메뉴 건너뛰기




Volumn 4 MAR, Issue , 2014, Pages

Altered tumor-cell glycosylation promotes metastasis

Author keywords

Cancer; Galectins; Glycan ligands; Glycosylation; Metastasis; Mucins; Selectins; Siglecs

Indexed keywords

ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; GALECTIN; GALECTIN 1; GALECTIN 3; GEMTUZUMAB; GLYCAN; PADGEM PROTEIN; SELECTIN; SIALIC ACID BINDING IMMUNOGLOBULIN LIKE LECTIN; VASCULAR CELL ADHESION MOLECULE 1;

EID: 84898022102     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2014.00028     Document Type: Review
Times cited : (291)

References (236)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • doi: 10.1016/j.cell.2011.02.013
    • Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell (2011) 144:646-74. doi: 10.1016/j.cell.2011.02.013
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 0022262016 scopus 로고
    • Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives
    • Hakomori S. Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives. Cancer Res (1985) 45:2405-14.
    • (1985) Cancer Res , vol.45 , pp. 2405-2414
    • Hakomori, S.1
  • 3
    • 0030811894 scopus 로고    scopus 로고
    • Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer
    • doi:10.1023/A:1018532409041
    • Kannagi R. Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer. Glycoconj J (1997) 14:577-84. doi:10.1023/A:1018532409041
    • (1997) Glycoconj J , vol.14 , pp. 577-584
    • Kannagi, R.1
  • 4
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • doi:10.1023/A:1018580324971
    • Kim YJ, Varki A. Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj J (1997) 14:569-76. doi:10.1023/A:1018580324971
    • (1997) Glycoconj J , vol.14 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 5
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: glycans as novel therapeutic targets
    • doi:10.1038/nrc1649
    • Fuster MM, Esko JD. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat Rev Cancer (2005) 5:526-42. doi:10.1038/nrc1649
    • (2005) Nat Rev Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 6
    • 0032482987 scopus 로고    scopus 로고
    • P-selectin deficiency attenuates tumor growth and metastasis
    • doi:10.1073/pnas.95.16.9325
    • Kim YJ, Borsig L, Varki NM, Varki A. P-selectin deficiency attenuates tumor growth and metastasis. Proc Natl Acad Sci U S A (1998) 95:9325-30. doi:10.1073/pnas.95.16.9325
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 9325-9330
    • Kim, Y.J.1    Borsig, L.2    Varki, N.M.3    Varki, A.4
  • 7
    • 34548838824 scopus 로고    scopus 로고
    • Trousseau's syndrome: multiple definitions and multiple mechanisms
    • doi:10.1182/blood-2006-10-053736
    • Varki A. Trousseau's syndrome: multiple definitions and multiple mechanisms. Blood (2007) 110:1723-9. doi:10.1182/blood-2006-10-053736
    • (2007) Blood , vol.110 , pp. 1723-1729
    • Varki, A.1
  • 8
    • 84871485133 scopus 로고    scopus 로고
    • The initial hours of metastasis: the importance of cooperative host-tumor cell interactions during hematogenous dissemination
    • doi:10.1158/2159-8290.CD-12-0329
    • Labelle M, Hynes RO. The initial hours of metastasis: the importance of cooperative host-tumor cell interactions during hematogenous dissemination. Cancer Discov (2012) 2:1091-9. doi:10.1158/2159-8290.CD-12-0329
    • (2012) Cancer Discov , vol.2 , pp. 1091-1099
    • Labelle, M.1    Hynes, R.O.2
  • 9
    • 77956614939 scopus 로고    scopus 로고
    • Selectins promote tumor metastasis
    • doi:10.1016/j.semcancer.2010.04.005
    • Läubli H, Borsig L. Selectins promote tumor metastasis. Semin Cancer Biol (2010) 20:169-77. doi:10.1016/j.semcancer.2010.04.005
    • (2010) Semin Cancer Biol , vol.20 , pp. 169-177
    • Läubli, H.1    Borsig, L.2
  • 10
    • 38549159585 scopus 로고    scopus 로고
    • The selectin-selectin ligand axis in tumor progression
    • doi:10.1007/s10555-007-9101-z
    • Witz IP. The selectin-selectin ligand axis in tumor progression. Cancer Metastasis Rev (2008) 27:19-30. doi:10.1007/s10555-007-9101-z
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 19-30
    • Witz, I.P.1
  • 11
    • 0037133173 scopus 로고    scopus 로고
    • Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis
    • doi:10.1073/pnas.261704098
    • Borsig L, Wong R, Hynes RO, Varki NM, Varki A. Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis. Proc Natl Acad Sci U S A (2002) 99:2193-8. doi:10.1073/pnas.261704098
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2193-2198
    • Borsig, L.1    Wong, R.2    Hynes, R.O.3    Varki, N.M.4    Varki, A.5
  • 12
    • 84893846552 scopus 로고    scopus 로고
    • Metastatic growth progression caused by PSGL-1-mediated recruitment of monocytes to metastatic sites
    • doi:10.1158/0008-5472.CAN-13-0946
    • Hoos A, Protsyuk D, Borsig L. Metastatic growth progression caused by PSGL-1-mediated recruitment of monocytes to metastatic sites. Cancer Res (2014) 74:695-704. doi:10.1158/0008-5472.CAN-13-0946
    • (2014) Cancer Res , vol.74 , pp. 695-704
    • Hoos, A.1    Protsyuk, D.2    Borsig, L.3
  • 13
    • 32944476784 scopus 로고    scopus 로고
    • L-selectin facilitation of metastasis involves temporal induction of fut7-dependent ligands at sites of tumor cell arrest
    • doi:10.1158/0008-5472.CAN-05-3121
    • Läubli H, Stevenson JL, Varki A, Varki NM, Borsig L. L-selectin facilitation of metastasis involves temporal induction of fut7-dependent ligands at sites of tumor cell arrest. Cancer Res (2006) 66:1536-42. doi:10.1158/0008-5472.CAN-05-3121
    • (2006) Cancer Res , vol.66 , pp. 1536-1542
    • Läubli, H.1    Stevenson, J.L.2    Varki, A.3    Varki, N.M.4    Borsig, L.5
  • 14
    • 77952482466 scopus 로고    scopus 로고
    • Identification of Siglec-9 as the receptor for MUC16 on human NK cells, B cells, and monocytes.
    • doi:10.1186/1476-4598-9-118
    • Belisle JA, Horibata S, Jennifer GA, Petrie S, Kapur A, Andre S, et al. Identification of Siglec-9 as the receptor for MUC16 on human NK cells, B cells, and monocytes. Mol Cancer (2010) 9:118. doi:10.1186/1476-4598-9-118
    • (2010) Mol Cancer , vol.9 , pp. 118
    • Belisle, J.A.1    Horibata, S.2    Jennifer, G.A.3    Petrie, S.4    Kapur, A.5    Andre, S.6
  • 15
    • 84860348346 scopus 로고    scopus 로고
    • Colonic epithelial cells express specific ligands for mucosal macrophage immunosuppressive receptors siglec-7 and -9
    • doi:10.4049/jimmunol.1100605
    • Miyazaki K, Sakuma K, Kawamura YI, Izawa M, Ohmori K, Mitsuki M, et al. Colonic epithelial cells express specific ligands for mucosal macrophage immunosuppressive receptors siglec-7 and -9. J Immunol (2012) 188:4690-700. doi:10.4049/jimmunol.1100605
    • (2012) J Immunol , vol.188 , pp. 4690-4700
    • Miyazaki, K.1    Sakuma, K.2    Kawamura, Y.I.3    Izawa, M.4    Ohmori, K.5    Mitsuki, M.6
  • 16
    • 84867990611 scopus 로고    scopus 로고
    • Galectin-1 as a potent target for cancer therapy: role in the tumor microenvironment
    • doi:10.1007/s10555-012-9388-2
    • Ito K, Stannard K, Gabutero E, Clark AM, Neo SY, Onturk S, et al. Galectin-1 as a potent target for cancer therapy: role in the tumor microenvironment. Cancer Metastasis Rev (2012) 31:763-78. doi:10.1007/s10555-012-9388-2
    • (2012) Cancer Metastasis Rev , vol.31 , pp. 763-778
    • Ito, K.1    Stannard, K.2    Gabutero, E.3    Clark, A.M.4    Neo, S.Y.5    Onturk, S.6
  • 17
    • 0023255440 scopus 로고
    • Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • doi:10.1126/science.2953071
    • Dennis JW, Laferte S, Waghorne C, Breitman ML, Kerbel RS. Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science (1987) 236:582-5. doi:10.1126/science.2953071
    • (1987) Science , vol.236 , pp. 582-585
    • Dennis, J.W.1    Laferte, S.2    Waghorne, C.3    Breitman, M.L.4    Kerbel, R.S.5
  • 18
    • 53049084874 scopus 로고    scopus 로고
    • N-Glycans in cancer progression
    • doi:10.1093/glycob/cwn071
    • Lau KS, Dennis JW. N-Glycans in cancer progression. Glycobiology (2008) 18:750-60. doi:10.1093/glycob/cwn071
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 19
    • 34547610472 scopus 로고    scopus 로고
    • Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase
    • doi:10.1074/jbc.M611518200
    • Guo HB, Randolph M, Pierce M. Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase. J Biol Chem (2007) 282:22150-62. doi:10.1074/jbc.M611518200
    • (2007) J Biol Chem , vol.282 , pp. 22150-22162
    • Guo, H.B.1    Randolph, M.2    Pierce, M.3
  • 20
    • 33645822097 scopus 로고    scopus 로고
    • Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells
    • doi:10.1128/MCB.26.8.3181-3193.2006
    • Lagana A, Goetz JG, Cheung P, Raz A, Dennis JW, Nabi IR. Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells. Mol Cell Biol (2006) 26:3181-93. doi:10.1128/MCB.26.8.3181-3193.2006
    • (2006) Mol Cell Biol , vol.26 , pp. 3181-3193
    • Lagana, A.1    Goetz, J.G.2    Cheung, P.3    Raz, A.4    Dennis, J.W.5    Nabi, I.R.6
  • 21
    • 0034061923 scopus 로고    scopus 로고
    • Suppression of tumor growth and metastasis in Mgat5-deficient mice
    • doi:10.1038/73163
    • Granovsky M, Fata J, Pawling J, Muller WJ, Khokha R, Dennis JW. Suppression of tumor growth and metastasis in Mgat5-deficient mice. Nat Med (2000) 6:306-12. doi:10.1038/73163
    • (2000) Nat Med , vol.6 , pp. 306-312
    • Granovsky, M.1    Fata, J.2    Pawling, J.3    Muller, W.J.4    Khokha, R.5    Dennis, J.W.6
  • 22
    • 6044239186 scopus 로고    scopus 로고
    • Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis
    • doi:10.1126/science.1102109
    • Partridge EA, Le Roy C, Di Guglielmo GM, Pawling J, Cheung P, Granovsky M, et al. Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science (2004) 306:120-4. doi:10.1126/science.1102109
