5    Kishimoto, M.6
  • 11
    • 29144488001 scopus 로고    scopus 로고
    • Predictive value of N-acetylglucosaminyltransferase-V for superficial bladder cancer recurrence
    • Takahashi, T.; Hagisawa, S.; Yoshikawa, K.; Tezuka, F.; Kaku, M.; Ohyama, C. Predictive value of N-acetylglucosaminyltransferase-V for superficial bladder cancer recurrence. J. Urol. 2006, 175, 90-93.
    • (2006) J. Urol. , vol.175 , pp. 90-93
    • Takahashi, T.1    Hagisawa, S.2    Yoshikawa, K.3    Tezuka, F.4    Kaku, M.5    Ohyama, C.6
  • 12
    • 33646388649 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase V and beta1-6 branching N-linked oligosaccharides are associated with good prognosis of patients with bladder cancer
    • Ishimura, H.; Takahashi, T.; Nakagawa, H.; Nishimura, S.; Arai, Y.; Horikawa, Y.; Habuchi, T.; Miyoshi, E.; Kyan, A.; Hagisawa, S.; et al. N-acetylglucosaminyltransferase V and beta1-6 branching N-linked oligosaccharides are associated with good prognosis of patients with bladder cancer. Clin. Cancer Res. 2006, 12, 2506-2511.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 2506-2511
    • Ishimura, H.1    Takahashi, T.2    Nakagawa, H.3    Nishimura, S.4    Arai, Y.5    Horikawa, Y.6    Habuchi, T.7    Miyoshi, E.8    Kyan, A.9    Hagisawa, S.10
  • 14
    • 0035895782 scopus 로고    scopus 로고
    • Novel functions of complex carbohydrates elucidated by the mutant mice of glycosyltransferase genes
    • Furukawa, K.; Takamiya, K.; Okada, M.; Inoue, M.; Fukumoto, S.; Furukawa, K. Novel functions of complex carbohydrates elucidated by the mutant mice of glycosyltransferase genes. Biochim. Biophys. Acta 2001, 1525, 1-12.
    • (2001) Biochim. Biophys. Acta , vol.1525 , pp. 1-12
    • Furukawa, K.1    Takamiya, K.2    Okada, M.3    Inoue, M.4    Fukumoto, S.5    Furukawa, K.6
  • 15
    • 0029989766 scopus 로고    scopus 로고
    • Possible roles of tumor-associated carbohydrate antigens
    • Fukuda, M. Possible roles of tumor-associated carbohydrate antigens. Cancer Res. 1996, 56, 2237-2244.
    • (1996) Cancer Res. , vol.56 , pp. 2237-2244
    • Fukuda, M.1
  • 16
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: New wine in an old bottle
    • Hakomori, S. Glycosylation defining cancer malignancy: New wine in an old bottle. Proc. Natl. Acad. Sci. USA 2002, 99, 10231-10233.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 17
    • 53049084874 scopus 로고    scopus 로고
    • N-glycans in cancer progression
    • Lau, K.S.; Dennis, J.W. N-glycans in cancer progression. Glycobiology 2008, 18, 750-760.
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 18
    • 84887914597 scopus 로고    scopus 로고
    • Bisected, complex N-glycans and galectins in mouse mammary tumor progression and human Breast cancer
    • Miwa, H.E.; Koba, W.R.; Fine, E.J.; Giricz, O.; Kenny, P.A.; Stanley, P. Bisected, complex N-glycans and galectins in mouse mammary tumor progression and human breast cancer. Glycobiology 2013, 23, 1477-1490.
    • (2013) Glycobiology , vol.23 , pp. 1477-1490
    • Miwa, H.E.1    Koba, W.R.2    Fine, E.J.3    Giricz, O.4    Kenny, P.A.5    Stanley, P.6
  • 19
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • Thiery, J.P.; Acloque, H.; Huang, R.Y.; Nieto, M.A. Epithelial-mesenchymal transitions in development and disease. Cell 2009, 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
  • 20
    • 79958779687 scopus 로고    scopus 로고
    • Scar wars: Mapping the fate of epithelial-mesenchymal-myofibroblast transition
    • Quaggin, S.E.; Kapus, A. Scar wars: Mapping the fate of epithelial-mesenchymal-myofibroblast transition. Kidney Int. 2011, 80, 41-50.
