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Volumn 68, Issue 6, 2011, Pages 1011-1020

Modulation of E-cadherin function and dysfunction by N-glycosylation

Author keywords

Cancer; Cell adhesion; E cadherin; Glycosyltransferases; N glycosylation

Indexed keywords

ALPHA 1,3(6) MANNOSYLGLYCOPROTEIN BETA 1,6 N ACETYLGLUCOSAMINYLTRANSFERASE; ALPHA1,6 FUCOSYLTRANSFERASE; GLYCOSYLTRANSFERASE; N ACETYLGLUCOSAMINYLTRANSFERASE; N ACETYLGLUCOSAMINYLTRANSFERASE III; UNCLASSIFIED DRUG; UVOMORULIN;

EID: 79953721653     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0595-0     Document Type: Review
Times cited : (134)

References (62)
  • 1
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • DOI 10.1038/nrm1699
    • BM Gumbiner 2005 Regulation of cadherin-mediated adhesion in morphogenesis Nat Rev Mol Cell Biol 6 622 634 1:CAS:528:DC%2BD2MXmvVGhtrk%3D 10.1038/nrm1699 16025097 (Pubitemid 41081266)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.8 , pp. 622-634
    • Gumbiner, B.M.1
  • 2
    • 0032102397 scopus 로고    scopus 로고
    • Structure-function analysis of cell adhesion by neural (N-) cadherin
    • DOI 10.1016/S0896-6273(00)80496-1
    • K Tamura WS Shan WA Hendrickson DR Colman L Shapiro 1998 Structure-function analysis of cell adhesion by neural (N-) cadherin Neuron 20 1153 1163 1:CAS:528:DyaK1cXktFOksLc%3D 10.1016/S0896-6273(00)80496-1 9655503 (Pubitemid 28293132)
    • (1998) Neuron , vol.20 , Issue.6 , pp. 1153-1163
    • Tamura, K.1    Shan, W.-S.2    Hendrickson, W.A.3    Colman, D.R.4    Shapiro, L.5
  • 3
    • 77954351636 scopus 로고    scopus 로고
    • Allosteric cross talk between cadherin extracellular domains
    • 1:CAS:528:DC%2BC3cXpsVWqtLc%3D 10.1016/j.bpj.2010.03.062 20655837
    • QM Shi V Maruthamuthu F Li D Leckband 2010 Allosteric cross talk between cadherin extracellular domains Biophys J 99 95 104 1:CAS:528: DC%2BC3cXpsVWqtLc%3D 10.1016/j.bpj.2010.03.062 20655837
    • (2010) Biophys J , vol.99 , pp. 95-104
    • Shi, Q.M.1    Maruthamuthu, V.2    Li, F.3    Leckband, D.4
  • 4
    • 42449110795 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by the cadherin-catenin complex
    • DOI 10.1042/BST0360149
    • WJ Nelson 2008 Regulation of cell-cell adhesion by the cadherin-catenin complex Biochem Soc Trans 36 149 155 1:CAS:528:DC%2BD1cXktVWkt74%3D 10.1042/BST0360149 18363555 (Pubitemid 351570584)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.2 , pp. 149-155
    • Nelson, W.J.1
  • 5
    • 38349138921 scopus 로고    scopus 로고
    • EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt
    • 1:CAS:528:DC%2BD1cXpvV2ltA%3D%3D 10.1073/pnas.0710504105 18093941
    • K Abe M Takeichi 2008 EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt Proc Natl Acad Sci U S A 105 13 19 1:CAS:528:DC%2BD1cXpvV2ltA%3D%3D 10.1073/pnas.0710504105 18093941
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 13-19
    • Abe, K.1    Takeichi, M.2
  • 6
    • 0031686121 scopus 로고    scopus 로고
    • Mutations of the human E-cadherin (CDH1) gene
    • DOI 10.1002/(SICI)1098-1004(1998)12:4<226::AID-HUMU2>3.0.CO;2-D
    • G Berx KF Becker H Hofler RF van 1998 Mutations of the human E-cadherin (CDH1) gene Hum Mutat 12 226 237 1:CAS:528:DyaK1cXmtFWqsr8%3D 10.1002/(SICI)1098-1004(1998)12:4<226::AID-HUMU2>3.0.CO;2-D 9744472 (Pubitemid 28418891)
    • (1998) Human Mutation , vol.12 , Issue.4 , pp. 226-237
    • Berx, G.1    Becker, K.-F.2    Hofler, H.3    Van Roy, F.4
  • 8
    • 63849130585 scopus 로고    scopus 로고
    • Role of the epithelial-mesenchymal transition regulator Slug in primary human cancers
    • 10.2741/3433 19273255
