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Volumn 22, Issue 5, 2012, Pages 638-648

Deoxycholic acid impairs glycosylation and fucosylation processes in esophageal epithelial cells

Author keywords

Barrett's esophagus; bile acid; E cadherin; esophageal cancer; glycosylation

Indexed keywords

ALPHA METHYL MANNOSIDE; BILE ACID; CELL SURFACE PROTEIN; CONCANAVALIN A; DEOXYCHOLIC ACID; FUCOSE; GLYCAN; LITHOCHOLIC ACID; N ACETYLGLUCOSAMINE; PEANUT AGGLUTININ; TUNICAMYCIN; UVOMORULIN; WHEAT GERM AGGLUTININ;

EID: 84859088074     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr190     Document Type: Article
Times cited : (20)

References (45)
  • 1
    • 0033398025 scopus 로고    scopus 로고
    • Barrett's esophagus: An overview of the molecular biology
    • Aldulaimi D, Jankowski J. 1999. Barrett's esophagus: An overview of the molecular biology. Dis Esophagus. 12:177-180
    • (1999) Dis Esophagus. , vol.12 , pp. 177-180
    • Aldulaimi, D.1    Jankowski, J.2
  • 3
    • 39349083349 scopus 로고    scopus 로고
    • A highly sensitive assay for monitoring the secretory pathway and ER stress
    • Badr CE, Hewett JW, Breakefield XO, Tannous BA. 2007. A highly sensitive assay for monitoring the secretory pathway and ER stress. PLoS One. 2: e571.
    • (2007) PLoS One. , vol.2
    • Badr, C.E.1    Hewett, J.W.2    Breakefield, X.O.3    Tannous, B.A.4
  • 4
    • 0031984835 scopus 로고    scopus 로고
    • Altered cadherin and catenin complexes in the Barrett's esophagus-dysplasia-adenocarcinoma sequence: Correlation with disease progression and dedifferentiation
    • Bailey T, Biddlestone L, Shepherd N, Barr H, Warner P, Jankowski J. 1998. Altered cadherin and catenin complexes in the Barrett's esophagus-dysplasia- adenocarcinoma sequence: Correlation with disease progression and dedifferentiation. Am J Pathol. 152:135-144
    • (1998) Am J Pathol. , vol.152 , pp. 135-144
    • Bailey, T.1    Biddlestone, L.2    Shepherd, N.3    Barr, H.4    Warner, P.5    Jankowski, J.6
  • 5
    • 77950904660 scopus 로고    scopus 로고
    • Bile acids modulate the Golgi membrane fission process via a protein kinase Ceta and protein kinase D-dependent pathway in colonic epithelial cells
    • Byrne AM, Foran E, Sharma R, Davies A, Mahon C, O'Sullivan J, O'Donoghue D, Kelleher D, Long A. 2010. Bile acids modulate the Golgi membrane fission process via a protein kinase Ceta and protein kinase D-dependent pathway in colonic epithelial cells. Carcinogenesis. 31:737-744
    • (2010) Carcinogenesis. , vol.31 , pp. 737-744
    • Byrne, A.M.1    Foran, E.2    Sharma, R.3    Davies, A.4    Mahon, C.5    O'sullivan, J.6    O'donoghue, D.7    Kelleher, D.8    Long, A.9
  • 7
    • 59149101665 scopus 로고    scopus 로고
    • Siglecs as positive and negative regulators of the immune system
    • Crocker PR, Redelinghuys P. 2008. Siglecs as positive and negative regulators of the immune system. Biochem Soc Trans. 36:1467-1471
    • (2008) Biochem Soc Trans. , vol.36 , pp. 1467-1471
    • Crocker, P.R.1    Redelinghuys, P.2
  • 9
    • 70350685770 scopus 로고    scopus 로고
    • Adaptive regulation at the cell surface by N-glycosylation
    • Dennis JW, Lau KS, Demetriou M, Nabi IR. 2009. Adaptive regulation at the cell surface by N-glycosylation. Traffic. 10:1569-1578
    • (2009) Traffic. , vol.10 , pp. 1569-1578
    • Dennis, J.W.1    Lau, K.S.2    Demetriou, M.3    Nabi, I.R.4
  • 13
