메뉴 건너뛰기




Volumn 7, Issue 23, 2016, Pages 35478-35489

Hallmarks of glycosylation in cancer

Author keywords

Aberrant; Cancer; Glycans; Glycosylation; Hallmarks

Indexed keywords

GLYCAN DERIVATIVE;

EID: 84973310291     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.8155     Document Type: Article
Times cited : (376)

References (157)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D and Weinberg RA. The hallmarks of cancer. Cell. 2000; 100:57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 67650151005 scopus 로고    scopus 로고
    • Cancer-related inflammation, the seventh hallmark of cancer: links to genetic instability
    • Colotta F, Allavena P, Sica A, Garlanda C and Mantovani A. Cancer-related inflammation, the seventh hallmark of cancer: links to genetic instability. Carcinogenesis. 2009; 30:1073-1081
    • (2009) Carcinogenesis , vol.30 , pp. 1073-1081
    • Colotta, F.1    Allavena, P.2    Sica, A.3    Garlanda, C.4    Mantovani, A.5
  • 3
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D and Weinberg RA. Hallmarks of cancer: the next generation. Cell. 2011; 144:646-674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 4
    • 0014531785 scopus 로고
    • Comparative studies on the carbohydrate-containing membrane components of normal and virus-transformed mouse fibroblasts. II. Separation of glycoproteins and glycopeptides by sephadex chromatography
    • Meezan E, Wu HC, Black PH and Robbins PW. Comparative studies on the carbohydrate-containing membrane components of normal and virus-transformed mouse fibroblasts. II. Separation of glycoproteins and glycopeptides by sephadex chromatography. Biochemistry. 1969; 8:2518-2524
    • (1969) Biochemistry , vol.8 , pp. 2518-2524
    • Meezan, E.1    Wu, H.C.2    Black, P.H.3    Robbins, P.W.4
  • 5
    • 0022318508 scopus 로고
    • Carbohydrate antigens in human cancer
    • Feizi T. Carbohydrate antigens in human cancer. Cancer Surv. 1985; 4:245-269
    • (1985) Cancer Surv , vol.4 , pp. 245-269
    • Feizi, T.1
  • 6
    • 0033057177 scopus 로고    scopus 로고
    • The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues
    • Hammarstrom S. The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues. Seminars in cancer biology. 1999; 9:67-81
    • (1999) Seminars in cancer biology , vol.9 , pp. 67-81
    • Hammarstrom, S.1
  • 9
    • 84898022102 scopus 로고    scopus 로고
    • Altered tumor-cell glycosylation promotes metastasis
    • Hauselmann I and Borsig L. Altered tumor-cell glycosylation promotes metastasis. Front Oncol. 2014; 4:28
    • (2014) Front Oncol , vol.4 , pp. 28
    • Hauselmann, I.1    Borsig, L.2
  • 10
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: glycans as novel therapeutic targets
    • Fuster MM and Esko JD. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat Rev Cancer. 2005; 5:526-542
    • (2005) Nat Rev Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 11
    • 84940449986 scopus 로고    scopus 로고
    • Glycosylation in cancer: mechanisms and clinical implications
    • Pinho SS and Reis CA. Glycosylation in cancer: mechanisms and clinical implications. Nat Rev Cancer. 2015; 15:540-555
    • (2015) Nat Rev Cancer , vol.15 , pp. 540-555
    • Pinho, S.S.1    Reis, C.A.2
  • 12
    • 84860239658 scopus 로고    scopus 로고
    • Aberrant glycosylation associated with enzymes as cancer biomarkers
    • Meany DL and Chan DW. Aberrant glycosylation associated with enzymes as cancer biomarkers. Clinical proteomics. 2011; 8:7
    • (2011) Clinical proteomics , vol.8 , pp. 7
    • Meany, D.L.1    Chan, D.W.2
  • 14
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation-potential for therapeutics and diagnostics
    • Dube DH and Bertozzi CR. Glycans in cancer and inflammation-potential for therapeutics and diagnostics. Nat Rev Drug Discov. 2005; 4:477-488
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 15
    • 84964711861 scopus 로고    scopus 로고
    • The role of N-glycans in colorectal cancer progression: Potential biomarkers and therapeutic applications
    • de-Freitas-Junior JC and Morgado-Diaz JA. The role of N-glycans in colorectal cancer progression: Potential biomarkers and therapeutic applications. Oncotarget. 2015. doi: 10.18632/oncotarget.6283
    • (2015) Oncotarget
    • de-Freitas-Junior, J.C.1    Morgado-Diaz, J.A.2
  • 18
    • 0035083062 scopus 로고    scopus 로고