    • CC Alves F Carneiro H Hoefler KF Becker 2009 Role of the epithelial-mesenchymal transition regulator Slug in primary human cancers Front Biosci 14 3035 3050 10.2741/3433 19273255
    • (2009) Front Biosci , vol.14 , pp. 3035-3050
    • Alves, C.C.1    Carneiro, F.2    Hoefler, H.3    Becker, K.F.4
  • 10
    • 0034681430 scopus 로고    scopus 로고
    • Casein kinase II phosphorylation of E-cadherin increases E-cadherin/β- catenin interaction and strengthens cell-cell adhesion
    • DOI 10.1074/jbc.275.7.5090
    • H Lickert A Bauer R Kemler J Stappert 2000 Casein kinase II phosphorylation of E-cadherin increases E-cadherin/β-catenin interaction and strengthens cell-cell adhesion J Biol Chem 275 5090 5095 1:CAS:528:DC%2BD3cXhsVymtr8%3D 10.1074/jbc.275.7.5090 10671552 (Pubitemid 30108909)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 5090-5095
    • Lickert, H.1    Bauer, A.2    Kemler, R.3    Stappert, J.4
  • 11
    • 0035503219 scopus 로고    scopus 로고
    • Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis
    • DOI 10.1093/emboj/20.21.5999
    • W Zhu B Leber DW Andrews 2001 Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis EMBO J 20 5999 6007 1:CAS:528:DC%2BD3MXovVSitL4%3D 10.1093/emboj/20.21.5999 11689440 (Pubitemid 33049275)
    • (2001) EMBO Journal , vol.20 , Issue.21 , pp. 5999-6007
    • Zhu, W.1    Leber, B.2    Andrews, D.W.3
  • 12
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • R Kornfeld S Kornfeld 1985 Assembly of asparagine-linked oligosaccharides Annu Rev Biochem 54 631 664 1:STN:280:DyaL2M3nvVSjsA%3D%3D 10.1146/annurev.bi. 54.070185.003215 3896128 (Pubitemid 15073660)
    • (1985) Annual Review of Biochemistry , vol.VOL. 54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 13
    • 58949097354 scopus 로고    scopus 로고
    • Role of E-cadherin N-glycosylation profile in a mammary tumor model
    • 1:CAS:528:DC%2BD1MXhs1anu7k%3D 10.1016/j.bbrc.2009.01.024 19159617
    • SS Pinho H Osorio M Nita-Lazar J Gomes C Lopes F Gartner CA Reis 2009 Role of E-cadherin N-glycosylation profile in a mammary tumor model Biochem Biophys Res Commun 379 1091 1096 1:CAS:528:DC%2BD1MXhs1anu7k%3D 10.1016/j.bbrc.2009.01.024 19159617
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 1091-1096
    • Pinho, S.S.1    Osorio, H.2    Nita-Lazar, M.3    Gomes, J.4    Lopes, C.5    Gartner, F.6    Reis, C.A.7
  • 14
    • 0028012014 scopus 로고
    • Mice lacking N-acetylglucosaminyltransferase i activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates
    • 1:CAS:528:DyaK2cXhtlWnsLY%3D 10.1073/pnas.91.2.728 8290590
    • E Ioffe P Stanley 1994 Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates Proc Natl Acad Sci U S A 91 728 732 1:CAS:528: DyaK2cXhtlWnsLY%3D 10.1073/pnas.91.2.728 8290590
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 728-732
    • Ioffe, E.1    Stanley, P.2
  • 15
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • DOI 10.1038/nrg1894, PII N1894
    • HH Freeze 2006 Genetic defects in the human glycome Nat Rev Genet 7 537 551 1:CAS:528:DC%2BD28XlvVGltL4%3D 10.1038/nrg1894 16755287 (Pubitemid 43943571)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.7 , pp. 537-551
    • Freeze, H.H.1
  • 16
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • A Varki 1993 Biological roles of oligosaccharides: all of the theories are correct Glycobiology 3 97 130 1:CAS:528:DyaK3sXlsFCju7k%3D 10.1093/glycob/3.2.97 8490246 (Pubitemid 23132602)
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 97-130
    • Varki, A.1
  • 17
    • 53849109165 scopus 로고    scopus 로고
    • Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD
    • 1:CAS:528:DC%2BD1cXht1equrfE 10.1007/s10719-008-9133-9 18491227