    • (2004) Science , vol.306 , pp. 120-124
    • Partridge, E.A.1    Le Roy, C.2    Di Guglielmo, G.M.3    Pawling, J.4    Cheung, P.5    Granovsky, M.6
  • 24
  • 26
    • 77949577301 scopus 로고    scopus 로고
    • Altered expression of glycan genes in cancers induced by epigenetic silencing and tumor hypoxia: clues in the ongoing search for new tumor markers
    • doi:10.1111/j.1349-7006.2009.01455.x
    • Kannagi R, Sakuma K, Miyazaki K, Lim KT, Yusa A, Yin J, et al. Altered expression of glycan genes in cancers induced by epigenetic silencing and tumor hypoxia: clues in the ongoing search for new tumor markers. Cancer Sci (2010) 101:586-93. doi:10.1111/j.1349-7006.2009.01455.x
    • (2010) Cancer Sci , vol.101 , pp. 586-593
    • Kannagi, R.1    Sakuma, K.2    Miyazaki, K.3    Lim, K.T.4    Yusa, A.5    Yin, J.6
  • 27
    • 2542588628 scopus 로고    scopus 로고
    • Hypoxia induces adhesion molecules on cancer cells: a missing link between Warburg effect and induction of selectin-ligand carbohydrates
    • doi:10.1073/pnas.0402088101
    • Koike T, Kimura N, Miyazaki K, Yabuta T, Kumamoto K, Takenoshita S, et al. Hypoxia induces adhesion molecules on cancer cells: a missing link between Warburg effect and induction of selectin-ligand carbohydrates. Proc Natl Acad Sci U S A (2004) 101:8132-7. doi:10.1073/pnas.0402088101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8132-8137
    • Koike, T.1    Kimura, N.2    Miyazaki, K.3    Yabuta, T.4    Kumamoto, K.5    Takenoshita, S.6
  • 28
    • 84867965064 scopus 로고    scopus 로고
    • Regulation of the metastatic cell phenotype by sialylated glycans
    • doi:10.1007/s10555-012-9359-7
    • Schultz MJ, Swindall AF, Bellis SL. Regulation of the metastatic cell phenotype by sialylated glycans. Cancer Metastasis Rev (2012) 31:501-18. doi:10.1007/s10555-012-9359-7
    • (2012) Cancer Metastasis Rev , vol.31 , pp. 501-518
    • Schultz, M.J.1    Swindall, A.F.2    Bellis, S.L.3
  • 29
    • 34547929295 scopus 로고    scopus 로고
    • Diversity in cell surface sialic acid presentations: implications for biology and disease
    • doi:10.1038/labinvest.3700656
    • Varki NM, Varki A. Diversity in cell surface sialic acid presentations: implications for biology and disease. Lab Invest (2007) 87:851-7. doi:10.1038/labinvest.3700656
    • (2007) Lab Invest , vol.87 , pp. 851-857
    • Varki, N.M.1    Varki, A.2
  • 30
    • 0024448635 scopus 로고
    • Increased CMP-NeuAc:Gal beta 1,4GlcNAc-R alpha 2,6 sialyltransferase activity in human colorectal cancer tissues
    • doi:10.1002/ijc.2910440309
    • Dall'Olio F, Malagolini N, di Stefano G, Minni F, Marrano D, Serafini-Cessi F. Increased CMP-NeuAc:Gal beta 1,4GlcNAc-R alpha 2,6 sialyltransferase activity in human colorectal cancer tissues. Int J Cancer (1989) 44:434-9. doi:10.1002/ijc.2910440309
    • (1989) Int J Cancer , vol.44 , pp. 434-439
    • Dall'Olio, F.1    Malagolini, N.2    di Stefano, G.3    Minni, F.4    Marrano, D.5    Serafini-Cessi, F.6
  • 31
    • 0027723424 scopus 로고
    • Enhanced activity of CMP-neuAc:Gal beta 1-4GlcNAc:alpha 2,6-sialyltransferase in metastasizing human colorectal tumor tissue and serum of tumor patients
    • doi:10.1016/0304-3835(93)90056-F
    • Gessner P, Riedl S, Quentmaier A, Kemmner W. Enhanced activity of CMP-neuAc:Gal beta 1-4GlcNAc:alpha 2,6-sialyltransferase in metastasizing human colorectal tumor tissue and serum of tumor patients. Cancer Lett (1993) 75:143-9. doi:10.1016/0304-3835(93)90056-F
    • (1993) Cancer Lett , vol.75 , pp. 143-149
    • Gessner, P.1    Riedl, S.2    Quentmaier, A.3    Kemmner, W.4
  • 32
    • 19644364143 scopus 로고    scopus 로고
    • Hypersialylation of beta1 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility
    • doi:10.1158/0008-5472.CAN-04-3117
    • Seales EC, Jurado GA, Brunson BA, Wakefield JK, Frost AR, Bellis SL. Hypersialylation of beta1 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility. Cancer Res (2005) 65:4645-52. doi:10.1158/0008-5472.CAN-04-3117
    • (2005) Cancer Res , vol.65 , pp. 4645-4652
    • Seales, E.C.1    Jurado, G.A.2    Brunson, B.A.3    Wakefield, J.K.4    Frost, A.R.5    Bellis, S.L.6
  • 34
    • 62049084618 scopus 로고    scopus 로고
    • Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4
    • doi:10.1038/onc.2008.471
    • Uemura T, Shiozaki K, Yamaguchi K, Miyazaki S, Satomi S, Kato K, et al. Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4. Oncogene (2009) 28:1218-29. doi:10.1038/onc.2008.471
    • (2009) Oncogene , vol.28 , pp. 1218-1229
    • Uemura, T.1    Shiozaki, K.2    Yamaguchi, K.3    Miyazaki, S.4    Satomi, S.5    Kato, K.6
  • 35
    • 18444395585 scopus 로고    scopus 로고
    • Comparative evaluation of the prognostic value of MUC1, MUC2, sialyl-Lewis(a) and sialyl-Lewis(x) antigens in colorectal adenocarcinoma
    • doi:10.1046/j.1365-2559.2002.01389.x
    • Baldus SE, Monig SP, Hanisch FG, Zirbes TK, Flucke U, Oelert S, et al. Comparative evaluation of the prognostic value of MUC1, MUC2, sialyl-Lewis(a) and sialyl-Lewis(x) antigens in colorectal adenocarcinoma. Histopathology (2002) 40:440-9. doi:10.1046/j.1365-2559.2002.01389.x
    • (2002) Histopathology , vol.40 , pp. 440-449
    • Baldus, S.E.1    Monig, S.P.2    Hanisch, F.G.3    Zirbes, T.K.4    Flucke, U.5    Oelert, S.6
  • 36
    • 0028895533 scopus 로고
    • Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin
    • doi:10.1172/JCI117700
    • Campbell BJ, Finnie IA, Hounsell EF, Rhodes JM. Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin. J Clin Invest (1995) 95:571-6. doi:10.1172/JCI117700
    • (1995) J Clin Invest , vol.95 , pp. 571-576
    • Campbell, B.J.1    Finnie, I.A.2    Hounsell, E.F.3    Rhodes, J.M.4
  • 37
    • 26444452697 scopus 로고    scopus 로고
    • Thomsen-Friedenreich and Tn antigens in nipple fluid: carbohydrate biomarkers for breast cancer detection
    • doi:10.1158/1078-0432.CCR-05-0146
    • Kumar SR, Sauter ER, Quinn TP, Deutscher SL. Thomsen-Friedenreich and Tn antigens in nipple fluid: carbohydrate biomarkers for breast cancer detection. Clin Cancer Res (2005) 11:6868-71. doi:10.1158/1078-0432.CCR-05-0146
    • (2005) Clin Cancer Res , vol.11 , pp. 6868-6871
    • Kumar, S.R.1    Sauter, E.R.2    Quinn, T.P.3    Deutscher, S.L.4
  • 38
    • 0028043999 scopus 로고
    • The Thomsen-Friedenreich antigen-related carbohydrate antigens in human gastric intestinal metaplasia and cancer
    • doi:10.1177/42.12.7527063
    • Sotozono MA, Okada Y, Tsuji T. The Thomsen-Friedenreich antigen-related carbohydrate antigens in human gastric intestinal metaplasia and cancer. J Histochem Cytochem (1994) 42:1575-84. doi:10.1177/42.12.7527063
    • (1994) J Histochem Cytochem , vol.42 , pp. 1575-1584
    • Sotozono, M.A.1    Okada, Y.2    Tsuji, T.3
  • 39
    • 0021141716 scopus 로고
    • T and Tn, general carcinoma autoantigens
    • doi:10.1126/science.6729450
    • Springer GF. T and Tn, general carcinoma autoantigens. Science (1984) 224:1198-206. doi:10.1126/science.6729450
    • (1984) Science , vol.224 , pp. 1198-1206
    • Springer, G.F.1
  • 40
    • 40949133707 scopus 로고    scopus 로고
    • Human tumor antigens Tn and sialyl Tn arise from mutations in Cosmc
    • doi:10.1158/0008-5472.CAN-07-2345
    • Ju T, Lanneau GS, Gautam T, Wang Y, Xia B, Stowell SR, et al. Human tumor antigens Tn and sialyl Tn arise from mutations in Cosmc. Cancer Res (2008) 68:1636-46. doi:10.1158/0008-5472.CAN-07-2345
    • (2008) Cancer Res , vol.68 , pp. 1636-1646
    • Ju, T.1    Lanneau, G.S.2    Gautam, T.3    Wang, Y.4    Xia, B.5    Stowell, S.R.6
  • 41
    • 3042820893 scopus 로고    scopus 로고
    • Loss of disialyl Lewis(a), the ligand for lymphocyte inhibitory receptor sialic acid-binding immunoglobulin-like lectin-7 (Siglec-7) associated with increased sialyl Lewis(a) expression on human colon cancers
    • doi:10.1158/0008-5472.CAN-03-3614
    • Miyazaki K, Ohmori K, Izawa M, Koike T, Kumamoto K, Furukawa K, et al. Loss of disialyl Lewis(a), the ligand for lymphocyte inhibitory receptor sialic acid-binding immunoglobulin-like lectin-7 (Siglec-7) associated with increased sialyl Lewis(a) expression on human colon cancers. Cancer Res (2004) 64:4498-505. doi:10.1158/0008-5472.CAN-03-3614
    • (2004) Cancer Res , vol.64 , pp. 4498-4505
    • Miyazaki, K.1    Ohmori, K.2    Izawa, M.3    Koike, T.4    Kumamoto, K.5    Furukawa, K.6
  • 42
    • 0038604168 scopus 로고    scopus 로고
    • Synthesis of disialyl Lewis a (Le(a)) structure in colon cancer cell lines by a sialyltransferase, ST6GalNAc VI, responsible for the synthesis of alpha-series gangliosides
    • doi:10.1074/jbc.M211034200
    • Tsuchida A, Okajima T, Furukawa K, Ando T, Ishida H, Yoshida A, et al. Synthesis of disialyl Lewis a (Le(a)) structure in colon cancer cell lines by a sialyltransferase, ST6GalNAc VI, responsible for the synthesis of alpha-series gangliosides. J Biol Chem (2003) 278:22787-94. doi:10.1074/jbc.M211034200
    • (2003) J Biol Chem , vol.278 , pp. 22787-22794
    • Tsuchida, A.1    Okajima, T.2    Furukawa, K.3    Ando, T.4    Ishida, H.5    Yoshida, A.6
  • 43
    • 0023038687 scopus 로고
    • Novel fucolipids of human adenocarcinoma: disialosyl Lea antigen (III4FucIII6NeuAcI V3NeuAcLc4) of human colonic adenocarcinoma and the monoclonal antibody (FH7) defining this structure
    • Nudelman E, Fukushi Y, Levery SB, Higuchi T, Hakomori S. Novel fucolipids of human adenocarcinoma: disialosyl Lea antigen (III4FucIII6NeuAcI V3NeuAcLc4) of human colonic adenocarcinoma and the monoclonal antibody (FH7) defining this structure. J Biol Chem (1986) 261:5487-95.