    • Pathways of mucin O-glycosylation in normal and malignant rat colonic epithelial cells reveal a mechanism for cancer-associated Sialyl-Tn antigen expression
    • Brockhausen I, Yang J, Lehotay M, Ogata S and Itzkowitz S. Pathways of mucin O-glycosylation in normal and malignant rat colonic epithelial cells reveal a mechanism for cancer-associated Sialyl-Tn antigen expression. Biol Chem. 2001; 382:219-232
    • (2001) Biol Chem , vol.382 , pp. 219-232
    • Brockhausen, I.1    Yang, J.2    Lehotay, M.3    Ogata, S.4    Itzkowitz, S.5
  • 19
    • 84903767444 scopus 로고    scopus 로고
    • O-GlcNAc profiling: from proteins to proteomes
    • Ma J and Hart GW. O-GlcNAc profiling: from proteins to proteomes. Clinical proteomics. 2014; 11:8
    • (2014) Clinical proteomics , vol.11 , pp. 8
    • Ma, J.1    Hart, G.W.2
  • 20
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: implications for cancer cell biology
    • Slawson C and Hart GW. O-GlcNAc signalling: implications for cancer cell biology. Nat Rev Cancer. 2011; 11:678-684
    • (2011) Nat Rev Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 21
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • Schwarz F and Aebi M. Mechanisms and principles of N-linked protein glycosylation. Current opinion in structural biology. 2011; 21:576-582
    • (2011) Current opinion in structural biology , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 22
    • 84923288088 scopus 로고    scopus 로고
    • Glycans and cancer: role of N-glycans in cancer biomarker, progression and metastasis, and therapeutics
    • Taniguchi N and Kizuka Y. Glycans and cancer: role of N-glycans in cancer biomarker, progression and metastasis, and therapeutics. Adv Cancer Res. 2015; 126:11-51
    • (2015) Adv Cancer Res , vol.126 , pp. 11-51
    • Taniguchi, N.1    Kizuka, Y.2
  • 26
    • 84955565229 scopus 로고    scopus 로고
    • Cracking the Glycome Encoder: Signaling, Trafficking, and Glycosylation
    • Bard F and Chia J. Cracking the Glycome Encoder: Signaling, Trafficking, and Glycosylation. Trends in cell biology. 2016
    • (2016) Trends in cell biology
    • Bard, F.1    Chia, J.2
  • 27
    • 77952429792 scopus 로고    scopus 로고
    • Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
    • Caldwell SA, Jackson SR, Shahriari KS, Lynch TP, Sethi G, Walker S, Vosseller K and Reginato MJ. Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1. Oncogene. 2010; 29:2831-2842
    • (2010) Oncogene , vol.29 , pp. 2831-2842
    • Caldwell, S.A.1    Jackson, S.R.2    Shahriari, K.S.3    Lynch, T.P.4    Sethi, G.5    Walker, S.6    Vosseller, K.7    Reginato, M.J.8
  • 30
    • 34249090239 scopus 로고    scopus 로고
    • A sugar-coated switch for cellular growth and arrest
    • Taniguchi N. A sugar-coated switch for cellular growth and arrest. Nat Chem Biol. 2007; 3:307-309
    • (2007) Nat Chem Biol , vol.3 , pp. 307-309
    • Taniguchi, N.1
  • 31
    • 33947725535 scopus 로고    scopus 로고
    • A method to the madness of N-glycan complexity?
    • Stanley P. A method to the madness of N-glycan complexity? Cell. 2007; 129:27-29
    • (2007) Cell , vol.129 , pp. 27-29
    • Stanley, P.1
  • 32
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, Demetriou M and Dennis JW. Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell. 2007; 129:123-134
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 34
    • 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
    • Todeschini AR, Dos Santos JN, Handa K and Hakomori SI. 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. 2007; 282:8123-8133
    • (2007) J Biol Chem , vol.282 , pp. 8123-8133
    • Todeschini, A.R.1    Dos Santos, J.N.2    Handa, K.3    Hakomori, S.I.4
  • 35
    • 68249112890 scopus 로고    scopus 로고
    • Control of cell motility by interaction of gangliosides, tetraspanins, and epidermal growth factor receptor in A431 versus KB epidermoid tumor cells
    • Park SY, Yoon SJ, Freire-de-Lima L, Kim JH and Hakomori SI. Control of cell motility by interaction of gangliosides, tetraspanins, and epidermal growth factor receptor in A431 versus KB epidermoid tumor cells. Carbohydr Res. 2009; 344:1479-1486
    • (2009) Carbohydr Res , vol.344 , pp. 1479-1486
    • Park, S.Y.1    Yoon, S.J.2    Freire-de-Lima, L.3    Kim, J.H.4    Hakomori, S.I.5
  • 36
    • 79955528442 scopus 로고    scopus 로고
    • Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor
    • Kim SH, Turnbull J and Guimond S. Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor. J Endocrinol. 2011; 209:139-151
    • (2011) J Endocrinol , vol.209 , pp. 139-151
    • Kim, S.H.1    Turnbull, J.2    Guimond, S.3
  • 39
    • 0032529429 scopus 로고    scopus 로고
    • Site-specific de-Nglycosylation of CD44 can activate hyaluronan binding, and CD44 activation states show distinct threshold densities for hyaluronan binding
    • English NM, Lesley JF and Hyman R. Site-specific de-Nglycosylation of CD44 can activate hyaluronan binding, and CD44 activation states show distinct threshold densities for hyaluronan binding. Cancer Res. 1998; 58:3736-3742
    • (1998) Cancer Res , vol.58 , pp. 3736-3742
    • English, N.M.1    Lesley, J.F.2    Hyman, R.3
  • 40
    • 0030929761 scopus 로고    scopus 로고
    • Increase of rat colon carcinoma cells tumorigenicity by alpha(1-2) fucosyltransferase gene transfection
    • Goupille C, Hallouin F, Meflah K and Le Pendu J. Increase of rat colon carcinoma cells tumorigenicity by alpha(1-2) fucosyltransferase gene transfection. Glycobiology. 1997; 7:221-229
    • (1997) Glycobiology , vol.7 , pp. 221-229
    • Goupille, C.1    Hallouin, F.2    Meflah, K.3    Le Pendu, J.4
  • 43
    • 79954449301 scopus 로고    scopus 로고
    • The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc
    • Wells L, Slawson C and Hart GW. The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc. Amino Acids. 2011; 40:877-883
    • (2011) Amino Acids , vol.40 , pp. 877-883
    • Wells, L.1    Slawson, C.2    Hart, G.W.3
  • 44
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang WH, Kim JE, Nam HW, Ju JW, Kim HS, Kim YS and Cho JW. Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat Cell Biol. 2006; 8:1074-1083
    • (2006) Nat Cell Biol , vol.8 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3    Ju, J.W.4    Kim, H.S.5    Kim, Y.S.6    Cho, J.W.7
  • 49
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O. On the origin of cancer cells. Science. 1956; 123:309-314
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 50
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
    • Wells L, Vosseller K and Hart GW. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science. 2001; 291:2376-2378
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 51
    • 84920157343 scopus 로고    scopus 로고
    • O-GlcNAc signaling in cancer metabolism and epigenetics
    • Singh JP, Zhang K, Wu J and Yang X. O-GlcNAc signaling in cancer metabolism and epigenetics. Cancer letters. 2015; 356(2 Pt A):244-250
    • (2015) Cancer letters , vol.356 , Issue.2 , pp. 244-250
    • Singh, J.P.1    Zhang, K.2    Wu, J.3    Yang, X.4
  • 52
    • 84958762084 scopus 로고    scopus 로고
    • Cancer metabolism: cross talk between signaling and O-GlcNAcylation
    • Ferrer CM and Reginato MJ. Cancer metabolism: cross talk between signaling and O-GlcNAcylation. Methods in molecular biology. 2014; 1176:73-88
    • (2014) Methods in molecular biology , vol.1176 , pp. 73-88
    • Ferrer, C.M.1    Reginato, M.J.2
  • 53
    • 84860184939 scopus 로고    scopus 로고
    • Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation
    • Hanover JA, Krause MW and Love DC. Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation. Nat Rev Mol Cell Biol. 2012; 13:312-321
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 312-321
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 54
    • 84918523488 scopus 로고    scopus 로고
    • Cancer metabolism and elevated O-GlcNAc in oncogenic signaling
    • Ma Z and Vosseller K. Cancer metabolism and elevated O-GlcNAc in oncogenic signaling. J Biol Chem. 2014; 289:34457-34465
    • (2014) J Biol Chem , vol.289 , pp. 34457-34465
    • Ma, Z.1    Vosseller, K.2
  • 60
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: a review of programmed cell death
    • Elmore S. Apoptosis: a review of programmed cell death. Toxicologic pathology. 2007; 35:495-516
    • (2007) Toxicologic pathology , vol.35 , pp. 495-516
    • Elmore, S.1
  • 61
    • 84880276658 scopus 로고    scopus 로고
    • Glycobiology of cell death: when glycans and lectins govern cell fate
    • Lichtenstein RG and Rabinovich GA. Glycobiology of cell death: when glycans and lectins govern cell fate. Cell death and differentiation. 2013; 20:976-986
    • (2013) Cell death and differentiation , vol.20 , pp. 976-986
    • Lichtenstein, R.G.1    Rabinovich, G.A.2
  • 64
    • 0033046601 scopus 로고    scopus 로고
    • Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/Fas)-mediated apoptosis and for infection by a lymphotropic virus
    • Keppler OT, Peter ME, Hinderlich S, Moldenhauer G, Stehling P, Schmitz I, Schwartz-Albiez R, Reutter W and Pawlita M. Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/Fas)-mediated apoptosis and for infection by a lymphotropic virus. Glycobiology. 1999; 9:557-569
    • (1999) Glycobiology , vol.9 , pp. 557-569
    • Keppler, O.T.1    Peter, M.E.2    Hinderlich, S.3    Moldenhauer, G.4    Stehling, P.5    Schmitz, I.6    Schwartz-Albiez, R.7    Reutter, W.8    Pawlita, M.9
  • 66
    • 79959563528 scopus 로고    scopus 로고
    • Sialylation of the Fas death receptor by ST6Gal-I provides protection against Fasmediated apoptosis in colon carcinoma cells
    • Swindall AF and Bellis SL. Sialylation of the Fas death receptor by ST6Gal-I provides protection against Fasmediated apoptosis in colon carcinoma cells. J Biol Chem. 2011; 286:22982-22990
    • (2011) J Biol Chem , vol.286 , pp. 22982-22990
    • Swindall, A.F.1    Bellis, S.L.2
  • 70
    • 24744455701 scopus 로고    scopus 로고
    • Galectin-3 inhibits tumor necrosis factor-related apoptosis-inducing ligandinduced apoptosis by activating Akt in human bladder carcinoma cells
    • Oka N, Nakahara S, Takenaka Y, Fukumori T, Hogan V, Kanayama HO, Yanagawa T and Raz A. Galectin-3 inhibits tumor necrosis factor-related apoptosis-inducing ligandinduced apoptosis by activating Akt in human bladder carcinoma cells. Cancer Res. 2005; 65:7546-7553
    • (2005) Cancer Res , vol.65 , pp. 7546-7553
    • Oka, N.1    Nakahara, S.2    Takenaka, Y.3    Fukumori, T.4    Hogan, V.5    Kanayama, H.O.6    Yanagawa, T.7    Raz, A.8
  • 71
    • 84857048734 scopus 로고    scopus 로고
    • Cell-surface galectin-3 confers resistance to TRAIL by impeding trafficking of death receptors in metastatic colon adenocarcinoma cells
    • Mazurek N, Byrd JC, Sun Y, Hafley M, Ramirez K, Burks J and Bresalier RS. Cell-surface galectin-3 confers resistance to TRAIL by impeding trafficking of death receptors in metastatic colon adenocarcinoma cells. Cell death and differentiation. 2012; 19:523-533
    • (2012) Cell death and differentiation , vol.19 , pp. 523-533
    • Mazurek, N.1    Byrd, J.C.2    Sun, Y.3    Hafley, M.4    Ramirez, K.5    Burks, J.6    Bresalier, R.S.7
  • 73
    • 0037203318 scopus 로고    scopus 로고
    • GD3 ganglioside and apoptosis
    • Malisan F and Testi R. GD3 ganglioside and apoptosis. Biochim Biophys Acta. 2002; 1585(2-3):179-187
    • (2002) Biochim Biophys Acta , vol.1585 , Issue.2-3 , pp. 179-187
    • Malisan, F.1    Testi, R.2
  • 75
    • 84860507660 scopus 로고    scopus 로고
    • Ceramide and apoptosis: exploring the enigmatic connections between sphingolipid metabolism and programmed cell death
    • Mullen TD and Obeid LM. Ceramide and apoptosis: exploring the enigmatic connections between sphingolipid metabolism and programmed cell death. Anti-cancer agents in medicinal chemistry. 2012; 12:340-363
    • (2012) Anti-cancer agents in medicinal chemistry , vol.12 , pp. 340-363
    • Mullen, T.D.1    Obeid, L.M.2
  • 76
    • 79952767541 scopus 로고    scopus 로고
    • Suppression of glucosylceramide synthase restores p53-dependent apoptosis in mutant p53 cancer cells
    • Liu YY, Patwardhan GA, Bhinge K, Gupta V, Gu X and Jazwinski SM. Suppression of glucosylceramide synthase restores p53-dependent apoptosis in mutant p53 cancer cells. Cancer Res. 2011; 71:2276-2285
    • (2011) Cancer Res , vol.71 , pp. 2276-2285
    • Liu, Y.Y.1    Patwardhan, G.A.2    Bhinge, K.3    Gupta, V.4    Gu, X.5    Jazwinski, S.M.6
  • 77
    • 84862503099 scopus 로고    scopus 로고
    • Quantification of alternative splicing variants of human telomerase reverse transcriptase and correlations with telomerase activity in lung cancer
    • Liu Y, Wu BQ, Zhong HH, Tian XX and Fang WG. Quantification of alternative splicing variants of human telomerase reverse transcriptase and correlations with telomerase activity in lung cancer. PLoS One. 2012; 7:e38868
    • (2012) PLoS One , vol.7
    • Liu, Y.1    Wu, B.Q.2    Zhong, H.H.3    Tian, X.X.4    Fang, W.G.5
  • 80
    • 0029049198 scopus 로고
    • c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas
    • Chou TY, Hart GW and Dang CV. c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. J Biol Chem. 1995; 270:18961-18965
    • (1995) J Biol Chem , vol.270 , pp. 18961-18965