    • F Zhou J Su L Fu Y Yang L Zhang L Wang H Zhao D Zhang Z Li X Zha 2008 Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD Glycoconj J 25 727 740 1:CAS:528:DC%2BD1cXht1equrfE 10.1007/s10719-008- 9133-9 18491227
    • (2008) Glycoconj J , vol.25 , pp. 727-740
    • Zhou, F.1    Su, J.2    Fu, L.3    Yang, Y.4    Zhang, L.5    Wang, L.6    Zhao, H.7    Zhang, D.8    Li, Z.9    Zha, X.10
  • 18
    • 46449101373 scopus 로고    scopus 로고
    • N-glycosylation affects the adhesive function of E-cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435
    • 1:CAS:528:DC%2BD1cXhtFant77M 10.1002/jcb.21608 17979184
    • H Zhao Y Liang Z Xu L Wang F Zhou Z Li J Jin Y Yang Z Fang Y Hu L Zhang J Su X Zha 2008 N-glycosylation affects the adhesive function of E-cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435 J Cell Biochem 104 162 175 1:CAS:528: DC%2BD1cXhtFant77M 10.1002/jcb.21608 17979184
    • (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
  • 19
    • 33747377812 scopus 로고    scopus 로고
    • N-glycosylation affects the molecular organization and stability of E-cadherin junctions
    • 1:CAS:528:DC%2BD28XnvVWjtb4%3D 10.1074/jbc.M512621200 16682414
    • A Liwosz T Lei MA Kukuruzinska 2006 N-glycosylation affects the molecular organization and stability of E-cadherin junctions J Biol Chem 281 23138 23149 1:CAS:528:DC%2BD28XnvVWjtb4%3D 10.1074/jbc.M512621200 16682414
    • (2006) J Biol Chem , vol.281 , pp. 23138-23149
    • Liwosz, A.1    Lei, T.2    Kukuruzinska, M.A.3
  • 20
    • 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
    • 1:CAS:528:DC%2BD1cXnsFCmtQ%3D%3D 10.1074/jbc.M704713200 18025087
    • O Vagin E Tokhtaeva I Yakubov E Shevchenko G Sachs 2008 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 2192 2202 1:CAS:528:DC%2BD1cXnsFCmtQ%3D%3D 10.1074/jbc.M704713200 18025087
    • (2008) J Biol Chem , vol.283 , pp. 2192-2202
    • Vagin, O.1    Tokhtaeva, E.2    Yakubov, I.3    Shevchenko, E.4    Sachs, G.5
  • 21
    • 0020373041 scopus 로고
    • Control of glycoprotein synthesis. UDP-GlcNac:Glycopeptide β4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β1-4 linkage to the β-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides
    • S Narasimhan 1982 Control of glycoprotein synthesis. UDP-GlcNAc: glycopeptide β 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β 1-4 linkage to the β-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides J Biol Chem 257 10235 10242 1:CAS:528:DyaL38XmtFWitr4%3D 6213618 (Pubitemid 13251022)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.17 , pp. 10235-10242
    • Narasimhan, S.1
  • 22
    • 0024117227 scopus 로고
    • The biosynthesis of highly branched N-glycans: Studies on the sequential pathway and functional role of N-acetylglucosaminyltransferases I, II, III, IV, v and VI
    • 1:CAS:528:DyaL1MXhsFSitLk%3D 10.1016/0300-9084(88)90289-1 2977290
    • I Brockhausen S Narasimhan H Schachter 1988 The biosynthesis of highly branched N-glycans: studies on the sequential pathway and functional role of N-acetylglucosaminyltransferases I, II, III, IV, V and VI Biochimie 70 1521 1533 1:CAS:528:DyaL1MXhsFSitLk%3D 10.1016/0300-9084(88)90289-1 2977290
    • (1988) Biochimie , vol.70 , pp. 1521-1533
    • Brockhausen, I.1    Narasimhan, S.2    Schachter, H.3
  • 24
    • 33749045903 scopus 로고    scopus 로고
    • Decoding sugar functions by identifying target glycoproteins
    • DOI 10.1016/j.sbi.2006.08.011, PII S0959440X06001461, Carbohydrates and Glycoconjugates / Biophysical Methods