    • (1986) J Biol Chem , vol.261 , pp. 5487-5495
    • Nudelman, E.1    Fukushi, Y.2    Levery, S.B.3    Higuchi, T.4    Hakomori, S.5
  • 44
    • 0037049967 scopus 로고    scopus 로고
    • Reduced sialidase expression in highly metastatic variants of mouse colon adenocarcinoma 26 and retardation of their metastatic ability by sialidase overexpression
    • doi:10.1002/ijc.1598
    • Sawada M, Moriya S, Saito S, Shineha R, Satomi S, Yamori T, et al. Reduced sialidase expression in highly metastatic variants of mouse colon adenocarcinoma 26 and retardation of their metastatic ability by sialidase overexpression. Int J Cancer (2002) 97:180-5. doi:10.1002/ijc.1598
    • (2002) Int J Cancer , vol.97 , pp. 180-185
    • Sawada, M.1    Moriya, S.2    Saito, S.3    Shineha, R.4    Satomi, S.5    Yamori, T.6
  • 45
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: protection and control of the cell surface
    • doi:10.1038/nrc1251
    • Hollingsworth MA, Swanson BJ. Mucins in cancer: protection and control of the cell surface. Nat Rev Cancer (2004) 4:45-60. doi:10.1038/nrc1251
    • (2004) Nat Rev Cancer , vol.4 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 46
    • 33744799438 scopus 로고    scopus 로고
    • Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions
    • doi:10.1038/sj.embor.7400705
    • Brockhausen I. Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions. EMBO Rep (2006) 7:599-604. doi:10.1038/sj.embor.7400705
    • (2006) EMBO Rep , vol.7 , pp. 599-604
    • Brockhausen, I.1
  • 48
    • 20144367969 scopus 로고    scopus 로고
    • Core 3 synthase is down-regulated in colon carcinoma and profoundly suppresses the metastatic potential of carcinoma cells
    • doi:10.1073/pnas.0407983102
    • Iwai T, Kudo T, Kawamoto R, Kubota T, Togayachi A, Hiruma T, et al. Core 3 synthase is down-regulated in colon carcinoma and profoundly suppresses the metastatic potential of carcinoma cells. Proc Natl Acad Sci U S A (2005) 102:4572-7. doi:10.1073/pnas.0407983102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4572-4577
    • Iwai, T.1    Kudo, T.2    Kawamoto, R.3    Kubota, T.4    Togayachi, A.5    Hiruma, T.6
  • 49
    • 84885586596 scopus 로고    scopus 로고
    • Expression of core 3 synthase in human pancreatic cancer cells suppresses tumor growth and metastasis
    • doi:10.1002/ijc.28322
    • Radhakrishnan P, Grandgenett PM, Mohr AM, Bunt SK, Yu F, Chowdhury S, et al. Expression of core 3 synthase in human pancreatic cancer cells suppresses tumor growth and metastasis. Int J Cancer (2013) 133:2824-33. doi:10.1002/ijc.28322
    • (2013) Int J Cancer , vol.133 , pp. 2824-2833
    • Radhakrishnan, P.1    Grandgenett, P.M.2    Mohr, A.M.3    Bunt, S.K.4    Yu, F.5    Chowdhury, S.6
  • 50
    • 0035266352 scopus 로고    scopus 로고
    • Clinicopathological significance of core 2 beta1,6-N-acetylglucosaminyltransferase messenger RNA expressed in the pulmonary adenocarcinoma determined by in situ hybridization
    • Machida E, Nakayama J, Amano J, Fukuda M. Clinicopathological significance of core 2 beta1,6-N-acetylglucosaminyltransferase messenger RNA expressed in the pulmonary adenocarcinoma determined by in situ hybridization. Cancer Res (2001) 61:2226-31.
    • (2001) Cancer Res , vol.61 , pp. 2226-2231
    • Machida, E.1    Nakayama, J.2    Amano, J.3    Fukuda, M.4
  • 51
    • 0030658888 scopus 로고    scopus 로고
    • Carcinoma-associated expression of core 2 beta-1,6-N-acetylglucosaminyltransferase gene in human colorectal cancer: role of O-glycans in tumor progression
    • Shimodaira K, Nakayama J, Nakamura N, Hasebe O, Katsuyama T, Fukuda M. Carcinoma-associated expression of core 2 beta-1,6-N-acetylglucosaminyltransferase gene in human colorectal cancer: role of O-glycans in tumor progression. Cancer Res (1997) 57:5201-6.
    • (1997) Cancer Res , vol.57 , pp. 5201-5206
    • Shimodaira, K.1    Nakayama, J.2    Nakamura, N.3    Hasebe, O.4    Katsuyama, T.5    Fukuda, M.6
  • 52
    • 63849339429 scopus 로고    scopus 로고
    • The high affinity selectin glycan ligand C2-O-sLex and mRNA transcripts of the core 2 beta-1,6-N-acetylglucosaminyltransferase (C2GnT1) gene are highly expressed in human colorectal adenocarcinomas.
    • doi:10.1186/1471-2407-9-79
    • St Hill CA, Farooqui M, Mitcheltree G, Gulbahce HE, Jessurun J, Cao Q, et al. The high affinity selectin glycan ligand C2-O-sLex and mRNA transcripts of the core 2 beta-1,6-N-acetylglucosaminyltransferase (C2GnT1) gene are highly expressed in human colorectal adenocarcinomas. BMC Cancer (2009) 9:79. doi:10.1186/1471-2407-9-79
    • (2009) BMC Cancer , vol.9 , pp. 79
    • St Hill, C.A.1    Farooqui, M.2    Mitcheltree, G.3    Gulbahce, H.E.4    Jessurun, J.5    Cao, Q.6
  • 53
    • 0028841588 scopus 로고
    • Mechanisms underlying aberrant glycosylation of MUC1 mucin in breast cancer cells
    • doi:10.1111/j.1432-1033.1995.607_2.x
    • Brockhausen I, Yang JM, Burchell J, Whitehouse C, Taylor-Papadimitriou J. Mechanisms underlying aberrant glycosylation of MUC1 mucin in breast cancer cells. Eur J Biochem (1995) 233:607-17. doi:10.1111/j.1432-1033.1995.607_2.x
    • (1995) Eur J Biochem , vol.233 , pp. 607-617
    • Brockhausen, I.1    Yang, J.M.2    Burchell, J.3    Whitehouse, C.4    Taylor-Papadimitriou, J.5
  • 54
    • 0035405258 scopus 로고    scopus 로고
    • O-linked glycosylation in the mammary gland: changes that occur during malignancy
    • doi:10.1023/A:1011331809881
    • Burchell JM, Mungul A, Taylor-Papadimitriou J. O-linked glycosylation in the mammary gland: changes that occur during malignancy. J Mammary Gland Biol Neoplasia (2001) 6:355-64. doi:10.1023/A:1011331809881
    • (2001) J Mammary Gland Biol Neoplasia , vol.6 , pp. 355-364
    • Burchell, J.M.1    Mungul, A.2    Taylor-Papadimitriou, J.3
  • 55
    • 0035815609 scopus 로고    scopus 로고
    • The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1
    • doi:10.1074/jbc.M006523200
    • Dalziel M, Whitehouse C, McFarlane I, Brockhausen I, Gschmeissner S, Schwientek T, et al. The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. J Biol Chem (2001) 276:11007-15. doi:10.1074/jbc.M006523200
    • (2001) J Biol Chem , vol.276 , pp. 11007-11015
    • Dalziel, M.1    Whitehouse, C.2    McFarlane, I.3    Brockhausen, I.4    Gschmeissner, S.5    Schwientek, T.6
  • 56
    • 84863195565 scopus 로고    scopus 로고
    • MUC1 in human and murine mammary carcinoma cells decreases the expression of core 2 beta1,6-N-acetylglucosaminyltransferase and beta-galactoside alpha2,3-sialyltransferase
    • doi:10.1093/glycob/cws075
    • Solatycka A, Owczarek T, Piller F, Piller V, Pula B, Wojciech L, et al. MUC1 in human and murine mammary carcinoma cells decreases the expression of core 2 beta1,6-N-acetylglucosaminyltransferase and beta-galactoside alpha2,3-sialyltransferase. Glycobiology (2012) 22:1042-54. doi:10.1093/glycob/cws075
    • (2012) Glycobiology , vol.22 , pp. 1042-1054
    • Solatycka, A.1    Owczarek, T.2    Piller, F.3    Piller, V.4    Pula, B.5    Wojciech, L.6
  • 57
    • 11544370976 scopus 로고    scopus 로고
    • Gene expression of fucosyl- and sialyl-transferases which synthesize sialyl Lewisx, the carbohydrate ligands for E-selectin, in human breast cancer
    • Matsuura N, Narita T, Hiraiwa N, Hiraiwa M, Murai H, Iwase T, et al. Gene expression of fucosyl- and sialyl-transferases which synthesize sialyl Lewisx, the carbohydrate ligands for E-selectin, in human breast cancer. Int J Oncol (1998) 12:1157-64.
    • (1998) Int J Oncol , vol.12 , pp. 1157-1164
    • Matsuura, N.1    Narita, T.2    Hiraiwa, N.3    Hiraiwa, M.4    Murai, H.5    Iwase, T.6
  • 58
    • 0029764743 scopus 로고    scopus 로고
    • Thomsen-Friedenreich-related carbohydrate antigens in normal adult human tissues: a systematic and comparative study
    • doi:10.1007/BF02484401
    • Cao Y, Stosiek P, Springer GF, Karsten U. Thomsen-Friedenreich-related carbohydrate antigens in normal adult human tissues: a systematic and comparative study. Histochem Cell Biol (1996) 106:197-207. doi:10.1007/BF02484401
    • (1996) Histochem Cell Biol , vol.106 , pp. 197-207
    • Cao, Y.1    Stosiek, P.2    Springer, G.F.3    Karsten, U.4
  • 59
    • 0019955052 scopus 로고
    • Blood group precursor T-antigen expression in human urinary bladder carcinoma
    • Coon JS, Weinstein RS, Summers JL. Blood group precursor T-antigen expression in human urinary bladder carcinoma. Am J Clin Pathol (1982) 77:692-9.