    • (2011) Kidney Int. , vol.80 , pp. 41-50
    • Quaggin, S.E.1    Kapus, A.2
  • 21
    • 67651005404 scopus 로고    scopus 로고
    • Emt: When epithelial cells decide to become mesenchymal-like cells
    • Kalluri, R. Emt: When epithelial cells decide to become mesenchymal-like cells. J. Clin. Investig. 2009, 119, 1417-1419.
    • (2009) J. Clin. Investig. , vol.119 , pp. 1417-1419
    • Kalluri, R.1
  • 22
    • 66149101390 scopus 로고    scopus 로고
    • Specific glycosphingolipids mediate epithelial-to-mesenchymal transition of human and mouse epithelial cell lines
    • Guan, F.; Handa, K.; Hakomori, S. Specific glycosphingolipids mediate epithelial-to-mesenchymal transition of human and mouse epithelial cell lines. Proc. Natl. Acad. Sci. USA 2009, 106, 7461-7466.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7461-7466
    • Guan, F.1    Handa, K.2    Hakomori, S.3
  • 23
    • 34447339656 scopus 로고    scopus 로고
    • Mgat5 and pten interact to regulate cell growth and polarity
    • Cheung, P.; Dennis, J.W. Mgat5 and Pten interact to regulate cell growth and polarity. Glycobiology 2007, 17, 767-773.
    • (2007) Glycobiology , vol.17 , pp. 767-773
    • Cheung, P.1    Dennis, J.W.2
  • 24
    • 84860879220 scopus 로고    scopus 로고
    • Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines
    • Xu, Q.; Isaji, T.; Lu, Y.; Gu, W.; Kondo, M.; Fukuda, T.; Du, Y.; Gu, J. Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines. J. Biol. Chem. 2012, 287, 16563-16574.
    • (2012) J. Biol. Chem. , vol.287 , pp. 16563-16574
    • Xu, Q.1    Isaji, T.2    Lu, Y.3    Gu, W.4    Kondo, M.5    Fukuda, T.6    Du, Y.7    Gu, J.8
  • 26
    • 0018177506 scopus 로고
    • Comparative studies on blood serum alpha-l-fucosidases from several mammalian species
    • Villar, E.; Calvo, P.; Cabezas, J.A. Comparative studies on blood serum alpha-l-fucosidases from several mammalian species. Comp. Biochem. Phys. B 1978, 60, 459-461.
    • (1978) Comp. Biochem. Phys. B , vol.60 , pp. 459-461
    • Villar, E.1    Calvo, P.2    Cabezas, J.A.3
  • 27
    • 2942545075 scopus 로고    scopus 로고
    • Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines
    • Przybylo, M.; Hoja-Lukowicz, D.; Litynska, A.; Laidler, P. Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines. Cancer Cell Int. 2002, doi: 10.1186/1475-2867-2-6.
    • (2002) Cancer Cell Int.
    • Przybylo, M.1    Hoja-Lukowicz, D.2    Litynska, A.3    Laidler, P.4
  • 28
  • 29
    • 14844297008 scopus 로고    scopus 로고
    • Different adhesion and migration properties of human HCV29 non-malignant urothelial and T24 bladder cancer cells: Role of glycosylation
    • Przybylo, M.; Litynska, A.; Pochec, E. Different adhesion and migration properties of human HCV29 non-malignant urothelial and T24 bladder cancer cells: Role of glycosylation. Biochimie 2005, 87, 133-142.
    • (2005) Biochimie , vol.87 , pp. 133-142
    • Przybylo, M.1    Litynska, A.2    Pochec, E.3
  • 30
    • 84902096317 scopus 로고    scopus 로고
    • Altered N-glycan expression profile in epithelial-to-mesenchymal transition of NMuMG cells revealed by an integrated strategy using mass spectrometry and glycogene and lectin microarray analysis
    • Tan, Z.; Lu, W.; Li, X.; Yang, G.; Guo, J.; Yu, H.; Li, Z.; Guan, F. Altered N-glycan expression profile in epithelial-to-mesenchymal transition of NMuMG cells revealed by an integrated strategy using mass spectrometry and glycogene and lectin microarray analysis. J. Proteome Res. 2014, 13, 2783-2795.