    • N Taniguchi E Miyoshi J Gu K Honke A Matsumoto 2006 Decoding sugar functions by identifying target glycoproteins Curr Opin Struct Biol 16 561 566 1:CAS:528:DC%2BD28XhtVagtrjE 10.1016/j.sbi.2006.08.011 16971114 (Pubitemid 44466412)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 561-566
    • Taniguchi, N.1    Miyoshi, E.2    Jianguo, G.3    Honke, K.4    Matsumoto, A.5
  • 25
    • 0032869011 scopus 로고    scopus 로고
    • Implication of N-acetylglucosaminyltransferases III and V in cancer: Gene regulation and signaling mechanism
    • DOI 10.1016/S0925-4439(99)00066-6, PII S0925443999000666
    • N Taniguchi E Miyoshi JH Ko Y Ikeda Y Ihara 1999 Implication of N-acetylglucosaminyltransferases III and V in cancer: gene regulation and signaling mechanism Biochim Biophys Acta 1455 287 300 1:CAS:528: DyaK1MXntlOhu7Y%3D 10571019 (Pubitemid 29435995)
    • (1999) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1455 , Issue.2-3 , pp. 287-300
    • Taniguchi, N.1    Miyoshi, E.2    Ko, J.H.3    Ikeda, Y.4    Ihara, Y.5
  • 26
    • 0030480250 scopus 로고    scopus 로고
    • Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism
    • S Hakomori 1996 Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism Cancer Res 56 5309 5318 1:CAS:528: DyaK28Xntl2mtr4%3D 8968075 (Pubitemid 27011703)
    • (1996) Cancer Research , vol.56 , Issue.23 , pp. 5309-5318
    • Hakomori, S.-I.1
  • 28
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection
    • 1:CAS:528:DyaK2MXotVGqs78%3D 10.1073/pnas.92.19.8754 7568011
    • M Yoshimura A Nishikawa Y Ihara S Taniguchi N Taniguchi 1995 Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection Proc Natl Acad Sci U S A 92 8754 8758 1:CAS:528: DyaK2MXotVGqs78%3D 10.1073/pnas.92.19.8754 7568011
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8754-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Taniguchi, S.4    Taniguchi, N.5
  • 29
    • 0029786915 scopus 로고    scopus 로고
    • Characterization of cis-acting elements of the gene for macrophage- stimulating protein from the human. The involvement of positive and negative regulatory elements
    • DOI 10.1074/jbc.271.34.20265
    • M Yoshimura Y Ihara Y Matsuzawa N Taniguchi 1996 Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis J Biol Chem 271 13811 13815 1:CAS:528:DyaK28XjsVOjs7k%3D 10.1074/jbc.271.34.20265 8662832 (Pubitemid 26281791)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20265-20272
    • Ueda, A.1    Yoshimura, T.2
  • 31
    • 2442450486 scopus 로고    scopus 로고
    • 1 Reduces Ligand Binding and Down-regulates Cell Adhesion and Cell Migration
    • DOI 10.1074/jbc.M311627200
    • T Isaji J Gu R Nishiuchi Y Zhao M Takahashi E Miyoshi K Honke K Sekiguchi N Taniguchi 2004 Introduction of bisecting GlcNAc into integrin α5β1 reduces ligand binding and down-regulates cell adhesion and cell migration J Biol Chem 279 19747 19754 1:CAS:528:DC%2BD2cXjs1WitrY%3D 10.1074/jbc.M311627200 14998999 (Pubitemid 38623413)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 19747-19754
    • Isaji, T.1    Gu, J.2    Nishiuchi, R.3    Zhao, Y.4    Takahashi, M.5    Miyoshi, E.6    Honke, K.7    Sekiguchi, K.8    Taniguchi, N.9
  • 32
    • 66449112293 scopus 로고    scopus 로고
    • An N-glycosylation site on the β-propeller domain of the integrin α5 subunit plays key roles in both its function and site-specific modification by β1, 4-N-acetylglucosaminyltransferase III
    • 1:CAS:528:DC%2BD1MXltVCmt7k%3D 10.1074/jbc.M807660200 19276077
    • Y Sato T Isaji M Tajiri S Yoshida-Yamamoto T Yoshinaka T Somehara T Fukuda Y Wada J Gu 2009 An N-glycosylation site on the β-propeller domain of the integrin α5 subunit plays key roles in both its function and site-specific modification by β1, 4-N-acetylglucosaminyltransferase III J Biol Chem 284 11873 11881 1:CAS:528:DC%2BD1MXltVCmt7k%3D 10.1074/jbc.M807660200 19276077