    • (1982) Am J Clin Pathol , vol.77 , pp. 692-699
    • Coon, J.S.1    Weinstein, R.S.2    Summers, J.L.3
  • 62
    • 0022479171 scopus 로고
    • T-antigen in normal and neoplastic urothelium
    • doi:10.1002/1097-0142(19860915)58:6<1236::AID-CNCR2820580611>3.0.CO;2-I
    • Limas C, Lange P. T-antigen in normal and neoplastic urothelium. Cancer (1986) 58:1236-45. doi:10.1002/1097-0142(19860915)58:6<1236::AID-CNCR2820580611>3.0.CO;2-I
    • (1986) Cancer , vol.58 , pp. 1236-1245
    • Limas, C.1    Lange, P.2
  • 63
    • 0030765682 scopus 로고    scopus 로고
    • Selection of tumor antigens as targets for immune attack using immunohistochemistry: II. Blood group-related antigens.
    • doi:10.1002/(SICI)1097-0215(19970926)73:1<42::AID-IJC8>3.0.CO;2-1
    • Zhang S, Zhang HS, Cordon-Cardo C, Reuter VE, Singhal AK, Lloyd KO, et al. Selection of tumor antigens as targets for immune attack using immunohistochemistry: II. Blood group-related antigens. Int J Cancer (1997) 73:50-6. doi:10.1002/(SICI)1097-0215(19970926)73:1<42::AID-IJC8>3.0.CO;2-1
    • (1997) Int J Cancer , vol.73 , pp. 50-56
    • Zhang, S.1    Zhang, H.S.2    Cordon-Cardo, C.3    Reuter, V.E.4    Singhal, A.K.5    Lloyd, K.O.6
  • 64
    • 0034101785 scopus 로고    scopus 로고
    • Expression of carbohydrate antigens in advanced-stage ovarian carcinomas and their metastases-A clinicopathologic study
    • doi:10.1006/gyno.1999.5708
    • Davidson B, Gotlieb WH, Ben-Baruch G, Kopolovic J, Goldberg I, Nesland JM, et al. Expression of carbohydrate antigens in advanced-stage ovarian carcinomas and their metastases-A clinicopathologic study. Gynecol Oncol (2000) 77:35-43. doi:10.1006/gyno.1999.5708
    • (2000) Gynecol Oncol , vol.77 , pp. 35-43
    • Davidson, B.1    Gotlieb, W.H.2    Ben-Baruch, G.3    Kopolovic, J.4    Goldberg, I.5    Nesland, J.M.6
  • 65
    • 0026928690 scopus 로고
    • Mucins: structure, function, and associations with malignancy
    • doi:10.1002/bies.950140909
    • Devine PL, McKenzie IF. Mucins: structure, function, and associations with malignancy. Bioessays (1992) 14:619-25. doi:10.1002/bies.950140909
    • (1992) Bioessays , vol.14 , pp. 619-625
    • Devine, P.L.1    McKenzie, I.F.2
  • 66
    • 34848915825 scopus 로고    scopus 로고
    • The oncofetal Thomsen-Friedenreich carbohydrate antigen in cancer progression
    • doi:10.1007/s10719-007-9034-3
    • Yu LG. The oncofetal Thomsen-Friedenreich carbohydrate antigen in cancer progression. Glycoconj J (2007) 24:411-20. doi:10.1007/s10719-007-9034-3
    • (2007) Glycoconj J , vol.24 , pp. 411-420
    • Yu, L.G.1
  • 67
    • 0035526308 scopus 로고    scopus 로고
    • Expression of sialyl-Tn antigen in breast cancer cells transfected with the human CMP-Neu5Ac: GalNAc alpha2,6-sialyltransferase (ST6GalNac I) cDNA
    • doi:10.1023/A:1022200525695
    • Julien S, Krzewinski-Recchi MA, Harduin-Lepers A, Gouyer V, Huet G, Le Bourhis X, et al. Expression of sialyl-Tn antigen in breast cancer cells transfected with the human CMP-Neu5Ac: GalNAc alpha2,6-sialyltransferase (ST6GalNac I) cDNA. Glycoconj J (2001) 18:883-93. doi:10.1023/A:1022200525695
    • (2001) Glycoconj J , vol.18 , pp. 883-893
    • Julien, S.1    Krzewinski-Recchi, M.A.2    Harduin-Lepers, A.3    Gouyer, V.4    Huet, G.5    Le Bourhis, X.6
  • 68
    • 84857366326 scopus 로고    scopus 로고
    • Enhancement of metastatic ability by ectopic expression of ST6GalNAcI on a gastric cancer cell line in a mouse model
    • doi:10.1007/s10585-011-9445-1
    • Ozaki H, Matsuzaki H, Ando H, Kaji H, Nakanishi H, Ikehara Y, et al. Enhancement of metastatic ability by ectopic expression of ST6GalNAcI on a gastric cancer cell line in a mouse model. Clin Exp Metastasis (2012) 29:229-38. doi:10.1007/s10585-011-9445-1
    • (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
  • 69
    • 0028564771 scopus 로고
    • Alterations of O-glycan biosynthesis in human colon cancer tissues
    • doi:10.1093/glycob/4.6.873
    • Yang JM, Byrd JC, Siddiki BB, Chung YS, Okuno M, Sowa M, et al. Alterations of O-glycan biosynthesis in human colon cancer tissues. Glycobiology (1994) 4:873-84. doi:10.1093/glycob/4.6.873
    • (1994) Glycobiology , vol.4 , pp. 873-884
    • Yang, J.M.1    Byrd, J.C.2    Siddiki, B.B.3    Chung, Y.S.4    Okuno, M.5    Sowa, M.6
  • 70
    • 0032760680 scopus 로고    scopus 로고
    • Pathways of O-glycan biosynthesis in cancer cells
    • doi:10.1016/S0304-4165(99)00170-1
    • Brockhausen I. Pathways of O-glycan biosynthesis in cancer cells. Biochim Biophys Acta (1999) 1473:67-95. doi:10.1016/S0304-4165(99)00170-1
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 67-95
    • Brockhausen, I.1
  • 71
    • 4944265751 scopus 로고    scopus 로고
    • Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the cancer-associated sialyl-Tn antigen
    • doi:10.1158/0008-5472.CAN-04-1921
    • Marcos NT, Pinho S, Grandela C, Cruz A, Samyn-Petit B, Harduin-Lepers A, et al. Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the cancer-associated sialyl-Tn antigen. Cancer Res (2004) 64:7050-7. doi:10.1158/0008-5472.CAN-04-1921
    • (2004) Cancer Res , vol.64 , pp. 7050-7057
    • Marcos, N.T.1    Pinho, S.2    Grandela, C.3    Cruz, A.4    Samyn-Petit, B.5    Harduin-Lepers, A.6
  • 72
    • 0035361378 scopus 로고    scopus 로고
    • Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas
    • Schneider F, Kemmner W, Haensch W, Franke G, Gretschel S, Karsten U, et al. Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas. Cancer Res (2001) 61:4605-11.
    • (2001) Cancer Res , vol.61 , pp. 4605-4611
    • Schneider, F.1    Kemmner, W.2    Haensch, W.3    Franke, G.4    Gretschel, S.5    Karsten, U.6
  • 73
    • 0035361603 scopus 로고    scopus 로고
    • Increased expression of UDP-galactose transporter messenger RNA in human colon cancer tissues and its implication in synthesis of Thomsen-Friedenreich antigen and Sialyl Lewis A/X determinants
    • Kumamoto K, Goto Y, Sekikawa K, Takenoshita S, Ishida N, Kawakita M, et al. Increased expression of UDP-galactose transporter messenger RNA in human colon cancer tissues and its implication in synthesis of Thomsen-Friedenreich antigen and Sialyl Lewis A/X determinants. Cancer Res (2001) 61:4620-7.
    • (2001) Cancer Res , vol.61 , pp. 4620-4627
    • Kumamoto, K.1    Goto, Y.2    Sekikawa, K.3    Takenoshita, S.4    Ishida, N.5    Kawakita, M.6
  • 74
    • 0037168608 scopus 로고    scopus 로고
    • A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase
    • doi:10.1073/pnas.262438199
    • Ju T, Cummings RD. A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase. Proc Natl Acad Sci U S A (2002) 99:16613-8. doi:10.1073/pnas.262438199
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16613-16618
    • Ju, T.1    Cummings, R.D.2
  • 75
    • 33749989239 scopus 로고    scopus 로고
    • A mutant chaperone converts a wild-type protein into a tumor-specific antigen
    • doi:10.1126/science.1129200
    • Schietinger A, Philip M, Yoshida BA, Azadi P, Liu H, Meredith SC, et al. A mutant chaperone converts a wild-type protein into a tumor-specific antigen. Science (2006) 314:304-8. doi:10.1126/science.1129200
    • (2006) Science , vol.314 , pp. 304-308
    • Schietinger, A.1    Philip, M.2    Yoshida, B.A.3    Azadi, P.4    Liu, H.5    Meredith, S.C.6
  • 76
    • 84875412068 scopus 로고    scopus 로고
    • Suppression of core 1 Gal-transferase is associated with reduction of TF and reciprocal increase of Tn, sialyl-Tn and Core 3 glycans in human colon cancer cells.