    • (2014) J. Proteome Res. , vol.13 , pp. 2783-2795
    • Tan, Z.1    Lu, W.2    Li, X.3    Yang, G.4    Guo, J.5    Yu, H.6    Li, Z.7    Guan, F.8
  • 33
    • 0141482211 scopus 로고    scopus 로고
    • Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry
    • Mechref, Y.; Novotny, M.V.; Krishnan, C. Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 2003, 75, 4895-4903.
    • (2003) Anal. Chem. , vol.75 , pp. 4895-4903
    • Mechref, Y.1    Novotny, M.V.2    Krishnan, C.3
  • 34
    • 0021873217 scopus 로고
    • Biosynthesis and modification of golgi mannosidase II in hela and 33 cells
    • Moremen, K.W.; Touster, O. Biosynthesis and modification of golgi mannosidase II in Hela and 33 cells. J. Biol. Chem. 1985, 260, 6654-6662.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6654-6662
    • Moremen, K.W.1    Touster, O.2
  • 35
    • 0025948387 scopus 로고
    • Novel purification of the catalytic domain of golgi alpha-mannosidase II. Characterization and comparison with the intact enzyme
    • Moremen, K.W.; Touster, O.; Robbins, P.W. Novel purification of the catalytic domain of golgi alpha-mannosidase II. Characterization and comparison with the intact enzyme. J. Biol. Chem. 1991, 266, 16876-16885.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16876-16885
    • Moremen, K.W.1    Touster, O.2    Robbins, P.W.3
  • 36
    • 0026325913 scopus 로고
    • Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a golgi enzyme that controls conversion of high mannose to complex N-glycans
    • Moremen, K.W.; Robbins, P.W. Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a golgi enzyme that controls conversion of high mannose to complex N-glycans. J. Cell Biol. 1991, 115, 1521-1534.
    • (1991) J. Cell Biol. , vol.115 , pp. 1521-1534
    • Moremen, K.W.1    Robbins, P.W.2
  • 37
    • 0029559787 scopus 로고
    • Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme
    • Misago, M.; Liao, Y.F.; Kudo, S.; Eto, S.; Mattei, M.G.; Moremen, K.W.; Fukuda, M.N. Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme. Proc. Natl. Acad. Sci. USA 1995, 92, 11766-11770.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11766-11770
    • Misago, M.1    Liao, Y.F.2    Kudo, S.3    Eto, S.4    Mattei, M.G.5    Moremen, K.W.6    Fukuda, M.N.7
  • 38
    • 0034871051 scopus 로고    scopus 로고
    • Congenital disorders involving defective N-glycosylation of proteins
    • Schachter, H. Congenital disorders involving defective N-glycosylation of proteins. Cell. Mol. Life Sci. 2001, 58, 1085-1104.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1085-1104
    • Schachter, H.1
  • 39
    • 0037137471 scopus 로고    scopus 로고
    • Golgi alpha-mannosidase II deficiency in vertebrate systems: Implications for asparagine-linked oligosaccharide processing in mammals
    • Moremen, K.W. Golgi alpha-mannosidase II deficiency in vertebrate systems: Implications for asparagine-linked oligosaccharide processing in mammals. Biochim. Biophys. Acta 2002, 1573, 225-235.
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 225-235
    • Moremen, K.W.1
  • 42
    • 67049095491 scopus 로고    scopus 로고
    • Comprehensive clinico-glycomic study of 16 colorectal cancer specimens: Elucidation of aberrant glycosylation and its mechanistic causes in colorectal cancer cells
    • Misonou, Y.; Shida, K.; Korekane, H.; Seki, Y.; Noura, S.; Ohue, M.; Miyamoto, Y. Comprehensive clinico-glycomic study of 16 colorectal cancer specimens: Elucidation of aberrant glycosylation and its mechanistic causes in colorectal cancer cells. J. Proteome Res. 2009, 8, 2990-3005.