    • (2009) J Biol Chem , vol.284 , pp. 11873-11881
    • Sato, Y.1    Isaji, T.2    Tajiri, M.3    Yoshida-Yamamoto, S.4    Yoshinaka, T.5    Somehara, T.6    Fukuda, T.7    Wada, Y.8    Gu, J.9
  • 33
  • 34
    • 33744958178 scopus 로고    scopus 로고
    • Cell-cell interaction-dependent regulation of N- acetylglucosaminyltransferase III and the bisected N-glycans in GE11 epithelial cells: Involvement of E-cadherin-mediated cell adhesion
    • DOI 10.1074/jbc.M601961200
    • J Iijima Y Zhao T Isaji A Kameyama S Nakaya X Wang H Ihara X Cheng T Nakagawa E Miyoshi A Kondo H Narimatsu N Taniguchi J Gu 2006 Cell-cell interaction-dependent regulation of N-acetylglucosaminyltransferase III and the bisected N-glycans in GE11 epithelial cells. Involvement of E-cadherin-mediated cell adhesion J Biol Chem 281 13038 13046 1:CAS:528:DC%2BD28Xkt1ymsrw%3D 10.1074/jbc.M601961200 16537539 (Pubitemid 43855213)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13038-13046
    • Iijima, J.1    Zhao, Y.2    Isaji, T.3    Kameyama, A.4    Nakaya, S.5    Wang, X.6    Ihara, H.7    Cheng, X.8    Nakagawa, T.9    Miyoshi, E.10    Kondo, A.11    Narimatsu, H.12    Taniguchi, N.13    Gu, J.14
  • 35
    • 61849083675 scopus 로고    scopus 로고
    • A mutual regulation between cell-cell adhesion and N-glycosylation: Implication of the bisecting GlcNAc for biological functions
    • 1:CAS:528:DC%2BD1cXhsVKis7zO 10.1021/pr800674g 19053837
    • J Gu Y Sato Y Kariya T Isaji N Taniguchi T Fukuda 2009 A mutual regulation between cell-cell adhesion and N-glycosylation: implication of the bisecting GlcNAc for biological functions J Proteome Res 8 431 435 1:CAS:528:DC%2BD1cXhsVKis7zO 10.1021/pr800674g 19053837
    • (2009) J Proteome Res , vol.8 , pp. 431-435
    • Gu, J.1    Sato, Y.2    Kariya, Y.3    Isaji, T.4    Taniguchi, N.5    Fukuda, T.6
  • 36
    • 50449107493 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin-catenin-actin complex
    • 1:CAS:528:DC%2BD1cXhtVGqs7%2FM 10.1002/pmic.200800038 18690644
    • R Akama Y Sato Y Kariya T Isaji T Fukuda L Lu N Taniguchi M Ozawa J Gu 2008 N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin-catenin-actin complex Proteomics 8 3221 3228 1:CAS:528:DC%2BD1cXhtVGqs7%2FM 10.1002/pmic.200800038 18690644
    • (2008) Proteomics , vol.8 , pp. 3221-3228
    • Akama, R.1    Sato, Y.2    Kariya, Y.3    Isaji, T.4    Fukuda, T.5    Lu, L.6    Taniguchi, N.7    Ozawa, M.8    Gu, J.9
  • 37
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: New wine in an old bottle
    • 1:CAS:528:DC%2BD38Xmt1CitL4%3D 10.1073/pnas.172380699 12149519
    • S Hakomori 2002 Glycosylation defining cancer malignancy: new wine in an old bottle Proc Natl Acad Sci U S A 99 10231 10233 1:CAS:528: DC%2BD38Xmt1CitL4%3D 10.1073/pnas.172380699 12149519
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 38
    • 0036894568 scopus 로고    scopus 로고
    • 1 integrin clustering and stimulates cell migration
    • HB Guo I Lee M Kamar SK Akiyama M Pierce 2002 Aberrant N-glycosylation of β1 integrin causes reduced α5β1 integrin clustering and stimulates cell migration Cancer Res 62 6837 6845 1:CAS:528:DC%2BD38XpsVahs7w%3D 12460896 (Pubitemid 35424070)
    • (2002) Cancer Research , vol.62 , Issue.23 , pp. 6837-6845
    • Guo, H.-B.1    Lee, I.2    Kamar, M.3    Akiyama, S.K.4    Pierce, M.5
  • 39
    • 0347993082 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase V Expression Levels Regulate Cadherin-associated Homotypic Cell-Cell Adhesion and Intracellular Signaling Pathways
    • DOI 10.1074/jbc.M308837200