    • doi:10.1371/journal.pone.0059792
    • Barrow H, Tam B, Duckworth CA, Rhodes JM, Yu LG. Suppression of core 1 Gal-transferase is associated with reduction of TF and reciprocal increase of Tn, sialyl-Tn and Core 3 glycans in human colon cancer cells. PLoS One (2013) 8:e59792. doi:10.1371/journal.pone.0059792
    • (2013) PLoS One , vol.8
    • Barrow, H.1    Tam, B.2    Duckworth, C.A.3    Rhodes, J.M.4    Yu, L.G.5
  • 77
    • 29444454759 scopus 로고    scopus 로고
    • ST6GalNAc I expression in MDA-MB-231 breast cancer cells greatly modifies their O-glycosylation pattern and enhances their tumourigenicity
    • doi:10.1093/glycob/cwj033
    • Julien S, Adriaenssens E, Ottenberg K, Furlan A, Courtand G, Vercoutter-Edouart AS, et al. ST6GalNAc I expression in MDA-MB-231 breast cancer cells greatly modifies their O-glycosylation pattern and enhances their tumourigenicity. Glycobiology (2006) 16:54-64. doi:10.1093/glycob/cwj033
    • (2006) Glycobiology , vol.16 , pp. 54-64
    • Julien, S.1    Adriaenssens, E.2    Ottenberg, K.3    Furlan, A.4    Courtand, G.5    Vercoutter-Edouart, A.S.6
  • 78
    • 0033233461 scopus 로고    scopus 로고
    • An alpha2,3 sialyltransferase (ST3Gal I) is elevated in primary breast carcinomas
    • doi:10.1093/glycob/9.12.1307
    • Burchell J, Poulsom R, Hanby A, Whitehouse C, Cooper L, Clausen H, et al. An alpha2,3 sialyltransferase (ST3Gal I) is elevated in primary breast carcinomas. Glycobiology (1999) 9:1307-11. doi:10.1093/glycob/9.12.1307
    • (1999) Glycobiology , vol.9 , pp. 1307-1311
    • Burchell, J.1    Poulsom, R.2    Hanby, A.3    Whitehouse, C.4    Cooper, L.5    Clausen, H.6
  • 79
  • 80
    • 0032521020 scopus 로고    scopus 로고
    • Coexpression of MUC1 mucin peptide core and the Thomsen-Friedenreich antigen in colorectal neoplasms
    • doi:10.1002/(SICI)1097-0142(19980315)82:6<1019::AID-CNCR3>3.0.CO;2-9
    • Baldus SE, Hanisch FG, Kotlarek GM, Zirbes TK, Thiele J, Isenberg J, et al. Coexpression of MUC1 mucin peptide core and the Thomsen-Friedenreich antigen in colorectal neoplasms. Cancer (1998) 82:1019-27. doi:10.1002/(SICI)1097-0142(19980315)82:6<1019::AID-CNCR3>3.0.CO;2-9
    • (1998) Cancer , vol.82 , pp. 1019-1027
    • Baldus, S.E.1    Hanisch, F.G.2    Kotlarek, G.M.3    Zirbes, T.K.4    Thiele, J.5    Isenberg, J.6
  • 81
    • 0030827120 scopus 로고    scopus 로고
    • Oligosaccharides expressed on MUC1 produced by pancreatic and colon tumor cell lines
    • doi:10.1074/jbc.272.39.24198
    • Burdick MD, Harris A, Reid CJ, Iwamura T, Hollingsworth MA. Oligosaccharides expressed on MUC1 produced by pancreatic and colon tumor cell lines. J Biol Chem (1997) 272:24198-202. doi:10.1074/jbc.272.39.24198
    • (1997) J Biol Chem , vol.272 , pp. 24198-24202
    • Burdick, M.D.1    Harris, A.2    Reid, C.J.3    Iwamura, T.4    Hollingsworth, M.A.5
  • 82
    • 0034914003 scopus 로고    scopus 로고
    • Cell surface-expressed Thomsen-Friedenreich antigen in colon cancer is predominantly carried on high molecular weight splice variants of CD44
    • doi:10.1093/glycob/11.7.587
    • Singh R, Campbell BJ, Yu LG, Fernig DG, Milton JD, Goodlad RA, et al. Cell surface-expressed Thomsen-Friedenreich antigen in colon cancer is predominantly carried on high molecular weight splice variants of CD44. Glycobiology (2001) 11:587-92. doi:10.1093/glycob/11.7.587
    • (2001) Glycobiology , vol.11 , pp. 587-592
    • Singh, R.1    Campbell, B.J.2    Yu, L.G.3    Fernig, D.G.4    Milton, J.D.5    Goodlad, R.A.6
  • 83
    • 44449107032 scopus 로고    scopus 로고
    • The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum
    • doi:10.1093/glycob/cwn022
    • Storr SJ, Royle L, Chapman CJ, Hamid UM, Robertson JF, Murray A, et al. The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum. Glycobiology (2008) 18:456-62. doi:10.1093/glycob/cwn022
    • (2008) Glycobiology , vol.18 , pp. 456-462
    • Storr, S.J.1    Royle, L.2    Chapman, C.J.3    Hamid, U.M.4    Robertson, J.F.5    Murray, A.6
  • 84
    • 77649216263 scopus 로고    scopus 로고
    • MUC2 mucin is a major carrier of the cancer-associated sialyl-Tn antigen in intestinal metaplasia and gastric carcinomas
    • doi:10.1093/glycob/cwp161
    • Conze T, Carvalho AS, Landegren U, Almeida R, Reis CA, David L, et al. MUC2 mucin is a major carrier of the cancer-associated sialyl-Tn antigen in intestinal metaplasia and gastric carcinomas. Glycobiology (2010) 20:199-206. doi:10.1093/glycob/cwp161
    • (2010) Glycobiology , vol.20 , pp. 199-206
    • Conze, T.1    Carvalho, A.S.2    Landegren, U.3    Almeida, R.4    Reis, C.A.5    David, L.6
  • 85
    • 0026002788 scopus 로고
    • CD44 splice variants confer metastatic behavior in rats: homologous sequences are expressed in human tumor cell lines
    • Hofmann M, Rudy W, Zoller M, Tolg C, Ponta H, Herrlich P, et al. CD44 splice variants confer metastatic behavior in rats: homologous sequences are expressed in human tumor cell lines. Cancer Res (1991) 51:5292-7.
    • (1991) Cancer Res , vol.51 , pp. 5292-5297
    • Hofmann, M.1    Rudy, W.2    Zoller, M.3    Tolg, C.4    Ponta, H.5    Herrlich, P.6
  • 86
    • 0037227965 scopus 로고    scopus 로고
    • CD44: from adhesion molecules to signalling regulators
    • doi:10.1038/nrm1004
    • Ponta H, Sherman L, Herrlich PA. CD44: from adhesion molecules to signalling regulators. Nat Rev Mol Cell Biol (2003) 4:33-45. doi:10.1038/nrm1004
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 33-45
    • Ponta, H.1    Sherman, L.2    Herrlich, P.A.3
  • 87
    • 6344258588 scopus 로고    scopus 로고
    • The role of Osteopontin in tumor metastasis
    • doi:10.1016/j.jss.2004.03.028
    • Wai PY, Kuo PC. The role of Osteopontin in tumor metastasis. J Surg Res (2004) 121:228-41. doi:10.1016/j.jss.2004.03.028
    • (2004) J Surg Res , vol.121 , pp. 228-241
    • Wai, P.Y.1    Kuo, P.C.2
  • 88
    • 0025778637 scopus 로고
    • Mucin production by human colonic carcinoma cells correlates with their metastatic potential in animal models of colon cancer metastasis
    • doi:10.1172/JCI115063
    • Bresalier RS, Niv Y, Byrd JC, Duh QY, Toribara NW, Rockwell RW, et al. Mucin production by human colonic carcinoma cells correlates with their metastatic potential in animal models of colon cancer metastasis. J Clin Invest (1991) 87:1037-45. doi:10.1172/JCI115063
    • (1991) J Clin Invest , vol.87 , pp. 1037-1045
    • Bresalier, R.S.1    Niv, Y.2    Byrd, J.C.3    Duh, Q.Y.4    Toribara, N.W.5    Rockwell, R.W.6
  • 89
    • 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, et al. Increased expression of sialyl Lewisx antigen correlates with poor survival in patients with colorectal carcinoma: clinicopathological and immunohistochemical study. Cancer Res (1993) 53:3632-7.
    • (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
  • 90
    • 8744286641 scopus 로고    scopus 로고
    • Expression of sialyl-Tn epitopes on beta1 integrin alters epithelial cell phenotype, proliferation and haptotaxis
    • doi:10.1242/jcs.01350
    • Clement M, Rocher J, Loirand G, Le Pendu J. Expression of sialyl-Tn epitopes on beta1 integrin alters epithelial cell phenotype, proliferation and haptotaxis. J Cell Sci (2004) 117:5059-69. doi:10.1242/jcs.01350
    • (2004) J Cell Sci , vol.117 , pp. 5059-5069
    • Clement, M.1    Rocher, J.2    Loirand, G.3    Le Pendu, J.4
  • 91
    • 84862818251 scopus 로고    scopus 로고
    • pp-GalNAc-T13 induces high metastatic potential of murine Lewis lung cancer by generating trimeric Tn antigen
    • doi:10.1016/j.bbrc.2012.01.086
    • Matsumoto Y, Zhang Q, Akita K, Nakada H, Hamamura K, Tokuda N, et al. pp-GalNAc-T13 induces high metastatic potential of murine Lewis lung cancer by generating trimeric Tn antigen. Biochem Biophys Res Commun (2012) 419:7-13. doi:10.1016/j.bbrc.2012.01.086
    • (2012) Biochem Biophys Res Commun , vol.419 , pp. 7-13
    • Matsumoto, Y.1    Zhang, Q.2    Akita, K.3    Nakada, H.4    Hamamura, K.5    Tokuda, N.6
  • 92
    • 84889591821 scopus 로고    scopus 로고
    • B3GNT3 expression suppresses cell migration and invasion and predicts favorable outcomes in neuroblastoma
    • doi:10.1111/cas.12294
    • Ho WL, Che MI, Chou CH, Chang HH, Jeng YM, Hsu WM, et al. B3GNT3 expression suppresses cell migration and invasion and predicts favorable outcomes in neuroblastoma. Cancer Sci (2013) 104:1600-8. doi:10.1111/cas.12294
    • (2013) Cancer Sci , vol.104 , pp. 1600-1608
    • Ho, W.L.1    Che, M.I.2    Chou, C.H.3    Chang, H.H.4    Jeng, Y.M.5    Hsu, W.M.6
  • 93
    • 84860234082 scopus 로고    scopus 로고
    • CD33-related siglecs as potential modulators of inflammatory responses
    • doi:10.1111/j.1749-6632.2011.06449.x
    • Crocker PR, McMillan SJ, Richards HE. CD33-related siglecs as potential modulators of inflammatory responses. Ann N Y Acad Sci (2012) 1253:102-11. doi:10.1111/j.1749-6632.2011.06449.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 102-111
    • Crocker, P.R.1    McMillan, S.J.2    Richards, H.E.3
  • 94
    • 65349147691 scopus 로고    scopus 로고
    • Siglecs as targets for therapy in immune-cell-mediated disease
    • doi:10.1016/j.tips.2009.02.005
    • O'Reilly MK, Paulson JC. Siglecs as targets for therapy in immune-cell-mediated disease. Trends Pharmacol Sci (2009) 30:240-8. doi:10.1016/j.tips.2009.02.005
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 240-248