    • Chou, T.Y.1    Hart, G.W.2    Dang, C.V.3
  • 82
    • 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 U S A. 2002; 99:10231-10233
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 83
    • 0031937018 scopus 로고    scopus 로고
    • Dimeric sialyl-Le(x) expression in gastric carcinoma correlates with venous invasion and poor outcome
    • Amado M, Carneiro F, Seixas M, Clausen H and Sobrinho-Simoes M. Dimeric sialyl-Le(x) expression in gastric carcinoma correlates with venous invasion and poor outcome. Gastroenterology. 1998; 114:462-470
    • (1998) Gastroenterology , vol.114 , pp. 462-470
    • Amado, M.1    Carneiro, F.2    Seixas, M.3    Clausen, H.4    Sobrinho-Simoes, M.5
  • 84
    • 0027250266 scopus 로고
    • Increased expression of sialyl Lewisx antigen correlates with poor survival in patients with colorectal carcinoma: clinicopathological and immunohistochemical study
    • Nakamori S, Kameyama M, Imaoka S, Furukawa H, Ishikawa O, Sasaki Y, Kabuto T, Iwanaga T, Matsushita Y and Irimura T. Increased expression of sialyl Lewisx antigen correlates with poor survival in patients with colorectal carcinoma: clinicopathological and immunohistochemical study. Cancer Res. 1993; 53:3632-3637
    • (1993) Cancer Res , vol.53 , pp. 3632-3637
    • Nakamori, S.1    Kameyama, M.2    Imaoka, S.3    Furukawa, H.4    Ishikawa, O.5    Sasaki, Y.6    Kabuto, T.7    Iwanaga, T.8    Matsushita, Y.9    Irimura, T.10
  • 85
    • 0026483419 scopus 로고
    • Sialyl Tn as a prognostic marker in epithelial ovarian cancer
    • Kobayashi H, Terao T and Kawashima Y. Sialyl Tn as a prognostic marker in epithelial ovarian cancer. Br J Cancer. 1992; 66:984-985
    • (1992) Br J Cancer , vol.66 , pp. 984-985
    • Kobayashi, H.1    Terao, T.2    Kawashima, Y.3
  • 86
    • 0026531757 scopus 로고
    • Serum sialyl Tn as an independent predictor of poor prognosis in patients with epithelial ovarian cancer
    • Kobayashi H, Terao T and Kawashima Y. Serum sialyl Tn as an independent predictor of poor prognosis in patients with epithelial ovarian cancer. J Clin Oncol. 1992; 10:95-101
    • (1992) J Clin Oncol , vol.10 , pp. 95-101
    • Kobayashi, H.1    Terao, T.2    Kawashima, Y.3
  • 87
    • 0042131904 scopus 로고    scopus 로고
    • Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions
    • Seidenfaden R, Krauter A, Schertzinger F, Gerardy-Schahn R and Hildebrandt H. Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions. Mol Cell Biol. 2003; 23:5908-5918
    • (2003) Mol Cell Biol , vol.23 , pp. 5908-5918
    • Seidenfaden, R.1    Krauter, A.2    Schertzinger, F.3    Gerardy-Schahn, R.4    Hildebrandt, H.5
  • 89
    • 84959187211 scopus 로고    scopus 로고
    • Sugars and cell adhesion: The role of ST6GalNAc1 in prostate cancer progression
    • Munkley J and Elliott DJ. Sugars and cell adhesion: The role of ST6GalNAc1 in prostate cancer progression. Cancer Cell & Microenvironment. 2016; 3:e1174
    • (2016) Cancer Cell & Microenvironment , vol.3
    • Munkley, J.1    Elliott, D.J.2
  • 91
    • 84857366326 scopus 로고    scopus 로고
    • Enhancement of metastatic ability by ectopic expression of ST6GalNAcI on a gastric cancer cell line in a mouse model
    • Ozaki H, Matsuzaki H, Ando H, Kaji H, Nakanishi H, Ikehara Y and Narimatsu H. Enhancement of metastatic ability by ectopic expression of ST6GalNAcI on a gastric cancer cell line in a mouse model. Clin Exp Metastasis. 2012; 29:229-238
    • (2012) Clin Exp Metastasis , vol.29 , pp. 229-238
    • Ozaki, H.1    Matsuzaki, H.2    Ando, H.3    Kaji, H.4    Nakanishi, H.5    Ikehara, Y.6    Narimatsu, H.7
  • 94
    • 0036351383 scopus 로고    scopus 로고
    • Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells
    • Lin S, Kemmner W, Grigull S and Schlag PM. Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells. Exp Cell Res. 2002; 276:101-110
    • (2002) Exp Cell Res , vol.276 , pp. 101-110
    • Lin, S.1    Kemmner, W.2    Grigull, S.3    Schlag, P.M.4
  • 100
    • 0347993082 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways
    • Guo HB, 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. 2003; 278:52412-52424
    • (2003) J Biol Chem , vol.278 , pp. 52412-52424
    • Guo, H.B.1    Lee, I.2    Kamar, M.3    Pierce, M.4
  • 101
    • 0037053318 scopus 로고    scopus 로고
    • Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching
    • Ihara S, Miyoshi E, Ko JH, Murata K, Nakahara S, Honke K, Dickson RB, Lin CY and Taniguchi N. Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching. J Biol Chem. 2002; 277:16960-16967
    • (2002) J Biol Chem , vol.277 , pp. 16960-16967
    • Ihara, S.1    Miyoshi, E.2    Ko, J.H.3    Murata, K.4    Nakahara, S.5    Honke, K.6    Dickson, R.B.7    Lin, C.Y.8    Taniguchi, N.9
  • 102
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression
    • Song Y, Aglipay JA, Bernstein JD, Goswami S and Stanley P. The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression. Cancer Res. 2010; 70:3361-3371
    • (2010) Cancer Res , vol.70 , pp. 3361-3371
    • Song, Y.1    Aglipay, J.A.2    Bernstein, J.D.3    Goswami, S.4    Stanley, P.5
  • 103
    • 84887914597 scopus 로고    scopus 로고
    • Bisected, complex N-glycans and galectins in mouse mammary tumor progression and human breast cancer
    • Miwa HE, Koba WR, Fine EJ, Giricz O, Kenny PA and 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
  • 104
    • 0040668346 scopus 로고    scopus 로고
    • Sialyl Lewis(a): a tumorassociated carbohydrate antigen involved in adhesion and metastatic potential of cancer cells
    • Ugorski M and Laskowska A. Sialyl Lewis(a): a tumorassociated carbohydrate antigen involved in adhesion and metastatic potential of cancer cells. Acta biochimica Polonica. 2002; 49:303-311
    • (2002) Acta biochimica Polonica , vol.49 , pp. 303-311
    • Ugorski, M.1    Laskowska, A.2
  • 109
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan D and Folkman J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell. 1996; 86:353-364
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 110
    • 28444485987 scopus 로고    scopus 로고
    • Activation of human endothelial cells by tumor necrosis factor-alpha results in profound changes in the expression of glycosylation-related genes
    • Garcia-Vallejo JJ, Van Dijk W, Van Het Hof B, Van Die I, Engelse MA, Van Hinsbergh VW and Gringhuis SI. Activation of human endothelial cells by tumor necrosis factor-alpha results in profound changes in the expression of glycosylation-related genes. J Cell Physiol. 2006; 206:203-210
    • (2006) J Cell Physiol , vol.206 , pp. 203-210
    • Garcia-Vallejo, J.J.1    Van Dijk, W.2    Van Het Hof, B.3    Van Die, I.4    Engelse, M.A.5    Van Hinsbergh, V.W.6    Gringhuis, S.I.7
  • 112
    • 84922977686 scopus 로고    scopus 로고
    • Regulatory role of glycans in the control of hypoxia-driven angiogenesis and sensitivity to antiangiogenic treatment
    • Croci DO, Cerliani JP, Pinto NA, Morosi LG and Rabinovich GA. Regulatory role of glycans in the control of hypoxia-driven angiogenesis and sensitivity to antiangiogenic treatment. Glycobiology. 2014; 24:1283-1290
    • (2014) Glycobiology , vol.24 , pp. 1283-1290
    • Croci, D.O.1    Cerliani, J.P.2    Pinto, N.A.3    Morosi, L.G.4    Rabinovich, G.A.5
  • 113
    • 84859484538 scopus 로고    scopus 로고
    • Critical role of O-Linked beta-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis
    • Lynch TP, Ferrer CM, Jackson SR, Shahriari KS, Vosseller K and Reginato MJ. Critical role of O-Linked beta-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis. J Biol Chem. 2012; 287:11070-11081
    • (2012) J Biol Chem , vol.287 , pp. 11070-11081
    • Lynch, T.P.1    Ferrer, C.M.2    Jackson, S.R.3    Shahriari, K.S.4    Vosseller, K.5    Reginato, M.J.6
  • 115
    • 77949902267 scopus 로고    scopus 로고
    • Alpha2,6-sialic acid on platelet endothelial cell adhesion molecule (PECAM) regulates its homophilic interactions and downstream antiapoptotic signaling
    • Kitazume S, Imamaki R, Ogawa K, Komi Y, Futakawa S, Kojima S, Hashimoto Y, Marth JD, Paulson JC and Taniguchi N. Alpha2,6-sialic acid on platelet endothelial cell adhesion molecule (PECAM) regulates its homophilic interactions and downstream antiapoptotic signaling. J Biol Chem. 2010; 285:6515-6521
    • (2010) J Biol Chem , vol.285 , pp. 6515-6521
    • Kitazume, S.1    Imamaki, R.2    Ogawa, K.3    Komi, Y.4    Futakawa, S.5    Kojima, S.6    Hashimoto, Y.7    Marth, J.D.8    Paulson, J.C.9    Taniguchi, N.10
  • 116
    • 78650939979 scopus 로고    scopus 로고
    • Heparan sulfate regulates VEGF165-and VEGF121-mediated vascular hyperpermeability
    • Xu D, Fuster MM, Lawrence R and Esko JD. Heparan sulfate regulates VEGF165-and VEGF121-mediated vascular hyperpermeability. J Biol Chem. 2011; 286:737-745