    • HB Guo I Lee M Kamar M Pierce 2003 N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways J Biol Chem 278 52412 52424 1:CAS:528:DC%2BD3sXpvFGjsr0%3D 10.1074/jbc.M308837200 14561752 (Pubitemid 38035833)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52412-52424
    • Guo, H.-B.1    Lee, I.2    Kamar, M.3    Pierce, M.4
  • 40
    • 71749112448 scopus 로고    scopus 로고
    • Regulation of homotypic cell-cell adhesion by branched N-glycosylation of N-cadherin extracellular EC2 and EC3 domains
    • 1:CAS:528:DC%2BD1MXhsFWitbzM 10.1074/jbc.M109.060806 19846557
    • HB Guo H Johnson M Randolph M Pierce 2009 Regulation of homotypic cell-cell adhesion by branched N-glycosylation of N-cadherin extracellular EC2 and EC3 domains J Biol Chem 284 34986 34997 1:CAS:528:DC%2BD1MXhsFWitbzM 10.1074/jbc.M109.060806 19846557
    • (2009) J Biol Chem , vol.284 , pp. 34986-34997
    • Guo, H.B.1    Johnson, H.2    Randolph, M.3    Pierce, M.4
  • 41
    • 0027422524 scopus 로고
    • A collaborative study for the evaluation of lectin-reactive α- fetoproteins in early detection of hepatocellular carcinoma
    • K Taketa Y Endo C Sekiya K Tanikawa T Koji H Taga S Satomura S Matsuura T Kawai H Hirai 1993 A collaborative study for the evaluation of lectin-reactive α-fetoproteins in early detection of hepatocellular carcinoma Cancer Res 53 5419 5423 1:CAS:528:DyaK2cXltFCjsg%3D%3D 7693340 (Pubitemid 23342160)
    • (1993) Cancer Research , vol.53 , Issue.22 , pp. 5419-5423
    • Taketa, K.1    Endo, Y.2    Sekiya, C.3    Tanikawa, K.4    Koji, T.5    Taga, H.6    Satomura, S.7    Matsuura, S.8    Kawai, T.9    Hirai, H.10
  • 42
    • 0030612615 scopus 로고    scopus 로고
    • Expression of α1-6 fucosyltransferase in rat tissues and human cancer cell lines
    • DOI 10.1002/(SICI)1097-0215(19970917)72:6<1117::AID-IJC29>3.0.CO;2- #
    • E Miyoshi N Uozumi K Noda N Hayashi M Hori N Taniguchi 1997 Expression of α1-6 fucosyltransferase in rat tissues and human cancer cell lines Int J Cancer 72 1117 1121 1:CAS:528:DyaK2sXmsFahsrc%3D 10.1002/(SICI)1097- 0215(19970917)72:6<1117::AID-IJC29>3.0.CO;2-# 9378548 (Pubitemid 27433580)
    • (1997) International Journal of Cancer , vol.72 , Issue.6 , pp. 1117-1121
    • Miyoshi, E.1    Uozumi, N.2    Noda, K.3    Hayashi, N.4    Hori, M.5    Taniguchi, N.6
  • 45
    • 56949098199 scopus 로고    scopus 로고
    • E-cadherin core fucosylation regulates nuclear β-catenin accumulation in lung cancer cells
    • 1:CAS:528:DC%2BD1cXhsVagt7rK 10.1007/s10719-008-9144-6 18553167
    • P Hu B Shi F Geng C Zhang W Wu XZ Wu 2008 E-cadherin core fucosylation regulates nuclear β-catenin accumulation in lung cancer cells Glycoconj J 25 843 850 1:CAS:528:DC%2BD1cXhsVagt7rK 10.1007/s10719-008-9144-6 18553167
    • (2008) Glycoconj J , vol.25 , pp. 843-850
    • Hu, P.1    Shi, B.2    Geng, F.3    Zhang, C.4    Wu, W.5    Wu, X.Z.6
  • 46
    • 16644368317 scopus 로고    scopus 로고
    • The expression of core fucosylated E-cadherin in cancer cells and lung cancer patients: Prognostic implications
    • DOI 10.1038/sj.cr.7290243, PII 7290243
    • F Geng BZ Shi YF Yuan XZ Wu 2004 The expression of core fucosylated E-cadherin in cancer cells and lung cancer patients: prognostic implications Cell Res 14 423 433 1:CAS:528:DC%2BD2MXhsFektL0%3D 10.1038/sj.cr.7290243 15538974 (Pubitemid 43231805)
    • (2004) Cell Research , vol.14 , Issue.5 , pp. 423-433
    • Geng, F.1    Shi, B.Z.2    Yuan, Y.F.3    Wu, X.Z.4
  • 47
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • DOI 10.1126/science.291.5512.2364