    • O'Reilly, M.K.1    Paulson, J.C.2
  • 95
    • 84859416185 scopus 로고    scopus 로고
    • Multifarious roles of sialic acids in immunity
    • doi:10.1111/j.1749-6632.2012.06517.x
    • Varki A, Gagneux P. Multifarious roles of sialic acids in immunity. Ann N Y Acad Sci (2012) 1253:16-36. doi:10.1111/j.1749-6632.2012.06517.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 16-36
    • Varki, A.1    Gagneux, P.2
  • 96
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • doi:10.1038/nri2056
    • Crocker PR, Paulson JC, Varki A. Siglecs and their roles in the immune system. Nat Rev Immunol (2007) 7:255-66. doi:10.1038/nri2056
    • (2007) Nat Rev Immunol , vol.7 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 97
    • 34248662079 scopus 로고    scopus 로고
    • Negative regulation of leucocyte functions by CD33-related siglecs
    • doi:10.1042/BST0341024
    • Avril T, Attrill H, Zhang J, Raper A, Crocker PR. Negative regulation of leucocyte functions by CD33-related siglecs. Biochem Soc Trans (2006) 34:1024-7. doi:10.1042/BST0341024
    • (2006) Biochem Soc Trans , vol.34 , pp. 1024-1027
    • Avril, T.1    Attrill, H.2    Zhang, J.3    Raper, A.4    Crocker, P.R.5
  • 98
    • 4544283824 scopus 로고    scopus 로고
    • Expression of CD33-related siglecs on human mononuclear phagocytes, monocyte-derived dendritic cells and plasmacytoid dendritic cells
    • doi:10.1016/j.imbio.2004.04.007
    • Lock K, Zhang J, Lu J, Lee SH, Crocker PR. Expression of CD33-related siglecs on human mononuclear phagocytes, monocyte-derived dendritic cells and plasmacytoid dendritic cells. Immunobiology (2004) 209:199-207. doi:10.1016/j.imbio.2004.04.007
    • (2004) Immunobiology , vol.209 , pp. 199-207
    • Lock, K.1    Zhang, J.2    Lu, J.3    Lee, S.H.4    Crocker, P.R.5
  • 99
    • 0038044928 scopus 로고    scopus 로고
    • Ligation of Siglec-8: a selective mechanism for induction of human eosinophil apoptosis
    • doi:10.1182/blood-2002-10-3058
    • Nutku E, Aizawa H, Hudson SA, Bochner BS. Ligation of Siglec-8: a selective mechanism for induction of human eosinophil apoptosis. Blood (2003) 101:5014-20. doi:10.1182/blood-2002-10-3058
    • (2003) Blood , vol.101 , pp. 5014-5020
    • Nutku, E.1    Aizawa, H.2    Hudson, S.A.3    Bochner, B.S.4
  • 100
    • 84860252480 scopus 로고    scopus 로고
    • Glycobiology of immune responses
    • doi:10.1111/j.1749-6632.2012.06492.x
    • Rabinovich GA, van Kooyk Y, Cobb BA. Glycobiology of immune responses. Ann N Y Acad Sci (2012) 1253:1-15. doi:10.1111/j.1749-6632.2012.06492.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 1-15
    • Rabinovich, G.A.1    van Kooyk, Y.2    Cobb, B.A.3
  • 101
    • 84872001426 scopus 로고    scopus 로고
    • The interaction between Siglec-15 and tumor-associated sialyl-Tn antigen enhances TGF-beta secretion from monocytes/macrophages through the DAP12-Syk pathway
    • doi:10.1093/glycob/cws139
    • Takamiya R, Ohtsubo K, Takamatsu S, Taniguchi N, Angata T. The interaction between Siglec-15 and tumor-associated sialyl-Tn antigen enhances TGF-beta secretion from monocytes/macrophages through the DAP12-Syk pathway. Glycobiology (2013) 23:178-87. doi:10.1093/glycob/cws139
    • (2013) Glycobiology , vol.23 , pp. 178-187
    • Takamiya, R.1    Ohtsubo, K.2    Takamatsu, S.3    Taniguchi, N.4    Angata, T.5
  • 102
    • 0023003625 scopus 로고
    • Properties and distribution of a lectin-like hemagglutinin differentially expressed by murine stromal tissue macrophages
    • doi:10.1084/jem.164.6.1862
    • Crocker PR, Gordon S. Properties and distribution of a lectin-like hemagglutinin differentially expressed by murine stromal tissue macrophages. J Exp Med (1986) 164:1862-75. doi:10.1084/jem.164.6.1862
    • (1986) J Exp Med , vol.164 , pp. 1862-1875
    • Crocker, P.R.1    Gordon, S.2
  • 103
    • 29044438130 scopus 로고    scopus 로고
    • CD14 and CD169 expression in human lymph nodes and spleen: specific expansion of CD14+CD169- monocyte-derived cells in diffuse large B-cell lymphomas
    • doi:10.1016/j.humpath.2005.09.016
    • Marmey B, Boix C, Barbaroux JB, Dieu-Nosjean MC, Diebold J, Audouin J, et al. CD14 and CD169 expression in human lymph nodes and spleen: specific expansion of CD14+CD169- monocyte-derived cells in diffuse large B-cell lymphomas. Hum Pathol (2006) 37:68-77. doi:10.1016/j.humpath.2005.09.016
    • (2006) Hum Pathol , vol.37 , pp. 68-77
    • Marmey, B.1    Boix, C.2    Barbaroux, J.B.3    Dieu-Nosjean, M.C.4    Diebold, J.5    Audouin, J.6
  • 104
    • 0032862879 scopus 로고    scopus 로고
    • Macrophage-tumour cell interactions: identification of MUC1 on breast cancer cells as a potential counter-receptor for the macrophage-restricted receptor, sialoadhesin
    • doi:10.1046/j.1365-2567.1999.00827.x
    • Nath D, Hartnell A, Happerfield L, Miles DW, Burchell J, Taylor-Papadimitriou J, et al. Macrophage-tumour cell interactions: identification of MUC1 on breast cancer cells as a potential counter-receptor for the macrophage-restricted receptor, sialoadhesin. Immunology (1999) 98:213-9. doi:10.1046/j.1365-2567.1999.00827.x
    • (1999) Immunology , vol.98 , pp. 213-219
    • Nath, D.1    Hartnell, A.2    Happerfield, L.3    Miles, D.W.4    Burchell, J.5    Taylor-Papadimitriou, J.6
  • 105
    • 0028116948 scopus 로고
    • Tumor-derived monocyte chemoattractant protein-1 induces intratumoral infiltration of monocyte-derived macrophage subpopulation in transplanted rat tumors
    • Yamashiro S, Takeya M, Nishi T, Kuratsu J, Yoshimura T, Ushio Y, et al. Tumor-derived monocyte chemoattractant protein-1 induces intratumoral infiltration of monocyte-derived macrophage subpopulation in transplanted rat tumors. Am J Pathol (1994) 145:856-67.
    • (1994) Am J Pathol , vol.145 , pp. 856-867
    • Yamashiro, S.1    Takeya, M.2    Nishi, T.3    Kuratsu, J.4    Yoshimura, T.5    Ushio, Y.6
  • 106
    • 84883465032 scopus 로고    scopus 로고
    • CD169-positive macrophages in regional lymph nodes are associated with a favorable prognosis in patients with colorectal carcinoma
    • doi:10.1111/cas.12212
    • Ohnishi K, Komohara Y, Saito Y, Miyamoto Y, Watanabe M, Baba H, et al. CD169-positive macrophages in regional lymph nodes are associated with a favorable prognosis in patients with colorectal carcinoma. Cancer Sci (2013) 104:1237-44. doi:10.1111/cas.12212
    • (2013) Cancer Sci , vol.104 , pp. 1237-1244
    • Ohnishi, K.1    Komohara, Y.2    Saito, Y.3    Miyamoto, Y.4    Watanabe, M.5    Baba, H.6
  • 107
    • 0026469373 scopus 로고
    • Serum CA125 regression in epithelial ovarian cancer: correlation with reassessment findings and survival
    • doi:10.1016/0090-8258(92)90082-T
    • Buller RE, Berman ML, Bloss JD, Manetta A, DiSaia PJ. Serum CA125 regression in epithelial ovarian cancer: correlation with reassessment findings and survival. Gynecol Oncol (1992) 47:87-92. doi:10.1016/0090-8258(92)90082-T
    • (1992) Gynecol Oncol , vol.47 , pp. 87-92
    • Buller, R.E.1    Berman, M.L.2    Bloss, J.D.3    Manetta, A.4    DiSaia, P.J.5
  • 108
    • 41149114476 scopus 로고    scopus 로고
    • Siglec-9 enhances IL-10 production in macrophages via tyrosine-based motifs
    • doi:10.1016/j.bbrc.2008.02.111
    • Ando M, Tu W, Nishijima K, Iijima S. Siglec-9 enhances IL-10 production in macrophages via tyrosine-based motifs. Biochem Biophys Res Commun (2008) 369:878-83. doi:10.1016/j.bbrc.2008.02.111
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 878-883
    • Ando, M.1    Tu, W.2    Nishijima, K.3    Iijima, S.4
  • 109
    • 77957855197 scopus 로고    scopus 로고
    • Ganglioside DSGb5, preferred ligand for Siglec-7, inhibits NK cell cytotoxicity against renal cell carcinoma cells
    • doi:10.1093/glycob/cwq116
    • Kawasaki Y, Ito A, Withers DA, Taima T, Kakoi N, Saito S, et al. Ganglioside DSGb5, preferred ligand for Siglec-7, inhibits NK cell cytotoxicity against renal cell carcinoma cells. Glycobiology (2010) 20:1373-9. doi:10.1093/glycob/cwq116
    • (2010) Glycobiology , vol.20 , pp. 1373-1379
    • Kawasaki, Y.1    Ito, A.2    Withers, D.A.3    Taima, T.4    Kakoi, N.5    Saito, S.6
  • 110
    • 84890937257 scopus 로고    scopus 로고
    • Glygocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion
    • doi:10.1038/nchembio.1388
    • Hudak JE, Canham SM, Bertozzi CR. Glygocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion. Nat Chem Biol (2014) 10:69-75. doi:10.1038/nchembio.1388
    • (2014) Nat Chem Biol , vol.10 , pp. 69-75
    • Hudak, J.E.1    Canham, S.M.2    Bertozzi, C.R.3
  • 111
    • 84887109254 scopus 로고    scopus 로고
    • Binding of the sialic acid-binding lectin
    • doi:10.1074/jbc.M113.471318
    • Tanida S, Akita K, Ishida A, Mori Y, Toda M, Inoue M, et al. Binding of the sialic acid-binding lectin. J Biol Chem (2013) 288:31842-52. doi:10.1074/jbc.M113.471318
    • (2013) J Biol Chem , vol.288 , pp. 31842-31852
    • Tanida, S.1    Akita, K.2    Ishida, A.3    Mori, Y.4    Toda, M.5    Inoue, M.6
  • 112
    • 0023683935 scopus 로고
    • In vitro purging of bone marrow for autologous marrow transplantation in acute myelogenous leukemia using myeloid-specific monoclonal antibodies
    • Ball ED. In vitro purging of bone marrow for autologous marrow transplantation in acute myelogenous leukemia using myeloid-specific monoclonal antibodies. Bone Marrow Transplant (1988) 3:387-92.