    • (2011) J Biol Chem , vol.286 , pp. 737-745
    • Xu, D.1    Fuster, M.M.2    Lawrence, R.3    Esko, J.D.4
  • 121
    • 33745441066 scopus 로고    scopus 로고
    • The role of heparan sulphate proteoglycans in angiogenesis
    • Stringer SE. The role of heparan sulphate proteoglycans in angiogenesis. Biochem Soc Trans. 2006; 34(Pt 3):451-453
    • (2006) Biochem Soc Trans , vol.34 , pp. 451-453
    • Stringer, S.E.1
  • 122
    • 0034904186 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena
    • Iozzo RV and San Antonio JD. Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena. J Clin Invest. 2001; 108:349-355
    • (2001) J Clin Invest , vol.108 , pp. 349-355
    • Iozzo, R.V.1    San Antonio, J.D.2
  • 123
    • 0027064888 scopus 로고
    • Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms
    • Houck KA, Leung DW, Rowland AM, Winer J and Ferrara N. Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms. J Biol Chem. 1992; 267:26031-26037
    • (1992) J Biol Chem , vol.267 , pp. 26031-26037
    • Houck, K.A.1    Leung, D.W.2    Rowland, A.M.3    Winer, J.4    Ferrara, N.5
  • 126
    • 84898603944 scopus 로고    scopus 로고
    • Ovarian cancer cell heparan sulfate 6-O-sulfotransferases regulate an angiogenic program induced by heparin-binding epidermal growth factor (EGF)-like growth factor/EGF receptor signaling
    • Cole CL, Rushton G, Jayson GC and Avizienyte E. Ovarian cancer cell heparan sulfate 6-O-sulfotransferases regulate an angiogenic program induced by heparin-binding epidermal growth factor (EGF)-like growth factor/EGF receptor signaling. J Biol Chem. 2014; 289:10488-10501
    • (2014) J Biol Chem , vol.289 , pp. 10488-10501
    • Cole, C.L.1    Rushton, G.2    Jayson, G.C.3    Avizienyte, E.4
  • 127
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • Lane DP. Cancer. p53, guardian of the genome. Nature. 1992; 358:15-16
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 128
    • 79954434103 scopus 로고    scopus 로고
    • The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways
    • Zachara NE, Molina H, Wong KY, Pandey A and Hart GW. The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways. Amino Acids. 2011; 40:793-808
    • (2011) Amino Acids , vol.40 , pp. 793-808
    • Zachara, N.E.1    Molina, H.2    Wong, K.Y.3    Pandey, A.4    Hart, G.W.5
  • 130
    • 0022891340 scopus 로고
    • Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing
    • Dvorak HF. Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. N Engl J Med. 1986; 315:1650-1659
    • (1986) N Engl J Med , vol.315 , pp. 1650-1659
    • Dvorak, H.F.1
  • 131
    • 77954563614 scopus 로고    scopus 로고
    • Interactions between lymphocytes and myeloid cells regulate proversus anti-tumor immunity
    • DeNardo DG, Andreu P and Coussens LM. Interactions between lymphocytes and myeloid cells regulate proversus anti-tumor immunity. Cancer metastasis reviews. 2010; 29:309-316
    • (2010) Cancer metastasis reviews , vol.29 , pp. 309-316
    • DeNardo, D.G.1    Andreu, P.2    Coussens, L.M.3
  • 132
    • 77950346282 scopus 로고    scopus 로고
    • Immunity, inflammation, and cancer
    • Grivennikov SI, Greten FR and Karin M. Immunity, inflammation, and cancer. Cell. 2010; 140:883-899
    • (2010) Cell , vol.140 , pp. 883-899
    • Grivennikov, S.I.1    Greten, F.R.2    Karin, M.3
  • 133
    • 77950950894 scopus 로고    scopus 로고
    • Macrophage diversity enhances tumor progression and metastasis
    • Qian BZ and Pollard JW. Macrophage diversity enhances tumor progression and metastasis. Cell. 2010; 141:39-51
    • (2010) Cell , vol.141 , pp. 39-51
    • Qian, B.Z.1    Pollard, J.W.2
  • 134
    • 34247468926 scopus 로고    scopus 로고
    • Chemokine networks and breast cancer metastasis
    • Karnoub AE and Weinberg RA. Chemokine networks and breast cancer metastasis. Breast disease. 2006; 26:75-85
    • (2006) Breast disease , vol.26 , pp. 75-85
    • Karnoub, A.E.1    Weinberg, R.A.2
  • 135
    • 84858309804 scopus 로고    scopus 로고
    • Cancer cell adhesion and metastasis: selectins, integrins, and the inhibitory potential of heparins
    • Bendas G and Borsig L. Cancer cell adhesion and metastasis: selectins, integrins, and the inhibitory potential of heparins. Int J Cell Biol. 2012; 2012:676731
    • (2012) Int J Cell Biol , vol.2012 , pp. 676731
    • Bendas, G.1    Borsig, L.2
  • 136
    • 0029858031 scopus 로고    scopus 로고