    • A Helenius M Aebi 2001 Intracellular functions of N-linked glycans Science 291 2364 2369 1:CAS:528:DC%2BD3MXit1KnsLw%3D 10.1126/science.291.5512. 2364 11269317 (Pubitemid 32231791)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 48
    • 19744364877 scopus 로고    scopus 로고
    • A hypomorphic allele of the first N-glycosylation gene, ALG7, causes mitochondrial defects in yeast
    • DOI 10.1016/j.bbagen.2005.01.017, PII S0304416505000292
    • RD Mendelsohn EJ Helmerhorst JF Cipollo MA Kukuruzinska 2005 A hypomorphic allele of the first N-glycosylation gene, ALG7, causes mitochondrial defects in yeast Biochim Biophys Acta 1723 33 44 1:CAS:528:DC%2BD2MXks1GhsLs%3D 15794922 (Pubitemid 40744669)
    • (2005) Biochimica et Biophysica Acta - General Subjects , vol.1723 , Issue.1-3 , pp. 33-44
    • Mendelsohn, R.D.1    Helmerhorst, E.J.2    Cipollo, J.F.3    Kukuruzinska, M.A.4
  • 49
    • 0041591139 scopus 로고    scopus 로고
    • Deficiency of UDP-GlcNac:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij
    • DOI 10.1002/humu.10239
    • X Wu JS Rush D Karaoglu D Krasnewich MS Lubinsky CJ Waechter R Gilmore HH Freeze 2003 Deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type ij Hum Mutat 22 144 150 1:CAS:528:DC%2BD3sXms1Cks78%3D 10.1002/humu.10239 12872255 (Pubitemid 36950812)
    • (2003) Human Mutation , vol.22 , Issue.2 , pp. 144-150
    • Wu, X.1    Rush, J.S.2    Karaoglu, D.3    Krasnewich, D.4    Lubinsky, M.S.5    Waechter, C.J.6    Gilmore, R.7    Freeze, H.H.8
  • 51
    • 67650999377 scopus 로고    scopus 로고
    • Overexpression of DPAGT1 leads to aberrant N-glycosylation of E-cadherin and cellular discohesion in oral cancer
    • 1:CAS:528:DC%2BD1MXosV2ms70%3D 10.1158/0008-5472.CAN-08-4512 19549906
    • M Nita-Lazar V Noonan I Rebustini J Walker AS Menko MA Kukuruzinska 2009 Overexpression of DPAGT1 leads to aberrant N-glycosylation of E-cadherin and cellular discohesion in oral cancer Cancer Res 69 5673 5680 1:CAS:528: DC%2BD1MXosV2ms70%3D 10.1158/0008-5472.CAN-08-4512 19549906
    • (2009) Cancer Res , vol.69 , pp. 5673-5680
    • Nita-Lazar, M.1    Noonan, V.2    Rebustini, I.3    Walker, J.4    Menko, A.S.5    Kukuruzinska, M.A.6
  • 52
    • 77953232964 scopus 로고    scopus 로고
    • Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions
    • 1:CAS:528:DC%2BC3cXmslCrtrg%3D 10.1016/j.yexcr.2010.02.008 20156436
    • M Nita-Lazar I Rebustini J Walker MA Kukuruzinska 2010 Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions Exp Cell Res 316 1871 1884 1:CAS:528: DC%2BC3cXmslCrtrg%3D 10.1016/j.yexcr.2010.02.008 20156436
    • (2010) Exp Cell Res , vol.316 , pp. 1871-1884
    • Nita-Lazar, M.1    Rebustini, I.2    Walker, J.3    Kukuruzinska, M.A.4
  • 53
    • 0030884451 scopus 로고    scopus 로고
    • Purification and characterization of UDP-N-acetylglucosamine: α1,3-D- mannoside β1,4-N-acetylglucosaminyltransferase (N- acetylglucosaminyltransferase-IV) from bovine small intestine
    • DOI 10.1074/jbc.272.36.22721
    • S Oguri MT Minowa Y Ihara N Taniguchi H Ikenaga M Takeuchi 1997 Purification and characterization of UDP-N-acetylglucosamine: α1, 3-D-mannoside β1, 4-N-acetylglucosaminyltransferase (N- acetylglucosaminyltransferase-IV) from bovine small intestine J Biol Chem 272 22721 22727 1:CAS:528:DyaK2sXlvFGitbk%3D 10.1074/jbc.272.36.22721 9278430 (Pubitemid 27386089)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.36 , pp. 22721-22727
    • Oguri, S.1    Minowa, M.T.2    Ihara, Y.3    Taniguchi, N.4    Ikenaga, H.5    Takeuchi, M.6
  • 54
    • 0033566771 scopus 로고    scopus 로고
    • Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: A possible enzymatic basis of the formation of abnormal biantennary sugar chain