    • 50149084272 scopus 로고    scopus 로고
    • Bile acids repress E-cadherin through the induction of Snail and increase cancer invasiveness in human hepatobiliary carcinoma
    • Fukase K, Ohtsuka H, et al. 2008. Bile acids repress E-cadherin through the induction of Snail and increase cancer invasiveness in human hepatobiliary carcinoma. Cancer Sci. 99:1785-1792
    • (2008) Cancer Sci. , vol.99 , pp. 1785-1792
    • Fukase, K.1    Ohtsuka, H.2
  • 15
    • 66749116046 scopus 로고    scopus 로고
    • Importance of N-glycosylation on α5β1 integrin for its biological functions
    • Gu J, Isaji T, Sato Y, Kariya Y, Fukuda T. 2009. Importance of N-glycosylation on α5β1 integrin for its biological functions. Biol Pharm Bull. 32:780-785
    • (2009) Biol Pharm Bull. , vol.32 , pp. 780-785
    • Gu, J.1    Isaji, T.2    Sato, Y.3    Kariya, Y.4    Fukuda, T.5
  • 16
    • 22844433667 scopus 로고    scopus 로고
    • The chemistry and biology of mucin-type O-linked glycosylation
    • Hang HC, Bertozzi CR. 2005. The chemistry and biology of mucin-type O-linked glycosylation. Bioorg Med Chem. 13:5021-5034
    • (2005) Bioorg Med Chem. , vol.13 , pp. 5021-5034
    • Hang, H.C.1    Bertozzi, C.R.2
  • 20
    • 0037051978 scopus 로고    scopus 로고
    • Abnormal glycosylation and altered Golgi structure in colorectal cancer: Dependence on intra-Golgi pH
    • Kellokumpu S, Sormunen R, Kellokumpu I. 2002. Abnormal glycosylation and altered Golgi structure in colorectal cancer: Dependence on intra-Golgi pH. FEBS Lett. 516:217-224
    • (2002) FEBS Lett. , vol.516 , pp. 217-224
    • Kellokumpu, S.1    Sormunen, R.2    Kellokumpu, I.3
  • 22
    • 33847315195 scopus 로고    scopus 로고
    • Regulation of Cdx2 expression by promoter methylation, and effects of Cdx2 transfection on morphology and gene expression of human esophageal epithelial cells
    • Liu T, Zhang X, So C-K., Wang S, Wang P, Yan L, Myers R, Chen Z, Patterson AP, Yang CS, Chen X. 2007. Regulation of Cdx2 expression by promoter methylation, and effects of Cdx2 transfection on morphology and gene expression of human esophageal epithelial cells. Carcinogenesis. 28, 488-496
    • (2007) Carcinogenesis. , vol.28 , pp. 488-496
    • Liu, T.1    Zhang, X.2    So, C.-K.3    Wang, S.4    Wang, P.5    Yan, L.6    Myers, R.7    Chen, Z.8    Patterson, A.P.9    Yang, C.S.10    Chen, X.11
  • 23
    • 33747377812 scopus 로고    scopus 로고
    • N-Glycosylation affects the molecular organization and stability of E-cadherin junctions
    • Liwosz A, Lei T, Kukuruzinska MA. 2006. N-Glycosylation affects the molecular organization and stability of E-cadherin junctions. J Biol Chem. 281:23138-23149
    • (2006) J Biol Chem. , vol.281 , pp. 23138-23149
    • Liwosz, A.1    Lei, T.2    Kukuruzinska, M.A.3
  • 24
    • 35148832569 scopus 로고    scopus 로고
    • Epidermal growth factor receptor cooperates with signal transducer and activator of transcription 3 to induce epithelialmesenchymal transition in cancer cells via up-regulation of TWIST gene expression
    • Lo HW, Hsu SC, Xia W, Cao X, Shih JY, Wei Y, Abbruzzese JL, Hortobagyi GN, Hung MC. 2007. Epidermal growth factor receptor cooperates with signal transducer and activator of transcription 3 to induce epithelialmesenchymal transition in cancer cells via up-regulation of TWIST gene expression. Cancer Res. 67:9066-9076
    • (2007) Cancer Res. , vol.67 , pp. 9066-9076