    • Selectins and their ligands: current concepts and controversies
    • Kansas GS. Selectins and their ligands: current concepts and controversies. Blood. 1996; 88:3259-3287
    • (1996) Blood , vol.88 , pp. 3259-3287
    • Kansas, G.S.1
  • 137
    • 0036966385 scopus 로고    scopus 로고
    • Glycosylation might provide endothelial zip codes for organ-specific leukocyte traffic into inflammatory sites
    • Renkonen J, Tynninen O, Hayry P, Paavonen T and Renkonen R. Glycosylation might provide endothelial zip codes for organ-specific leukocyte traffic into inflammatory sites. Am J Pathol. 2002; 161:543-550
    • (2002) Am J Pathol , vol.161 , pp. 543-550
    • Renkonen, J.1    Tynninen, O.2    Hayry, P.3    Paavonen, T.4    Renkonen, R.5
  • 138
    • 33745298519 scopus 로고    scopus 로고
    • Nuclear factor-kappaB in cancer development and progression
    • Karin M. Nuclear factor-kappaB in cancer development and progression. Nature. 2006; 441:431-436
    • (2006) Nature , vol.441 , pp. 431-436
    • Karin, M.1
  • 140
    • 34848904215 scopus 로고    scopus 로고
    • Glycosylation regulates turnover of cyclooxygenase-2
    • Sevigny MB, Li CF, Alas M and Hughes-Fulford M. Glycosylation regulates turnover of cyclooxygenase-2. FEBS Lett. 2006; 580(28-29):6533-6536
    • (2006) FEBS Lett , vol.580 , Issue.28-29 , pp. 6533-6536
    • Sevigny, M.B.1    Li, C.F.2    Alas, M.3    Hughes-Fulford, M.4
  • 141
    • 84858341862 scopus 로고    scopus 로고
    • Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors
    • Sevigny MB, Graham K, Ponce E, Louie MC and Mitchell K. Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors. Pharmacological research. 2012; 65:445-450
    • (2012) Pharmacological research , vol.65 , pp. 445-450
    • Sevigny, M.B.1    Graham, K.2    Ponce, E.3    Louie, M.C.4    Mitchell, K.5
  • 142
    • 84898045925 scopus 로고    scopus 로고
    • Involvement of a non-human sialic Acid in human cancer
    • Samraj AN, Laubli H, Varki N and Varki A. Involvement of a non-human sialic Acid in human cancer. Front Oncol. 2014; 4:33
    • (2014) Front Oncol , vol.4 , pp. 33
    • Samraj, A.N.1    Laubli, H.2    Varki, N.3    Varki, A.4
  • 143
    • 84938740862 scopus 로고    scopus 로고
    • Inflammatory cytokines regulate the expression of glycosyltransferases involved in the biosynthesis of tumor-associated sialylated glycans in pancreatic cancer cell lines
    • Bassaganas S, Allende H, Cobler L, Ortiz MR, Llop E, de Bolos C and Peracaula R. Inflammatory cytokines regulate the expression of glycosyltransferases involved in the biosynthesis of tumor-associated sialylated glycans in pancreatic cancer cell lines. Cytokine. 2015; 75:197-206
    • (2015) Cytokine , vol.75 , pp. 197-206
    • Bassaganas, S.1    Allende, H.2    Cobler, L.3    Ortiz, M.R.4    Llop, E.5    de Bolos, C.6    Peracaula, R.7
  • 147
    • 67349258025 scopus 로고    scopus 로고
    • Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation
    • Rabinovich GA and Toscano MA. Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nature reviews Immunology. 2009; 9:338-352
    • (2009) Nature reviews Immunology , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 149
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • Liu FT and Rabinovich GA. Galectins as modulators of tumour progression. Nat Rev Cancer. 2005; 5:29-41
    • (2005) Nat Rev Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 150
    • 84942921705 scopus 로고    scopus 로고
    • Galectin-Binding O-Glycosylations as Regulators of Malignancy
    • Dimitroff CJ. Galectin-Binding O-Glycosylations as Regulators of Malignancy. Cancer Res. 2015; 75:3195-3202
    • (2015) Cancer Res , vol.75 , pp. 3195-3202
    • Dimitroff, C.J.1
  • 151
    • 84890937257 scopus 로고    scopus 로고
    • Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion
    • Hudak JE, Canham SM and Bertozzi CR. Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion. Nat Chem Biol. 2014; 10:69-75
    • (2014) Nat Chem Biol , vol.10 , pp. 69-75
    • Hudak, J.E.1    Canham, S.M.2    Bertozzi, C.R.3
  • 156
    • 85016347273 scopus 로고    scopus 로고
    • Sialyl-tn in cancer: (how) did we miss the target?
    • Julien S, Videira PA and Delannoy P. Sialyl-tn in cancer: (how) did we miss the target? Biomolecules. 2012; 2:435-466
    • (2012) Biomolecules , vol.2 , pp. 435-466
    • Julien, S.1    Videira, P.A.2    Delannoy, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.