    • S Takamatsu S Oguri MT Minowa A Yoshida K Nakamura M Takeuchi A Kobata 1999 Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: a possible enzymatic basis of the formation of abnormal biantennary sugar chain Cancer Res 59 3949 3953 1:CAS:528: DyaK1MXlsVOltL8%3D 10463590 (Pubitemid 29393560)
    • (1999) Cancer Research , vol.59 , Issue.16 , pp. 3949-3953
    • Takamatsu, S.1    Oguri, S.2    Minowa, M.T.3    Yoshida, A.4    Nakamura, K.5    Takeuchi, M.6    Kobata, A.7
  • 57
    • 4344590221 scopus 로고    scopus 로고
    • Relations of the type and branch of surface N-glycans to cell adhesion, migration and integrin expressions
    • DOI 10.1023/B:MCBI.0000026065.84798.62
    • Y Zhang JH Zhao XY Zhang HB Guo F Liu HL Chen 2004 Relations of the type and branch of surface N-glycans to cell adhesion, migration and integrin expressions Mol Cell Biochem 260 137 146 1:CAS:528:DC%2BD2cXjsFSmtbY%3D 10.1023/B:MCBI.0000026065.84798.62 15228095 (Pubitemid 39127581)
    • (2004) Molecular and Cellular Biochemistry , vol.260 , Issue.1 , pp. 137-146
    • Zhang, Y.1    Zhao, J.2    Zhang, X.3    Guo, H.4    Liu, F.5    Chen, H.-L.6
  • 58
    • 0032714568 scopus 로고    scopus 로고
    • Importance of glycosidases in mammalian glycoprotein biosynthesis
    • 1:CAS:528:DyaK1MXnsVKmtL4%3D 10580131
    • A Herscovics 1999 Importance of glycosidases in mammalian glycoprotein biosynthesis Biochim Biophys Acta 1473 96 107 1:CAS:528:DyaK1MXnsVKmtL4%3D 10580131
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 96-107
    • Herscovics, A.1
  • 59
    • 0037137471 scopus 로고    scopus 로고
    • Golgi α-mannosidase II deficiency in vertebrate systems: Implications for asparagine-linked oligosaccharide processing in mammals
    • DOI 10.1016/S0304-4165(02)00388-4, PII S0304416502003884
    • KW Moremen 2002 Golgi α-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals Biochim Biophys Acta 1573 225 235 1:CAS:528:DC%2BD38Xotl2gtr4%3D 12417404 (Pubitemid 35335432)
    • (2002) Biochimica et Biophysica Acta - General Subjects , vol.1573 , Issue.3 , pp. 225-235
    • Moremen, K.W.1
  • 60
    • 0035875663 scopus 로고    scopus 로고
    • Structure of Golgi α-mannosidase II: A target for inhibition of growth and metastasis of cancer cells
    • DOI 10.1093/emboj/20.12.3008
    • JM van den Elsen DA Kuntz DR Rose 2001 Structure of Golgi alpha-mannosidase II: a target for inhibition of growth and metastasis of cancer cells EMBO J 20 3008 3017 10.1093/emboj/20.12.3008 11406577 (Pubitemid 32611988)
    • (2001) EMBO Journal , vol.20 , Issue.12 , pp. 3008-3017
    • Van Den Elsen, J.M.H.1    Kuntz, D.A.2    Rose, D.R.3
  • 61
    • 0020469388 scopus 로고
    • Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase II
    • DR Tulsiani TM Harris O Touster 1982 Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase II J Biol Chem 257 7936 7939 1:CAS:528:DyaL38XkvVKksLk%3D 6806288 (Pubitemid 13241215)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.14 , pp. 7936-7939
    • Tulsiani, D.R.P.1    Harris, T.M.2    Touster, O.3
  • 62
    • 0030878261 scopus 로고    scopus 로고
    • Phase IB clinical trial of the oligosaccharide processing inhibitor swainsonine in patients with advanced malignancies
    • PE Goss CL Reid D Bailey JW Dennis 1997 Phase IB clinical trial of the oligosaccharide processing inhibitor swainsonine in patients with advanced malignancies Clin Cancer Res 3 1077 1086 1:CAS:528:DyaK2sXkvFCgs7c%3D 9815786 (Pubitemid 27319753)
    • (1997) Clinical Cancer Research , vol.3 , Issue.7 , pp. 1077-1086
    • Goss, P.E.1    Reid, C.L.2    Bailey, D.3    Dennis, J.W.4


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