    • Lo, H.W.1    Hsu, S.C.2    Xia, W.3    Cao, X.4    Shih, J.Y.5    Wei, Y.6    Abbruzzese, J.L.7    Hortobagyi, G.N.8    Hung, M.C.9
  • 25
    • 17044411372 scopus 로고    scopus 로고
    • Bile acid deoxycholate induces differential subcellular localisation of the PKC isoenzymes β1, and δ in colonic epithelial cells in a sodium butyrate insensitive manner
    • Looby E, Long A, Kelleher D, Volkov Y. 2005. Bile acid deoxycholate induces differential subcellular localisation of the PKC isoenzymes β1, and δ in colonic epithelial cells in a sodium butyrate insensitive manner. Int J Cancer. 114:887-895
    • (2005) Int J Cancer. , vol.114 , pp. 887-895
    • Looby, E.1    Long, A.2    Kelleher, D.3    Volkov, Y.4
  • 26
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley F, Trimble RB, Tarentino AL, Plummer TH, Jr.. 1989. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal Biochem. 180:195-204
    • (1989) Anal Biochem. , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer Jr., T.H.4
  • 27
    • 49749141107 scopus 로고    scopus 로고
    • N-Glycan fucosylation of epidermal growth factor receptor modulates receptor activity and sensitivity to epidermal growth factor receptor tyrosine kinase inhibitor
    • Matsumoto K, Yokote H, Arao T, Maegawa M, Tanaka K, Fujita Y, Shimizu C, Hanafusa T, Fujiwara Y, Nishio K. 2008. N-Glycan fucosylation of epidermal growth factor receptor modulates receptor activity and sensitivity to epidermal growth factor receptor tyrosine kinase inhibitor. Cancer Sci. 99:1611-1617
    • (2008) Cancer Sci. , vol.99 , pp. 1611-1617
    • Matsumoto, K.1    Yokote, H.2    Arao, T.3    Maegawa, M.4    Tanaka, K.5    Fujita, Y.6    Shimizu, C.7    Hanafusa, T.8    Fujiwara, Y.9    Nishio, K.10
  • 30
    • 0032965548 scopus 로고    scopus 로고
    • Toxic bile acids in gastro-oesophageal reflux disease: Influence of gastric acidity
    • Nehra D, Howell P, Williams CP, Pye JK, Beynon J. 1999. Toxic bile acids in gastro-oesophageal reflux disease: Influence of gastric acidity. Gut. 44:598-602
    • (1999) Gut. , vol.44 , pp. 598-602
    • Nehra, D.1    Howell, P.2    Williams, C.P.3    Pye, J.K.4    Beynon, J.5
  • 31
    • 58149159258 scopus 로고    scopus 로고
    • Lectin UEA-I-binding proteins are specifically increased in the squamous epithelium of patients with Barrett's esophagus
    • Neumann H, Wex T, Monkemuller K, Vieth M, Fry LC, Malfertheiner P. 2008. Lectin UEA-I-binding proteins are specifically increased in the squamous epithelium of patients with Barrett's esophagus. Digestion. 78:201-207
    • (2008) Digestion. , vol.78 , pp. 201-207
    • Neumann, H.1    Wex, T.2    Monkemuller, K.3    Vieth, M.4    Fry, L.C.5    Malfertheiner, P.6
  • 33
    • 0024355330 scopus 로고
    • Glycoproteins: What are the sugar chains for?
    • Paulson JC. 1989. Glycoproteins: What are the sugar chains for? Trends in Biochem Sci. 14:272-276
    • (1989) Trends in Biochem Sci. , vol.14 , pp. 272-276
    • Paulson, J.C.1
  • 35
    • 65549131351 scopus 로고    scopus 로고
    • Elevated Golgi pH impairs terminal N-glycosylation by inducing mislocalization of Golgi glycosyltransferases
    • Rivinoja A, Hassinen A, Kokkonen N, Kauppila A, Kellokumpu S. 2009. Elevated Golgi pH impairs terminal N-glycosylation by inducing mislocalization of Golgi glycosyltransferases. J Cell Physiol. 220:144-154
    • (2009) J Cell Physiol. , vol.220 , pp. 144-154