    • (1988) Bone Marrow Transplant , vol.3 , pp. 387-392
    • Ball, E.D.1
  • 113
    • 0023585057 scopus 로고
    • Classification of acute myeloid leukemias - a comparison of FAB and immunophenotyping
    • Drexler HG. Classification of acute myeloid leukemias - a comparison of FAB and immunophenotyping. Leukemia (1987) 1:697-705.
    • (1987) Leukemia , vol.1 , pp. 697-705
    • Drexler, H.G.1
  • 114
    • 0022655602 scopus 로고
    • Induction of features characteristic of hairy cell leukemia in chronic lymphocytic leukemia and prolymphocytic leukemia cells
    • Ziegler-Heitbrock HW, Munker R, Dorken B, Gaedicke G, Thiel E. Induction of features characteristic of hairy cell leukemia in chronic lymphocytic leukemia and prolymphocytic leukemia cells. Cancer Res (1986) 46:2172-8.
    • (1986) Cancer Res , vol.46 , pp. 2172-2178
    • Ziegler-Heitbrock, H.W.1    Munker, R.2    Dorken, B.3    Gaedicke, G.4    Thiel, E.5
  • 115
    • 79960371234 scopus 로고    scopus 로고
    • Targeting siglecs - a novel pharmacological strategy for immuno- and glycotherapy
    • doi:10.1016/j.bcp.2011.05.018
    • Jandus C, Simon HU, von Gunten S. Targeting siglecs - a novel pharmacological strategy for immuno- and glycotherapy. Biochem Pharmacol (2011) 82:323-32. doi:10.1016/j.bcp.2011.05.018
    • (2011) Biochem Pharmacol , vol.82 , pp. 323-332
    • Jandus, C.1    Simon, H.U.2    von Gunten, S.3
  • 116
    • 84898039457 scopus 로고    scopus 로고
    • Inotuzumab ozogamicin in the treatment of acute lymphoblastic leukemia
    • doi:10.2741/E688
    • Jain N, O Brien S, Thomas D, Kantarjian H. Inotuzumab ozogamicin in the treatment of acute lymphoblastic leukemia. Front Biosci (Elite Ed) (2014) 6:40-5. doi:10.2741/E688
    • (2014) Front Biosci (Elite Ed) , vol.6 , pp. 40-45
    • Jain, N.1    O'Brien, S.2    Thomas, D.3    Kantarjian, H.4
  • 117
    • 84880574025 scopus 로고    scopus 로고
    • Results of inotuzumab ozogamicin, a CD22 monoclonal antibody, in refractory and relapsed acute lymphocytic leukemia
    • doi:10.1002/cncr.28136
    • Kantarjian H, Thomas D, Jorgensen J, Kebriaei P, Jabbour E, Rytting M, et al. Results of inotuzumab ozogamicin, a CD22 monoclonal antibody, in refractory and relapsed acute lymphocytic leukemia. Cancer (2013) 119:2728-36. doi:10.1002/cncr.28136
    • (2013) Cancer , vol.119 , pp. 2728-2736
    • Kantarjian, H.1    Thomas, D.2    Jorgensen, J.3    Kebriaei, P.4    Jabbour, E.5    Rytting, M.6
  • 118
    • 84881305790 scopus 로고    scopus 로고
    • A phase 3 study of gemtuzumab ozogamicin during induction and postconsolidation therapy in younger patients with acute myeloid leukemia
    • doi:10.1182/blood-2013-01-466706
    • Petersdorf SH, Kopecky KJ, Slovak M, Willman C, Nevill T, Brandwein J, et al. A phase 3 study of gemtuzumab ozogamicin during induction and postconsolidation therapy in younger patients with acute myeloid leukemia. Blood (2013) 121:4854-60. doi:10.1182/blood-2013-01-466706
    • (2013) Blood , vol.121 , pp. 4854-4860
    • Petersdorf, S.H.1    Kopecky, K.J.2    Slovak, M.3    Willman, C.4    Nevill, T.5    Brandwein, J.6
  • 119
    • 84893006506 scopus 로고    scopus 로고
    • Antibody therapy for acute myeloid leukaemia
    • doi:10.1111/bjh.12691
    • Gasiorowski RE, Clark GJ, Bradstock K, Hart DN. Antibody therapy for acute myeloid leukaemia. Br J Haematol (2013) 164:481-75. doi:10.1111/bjh.12691
    • (2013) Br J Haematol , vol.164 , pp. 481-575
    • Gasiorowski, R.E.1    Clark, G.J.2    Bradstock, K.3    Hart, D.N.4
  • 120
    • 84886825064 scopus 로고    scopus 로고
    • SGN-CD33A: a novel CD33-targeting antibody-drug conjugate using a pyrrolobenzodiazepine dimer is active in models of drug-resistant AML
    • doi:10.1182/blood-2013-03-491506
    • Kung Sutherland MS, Walter RB, Jeffrey SC, Burke PJ, Yu C, Kostner H, et al. SGN-CD33A: a novel CD33-targeting antibody-drug conjugate using a pyrrolobenzodiazepine dimer is active in models of drug-resistant AML. Blood (2013) 122:1455-63. doi:10.1182/blood-2013-03-491506
    • (2013) Blood , vol.122 , pp. 1455-1463
    • Kung Sutherland, M.S.1    Walter, R.B.2    Jeffrey, S.C.3    Burke, P.J.4    Yu, C.5    Kostner, H.6
  • 121
    • 67349258025 scopus 로고    scopus 로고
    • Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation
    • doi:10.1038/nri2536
    • Rabinovich GA, Toscano MA. Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat Rev Immunol (2009) 9:338-52. doi:10.1038/nri2536
    • (2009) Nat Rev Immunol , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 122
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • doi:10.1038/nrc1527
    • Liu FT, Rabinovich GA. Galectins as modulators of tumour progression. Nat Rev Cancer (2005) 5:29-41. doi:10.1038/nrc1527
    • (2005) Nat Rev Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 124
    • 1542373600 scopus 로고    scopus 로고
    • Galectin-3 and metastasis
    • doi:10.1023/B:GLYC.0000014084.01324.15
    • Takenaka Y, Fukumori T, Raz A. Galectin-3 and metastasis. Glycoconj J (2004) 19:543-9. doi:10.1023/B:GLYC.0000014084.01324.15
    • (2004) Glycoconj J , vol.19 , pp. 543-549
    • Takenaka, Y.1    Fukumori, T.2    Raz, A.3
  • 125
    • 79959887879 scopus 로고    scopus 로고
    • Tumor galectin-1 mediates tumor growth and metastasis through regulation of T-cell apoptosis
    • doi:10.1158/0008-5472.CAN-10-4157
    • Banh A, Zhang J, Cao H, Bouley DM, Kwok S, Kong C, et al. Tumor galectin-1 mediates tumor growth and metastasis through regulation of T-cell apoptosis. Cancer Res (2011) 71:4423-31. doi:10.1158/0008-5472.CAN-10-4157
    • (2011) Cancer Res , vol.71 , pp. 4423-4431
    • Banh, A.1    Zhang, J.2    Cao, H.3    Bouley, D.M.4    Kwok, S.5    Kong, C.6
  • 126
    • 12144285871 scopus 로고    scopus 로고
    • Targeted inhibition of galectin-1 gene expression in tumor cells results in heightened T cell-mediated rejection; a potential mechanism of tumor-immune privilege
    • doi:10.1016/S1535-6108(04)00024-8
    • Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, et al. Targeted inhibition of galectin-1 gene expression in tumor cells results in heightened T cell-mediated rejection; a potential mechanism of tumor-immune privilege. Cancer Cell (2004) 5:241-51. doi:10.1016/S1535-6108(04)00024-8
    • (2004) Cancer Cell , vol.5 , pp. 241-251
    • Rubinstein, N.1    Alvarez, M.2    Zwirner, N.W.3    Toscano, M.A.4    Ilarregui, J.M.5    Bravo, A.6
  • 127
    • 84856960944 scopus 로고    scopus 로고
    • High expression of Galectin-1 in pancreatic stellate cells plays a role in the development and maintenance of an immunosuppressive microenvironment in pancreatic cancer
    • doi:10.1002/ijc.26290
    • Tang D, Yuan Z, Xue X, Lu Z, Zhang Y, Wang H, et al. High expression of Galectin-1 in pancreatic stellate cells plays a role in the development and maintenance of an immunosuppressive microenvironment in pancreatic cancer. Int J Cancer (2012) 130:2337-48. doi:10.1002/ijc.26290
    • (2012) Int J Cancer , vol.130 , pp. 2337-2348
    • Tang, D.1    Yuan, Z.2    Xue, X.3    Lu, Z.4    Zhang, Y.5    Wang, H.6
  • 128
    • 33749514807 scopus 로고    scopus 로고
    • Galectin-1 binds different CD43 glycoforms to cluster CD43 and regulate T cell death
    • Hernandez JD, Nguyen JT, He J, Wang W, Ardman B, Green JM, et al. Galectin-1 binds different CD43 glycoforms to cluster CD43 and regulate T cell death. J Immunol (2006) 177:5328-36.
    • (2006) J Immunol , vol.177 , pp. 5328-5336
    • Hernandez, J.D.1    Nguyen, J.T.2    He, J.3    Wang, W.4    Ardman, B.5    Green, J.M.6
  • 129
    • 0035889895 scopus 로고    scopus 로고
    • CD45 modulates galectin-1-induced T cell death: regulation by expression of core 2 O-glycans
    • Nguyen JT, Evans DP, Galvan M, Pace KE, Leitenberg D, Bui TN, et al. CD45 modulates galectin-1-induced T cell death: regulation by expression of core 2 O-glycans. J Immunol (2001) 167:5697-707.