    • (2009) J. Proteome Res. , vol.8 , pp. 2990-3005
    • Misonou, Y.1    Shida, K.2    Korekane, H.3    Seki, Y.4    Noura, S.5    Ohue, M.6    Miyamoto, Y.7
  • 44
    • 0024307863 scopus 로고
    • Mechanism of fibronectin-mediated cell migration: Dependence or independence of cell migration susceptibility on RGDS-directed receptor (integrin)
    • Straus, A.H.; Carter, W.G.; Wayner, E.A.; Hakomori, S. Mechanism of fibronectin-mediated cell migration: Dependence or independence of cell migration susceptibility on RGDS-directed receptor (integrin). Exp. Cell Res. 1989, 183, 126-139.
    • (1989) Exp. Cell Res. , vol.183 , pp. 126-139
    • Straus, A.H.1    Carter, W.G.2    Wayner, E.A.3    Hakomori, S.4
  • 45
    • 84868328596 scopus 로고    scopus 로고
    • Analysis of glycan-related genes expression and glycan profiles in mice with liver fibrosis
    • Yu, H.; Zhu, M.; Qin, Y.; Zhong, Y.; Yan, H.; Wang, Q.; Bian, H.; Li, Z. Analysis of glycan-related genes expression and glycan profiles in mice with liver fibrosis. J. Proteome Res. 2012, 11, 5277-5285.
    • (2012) J. Proteome Res. , vol.11 , pp. 5277-5285
    • Yu, H.1    Zhu, M.2    Qin, Y.3    Zhong, Y.4    Yan, H.5    Wang, Q.6    Bian, H.7    Li, Z.8
  • 46
    • 84862687423 scopus 로고    scopus 로고
    • Alteration of protein glycosylation in human hepatic stellate cells activated with transforming growth factor-β1
    • Qin, Y.; Zhong, Y.; Dang, L.; Zhu, M.; Yu, H.; Chen, W.; Cui, J.; Bian, H.; Li, Z. Alteration of protein glycosylation in human hepatic stellate cells activated with transforming growth factor-β1. J. Proteome Res. 2012, 75, 4114-4123.
    • (2012) J. Proteome Res. , vol.75 , pp. 4114-4123
    • Qin, Y.1    Zhong, Y.2    Dang, L.3    Zhu, M.4    Yu, H.5    Chen, W.6    Cui, J.7    Bian, H.8    Li, Z.9
  • 47
    • 84876474385 scopus 로고    scopus 로고
    • Selective isolation and analysis of glycoprotein fractions and their glycomes from hepatocellular carcinoma sera
    • Yang, G.; Cui, T.; Wang, Y.; Sun, S.; Ma, T.; Wang, T.; Chen, Q.; Li, Z. Selective isolation and analysis of glycoprotein fractions and their glycomes from hepatocellular carcinoma sera. Proteomics 2013, 13, 1481-1498.
    • (2013) Proteomics , vol.13 , pp. 1481-1498
    • Yang, G.1    Cui, T.2    Wang, Y.3    Sun, S.4    Ma, T.5    Wang, T.6    Chen, Q.7    Li, Z.8
  • 48
    • 4544341015 scopus 로고    scopus 로고
    • Linear models and empirical bayes methods for assessing differential expression in microarray experiments
    • Smyth, G.K. Linear models and empirical bayes methods for assessing differential expression in microarray experiments. Stat. Appl. Genet. Mol. 2004, doi: 10.2202/1544-6115.1027.
    • (2004) Stat. Appl. Genet. Mol.
    • Smyth, G.K.1
  • 49
    • 78649725167 scopus 로고    scopus 로고
    • Functional role of gangliotetraosylceramide in epithelial-to-mesenchymal transition process induced by hypoxia and by TGF-β
    • Guan, F.; Schaffer, L.; Handa, K.; Hakomori, S. Functional role of gangliotetraosylceramide in epithelial-to-mesenchymal transition process induced by hypoxia and by TGF-β. FASEB J. 2010, 24, 4889-4903.
    • (2010) FASEB J. , vol.24 , pp. 4889-4903
    • Guan, F.1    Schaffer, L.2    Handa, K.3    Hakomori, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.