    • Rivinoja, A.1    Hassinen, A.2    Kokkonen, N.3    Kauppila, A.4    Kellokumpu, S.5
  • 36
    • 30444446498 scopus 로고    scopus 로고
    • Ursodeoxycholic acid inhibits interleukin 1 beta [corrected] and deoxycholic acid-induced activation of NF-?B and AP-1 in human colon cancer cells
    • Shah SA, Volkov Y, Arfin Q, Abdel-Latif MM, Kelleher D. 2006. Ursodeoxycholic acid inhibits interleukin 1 beta [corrected] and deoxycholic acid-induced activation of NF-?B and AP-1 in human colon cancer cells. Int J Cancer. 118:532-539
    • (2006) Int J Cancer. , vol.118 , pp. 532-539
    • Shah, S.A.1    Volkov, Y.2    Arfin, Q.3    Abdel-Latif, M.M.4    Kelleher, D.5
  • 37
    • 77956342528 scopus 로고    scopus 로고
    • Bile acid toxicity structure-activity relationships: Correlations between cell viability and lipophilicity in a panel of new and known bile acids using an oesophageal cell line (HET-1A)
    • Sharma R, Majer F, Peta VK, Wang J, Keaveney R, Kelleher D, Long A, Gilmer JF. 2010. Bile acid toxicity structure-activity relationships: Correlations between cell viability and lipophilicity in a panel of new and known bile acids using an oesophageal cell line (HET-1A). Bioorg Med Chem. 18:6886-6895
    • (2010) Bioorg Med Chem. , vol.18 , pp. 6886-6895
    • Sharma, R.1    Majer, F.2    Peta, V.K.3    Wang, J.4    Keaveney, R.5    Kelleher, D.6    Long, A.7    Gilmer, J.F.8
  • 38
    • 0023518530 scopus 로고
    • Glycoconjugate expression in normal, metaplastic, and neoplastic human upper gastrointestinal mucosa
    • Shimamoto C, Weinstein WM, Boland CR. 1987. Glycoconjugate expression in normal, metaplastic, and neoplastic human upper gastrointestinal mucosa. J Clin Invest. 80:1670-1678
    • (1987) J Clin Invest. , vol.80 , pp. 1670-1678
    • Shimamoto, C.1    Weinstein, W.M.2    Boland, C.R.3
  • 39
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: Their functions and target proteins
    • Takahashi M, Kuroki Y, Ohtsubo K, Taniguchi N. 2009. Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: Their functions and target proteins. Carbohydr Res. 344:1387-1390
    • (2009) Carbohydr Res. , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Taniguchi, N.4
  • 41
    • 80053175737 scopus 로고    scopus 로고
    • Downregulation of E-Cadherin enhances proliferation of head and neck cancer through transcriptional regulation of EGFR
    • Wang D, Su L, Huang D, Zhang H, Shin DM, Chen ZG. 2011. Downregulation of E-Cadherin enhances proliferation of head and neck cancer through transcriptional regulation of EGFR. Mol Cancer. 10:116.
    • (2011) Mol Cancer. , vol.10 , pp. 116
    • Wang, D.1    Su, L.2    Huang, D.3    Zhang, H.4    Shin, D.M.5    Chen, Z.G.6
  • 42
    • 77955289215 scopus 로고    scopus 로고
    • Inhibition of Golgi apparatus glycosylation causes endoplasmic reticulum stress and decreased protein synthesis
    • Xu YX, Liu L, Caffaro CE, Hirschberg CB. 2010. Inhibition of Golgi apparatus glycosylation causes endoplasmic reticulum stress and decreased protein synthesis. J Biol Chem. 285:24600-24608
    • (2010) J Biol Chem. , vol.285 , pp. 24600-24608
    • Xu, Y.X.1    Liu, L.2    Caffaro, C.E.3    Hirschberg, C.B.4
  • 45
    • 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
    • Zhou F, Su J, Fu L, Yang Y, Zhang L, Wang L, Zhao H, Zhang D, Li Z, Zha X. 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.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.