    • (2001) J Immunol , vol.167 , pp. 5697-5707
    • Nguyen, J.T.1    Evans, D.P.2    Galvan, M.3    Pace, K.E.4    Leitenberg, D.5    Bui, T.N.6
  • 130
    • 0037470066 scopus 로고    scopus 로고
    • The ST6Gal I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death
    • doi:10.1074/jbc.M209595200
    • Amano M, Galvan M, He J, Baum LG. The ST6Gal I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death. J Biol Chem (2003) 278:7469-75. doi:10.1074/jbc.M209595200
    • (2003) J Biol Chem , vol.278 , pp. 7469-7475
    • Amano, M.1    Galvan, M.2    He, J.3    Baum, L.G.4
  • 131
    • 79251546096 scopus 로고    scopus 로고
    • Lung cancer-derived galectin-1 mediates dendritic cell anergy through inhibitor of DNA binding 3/IL-10 signaling pathway
    • doi:10.4049/jimmunol.1002940
    • Kuo PL, Hung JY, Huang SK, Chou SH, Cheng DE, Jong YJ, et al. Lung cancer-derived galectin-1 mediates dendritic cell anergy through inhibitor of DNA binding 3/IL-10 signaling pathway. J Immunol (2011) 186:1521-30. doi:10.4049/jimmunol.1002940
    • (2011) J Immunol , vol.186 , pp. 1521-1530
    • Kuo, P.L.1    Hung, J.Y.2    Huang, S.K.3    Chou, S.H.4    Cheng, D.E.5    Jong, Y.J.6
  • 132
    • 84873449312 scopus 로고    scopus 로고
    • Targeting galectin-1 overcomes breast cancer-associated immunosuppression and prevents metastatic disease
    • doi:10.1158/0008-5472.CAN-12-2418
    • Dalotto-Moreno T, Croci DO, Cerliani JP, Martinez-Allo VC, Dergan-Dylon S, Mendez-Huergo SP, et al. Targeting galectin-1 overcomes breast cancer-associated immunosuppression and prevents metastatic disease. Cancer Res (2013) 73:1107-17. doi:10.1158/0008-5472.CAN-12-2418
    • (2013) Cancer Res , vol.73 , pp. 1107-1117
    • Dalotto-Moreno, T.1    Croci, D.O.2    Cerliani, J.P.3    Martinez-Allo, V.C.4    Dergan-Dylon, S.5    Mendez-Huergo, S.P.6
  • 133
    • 0031959770 scopus 로고    scopus 로고
    • Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death
    • doi:10.1007/s001090050232
    • Perillo NL, Marcus ME, Baum LG. Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death. J Mol Med (Berl) (1998) 76:402-12. doi:10.1007/s001090050232
    • (1998) J Mol Med (Berl) , vol.76 , pp. 402-412
    • Perillo, N.L.1    Marcus, M.E.2    Baum, L.G.3
  • 134
    • 0037344258 scopus 로고    scopus 로고
    • Galectin-1 accumulation in the ovary carcinoma peritumoral stroma is induced by ovary carcinoma cells and affects both cancer cell proliferation and adhesion to laminin-1 and fibronectin
    • doi:10.1097/01.LAB.0000059949.01480.40
    • van den Brule F, Califice S, Garnier F, Fernandez PL, Berchuck A, Castronovo V. Galectin-1 accumulation in the ovary carcinoma peritumoral stroma is induced by ovary carcinoma cells and affects both cancer cell proliferation and adhesion to laminin-1 and fibronectin. Lab Invest (2003) 83:377-86. doi:10.1097/01.LAB.0000059949.01480.40
    • (2003) Lab Invest , vol.83 , pp. 377-386
    • van den Brule, F.1    Califice, S.2    Garnier, F.3    Fernandez, P.L.4    Berchuck, A.5    Castronovo, V.6
  • 135
    • 42049121650 scopus 로고    scopus 로고
    • The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation
    • doi:10.1096/fj.07-9524com
    • Pacienza N, Pozner RG, Bianco GA, D'Atri LP, Croci DO, Negrotto S, et al. The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation. FASEB J (2008) 22:1113-23. doi:10.1096/fj.07-9524com
    • (2008) FASEB J , vol.22 , pp. 1113-1123
    • Pacienza, N.1    Pozner, R.G.2    Bianco, G.A.3    D'Atri, L.P.4    Croci, D.O.5    Negrotto, S.6
  • 137
  • 138
    • 0037423206 scopus 로고    scopus 로고
    • MDA-MB-435 human breast carcinoma cell homo- and heterotypic adhesion under flow conditions is mediated in part by Thomsen-Friedenreich antigen-galectin-3 interactions
    • Khaldoyanidi SK, Glinsky VV, Sikora L, Glinskii AB, Mossine VV, Quinn TP, et al. MDA-MB-435 human breast carcinoma cell homo- and heterotypic adhesion under flow conditions is mediated in part by Thomsen-Friedenreich antigen-galectin-3 interactions. J Biol Chem (2003) 278:4127-34.
    • (2003) J Biol Chem , vol.278 , pp. 4127-4134
    • Khaldoyanidi, S.K.1    Glinsky, V.V.2    Sikora, L.3    Glinskii, A.B.4    Mossine, V.V.5    Quinn, T.P.6
  • 139
    • 77953627018 scopus 로고    scopus 로고
    • Interaction between circulating galectin-3 and cancer-associated MUC1 enhances tumour cell homotypic aggregation and prevents anoikis.
    • doi:10.1186/1476-4598-9-154
    • Zhao Q, Barclay M, Hilkens J, Guo X, Barrow H, Rhodes JM, et al. Interaction between circulating galectin-3 and cancer-associated MUC1 enhances tumour cell homotypic aggregation and prevents anoikis. Mol Cancer (2010) 9:154. doi:10.1186/1476-4598-9-154
    • (2010) Mol Cancer , vol.9 , pp. 154
    • Zhao, Q.1    Barclay, M.2    Hilkens, J.3    Guo, X.4    Barrow, H.5    Rhodes, J.M.6
  • 140
    • 0035874890 scopus 로고    scopus 로고
    • The role of Thomsen-Friedenreich antigen in adhesion of human breast and prostate cancer cells to the endothelium
    • Glinsky VV, Glinsky GV, Rittenhouse-Olson K, Huflejt ME, Glinskii OV, Deutscher SL, et al. The role of Thomsen-Friedenreich antigen in adhesion of human breast and prostate cancer cells to the endothelium. Cancer Res (2001) 61:4851-7.
    • (2001) Cancer Res , vol.61 , pp. 4851-4857
    • Glinsky, V.V.1    Glinsky, G.V.2    Rittenhouse-Olson, K.3    Huflejt, M.E.4    Glinskii, O.V.5    Deutscher, S.L.6
  • 141
    • 23944471882 scopus 로고    scopus 로고
    • Altered melanoma cell surface glycosylation mediates organ specific adhesion and metastasis via lectin receptors on the lung vascular endothelium
    • doi:10.1007/s10585-005-2036-2
    • Krishnan V, Bane SM, Kawle PD, Naresh KN, Kalraiya RD. Altered melanoma cell surface glycosylation mediates organ specific adhesion and metastasis via lectin receptors on the lung vascular endothelium. Clin Exp Metastasis (2005) 22:11-24. doi:10.1007/s10585-005-2036-2
    • (2005) Clin Exp Metastasis , vol.22 , pp. 11-24
    • Krishnan, V.1    Bane, S.M.2    Kawle, P.D.3    Naresh, K.N.4    Kalraiya, R.D.5
  • 142
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • doi:10.1016/j.cell.2007.01.049
    • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, Demetriou M, et al. Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell (2007) 129:123-34. doi:10.1016/j.cell.2007.01.049
    • (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
  • 143
    • 22944456543 scopus 로고    scopus 로고
    • Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours
    • doi:10.1111/j.1440-1711.2005.01351.x
    • Kobata A, Amano J. Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours. Immunol Cell Biol (2005) 83:429-39. doi:10.1111/j.1440-1711.2005.01351.x
    • (2005) Immunol Cell Biol , vol.83 , pp. 429-439
    • Kobata, A.1    Amano, J.2
  • 144
    • 0032558738 scopus 로고    scopus 로고
    • The her-2/neu oncogene stimulates the transcription of N-acetylglucosaminyltransferase V and expression of its cell surface oligosaccharide products
    • doi:10.1038/sj.onc.1202124
    • Chen L, Zhang W, Fregien N, Pierce M. The her-2/neu oncogene stimulates the transcription of N-acetylglucosaminyltransferase V and expression of its cell surface oligosaccharide products. Oncogene (1998) 17:2087-93. doi:10.1038/sj.onc.1202124
    • (1998) Oncogene , vol.17 , pp. 2087-2093
    • Chen, L.1    Zhang, W.2    Fregien, N.3    Pierce, M.4
  • 145
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V
    • doi:10.1083/jcb.130.2.383
    • Demetriou M, Nabi IR, Coppolino M, Dedhar S, Dennis JW. Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J Cell Biol (1995) 130:383-92. doi:10.1083/jcb.130.2.383
    • (1995) J Cell Biol , vol.130 , pp. 383-392
    • Demetriou, M.1    Nabi, I.R.2    Coppolino, M.3    Dedhar, S.4    Dennis, J.W.5
  • 146
    • 35549010724 scopus 로고    scopus 로고
    • Plasma membrane domain organization regulates EGFR signaling in tumor cells
    • doi:10.1083/jcb.200611106
    • Lajoie P, Partridge EA, Guay G, Goetz JG, Pawling J, Lagana A, et al. Plasma membrane domain organization regulates EGFR signaling in tumor cells. J Cell Biol (2007) 179:341-56. doi:10.1083/jcb.200611106
    • (2007) J Cell Biol , vol.179 , pp. 341-356
    • Lajoie, P.1    Partridge, E.A.2    Guay, G.3    Goetz, J.G.4    Pawling, J.5    Lagana, A.6
  • 147
    • 79961023938 scopus 로고    scopus 로고
    • A novel strategy for evasion of NK cell immunity by tumours expressing core2 O-glycans
    • doi:10.1038/emboj.2011.215
    • Tsuboi S, Sutoh M, Hatakeyama S, Hiraoka N, Habuchi T, Horikawa Y, et al. A novel strategy for evasion of NK cell immunity by tumours expressing core2 O-glycans. EMBO J (2011) 30:3173-85. doi:10.1038/emboj.2011.215
    • (2011) EMBO J , vol.30 , pp. 3173-3185
    • Tsuboi, S.1    Sutoh, M.2    Hatakeyama, S.3    Hiraoka, N.4    Habuchi, T.5    Horikawa, Y.6
  • 148
    • 79960720473 scopus 로고    scopus 로고
    • Glycosylation, galectins and cellular signaling
    • doi:10.1016/j.ceb.2011.05.001
    • Boscher C, Dennis JW, Nabi IR. Glycosylation, galectins and cellular signaling. Curr Opin Cell Biol (2011) 23:383-92. doi:10.1016/j.ceb.2011.05.001
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 383-392
    • Boscher, C.1    Dennis, J.W.2    Nabi, I.R.3
  • 149
    • 0028988148 scopus 로고
    • Glycosylation of beta-1 integrins in B16-F10 mouse melanoma cells as determinant of differential binding and acquisition of biological activity
    • doi:10.1002/ijc.2910610324
    • Veiga SS, Chammas R, Cella N, Brentani RR. Glycosylation of beta-1 integrins in B16-F10 mouse melanoma cells as determinant of differential binding and acquisition of biological activity. Int J Cancer (1995) 61:420-4. doi:10.1002/ijc.2910610324
    • (1995) Int J Cancer , vol.61 , pp. 420-424
    • Veiga, S.S.1    Chammas, R.2    Cella, N.3    Brentani, R.R.4
  • 150
    • 0028239080 scopus 로고
    • Functional role of N-glycosylation in alpha 5 beta 1 integrin receptor. De-N-glycosylation induces dissociation or altered association of alpha 5 and beta 1 subunits and concomitant loss of fibronectin binding activity.
    • Zheng M, Fang H, Hakomori S. Functional role of N-glycosylation in alpha 5 beta 1 integrin receptor. De-N-glycosylation induces dissociation or altered association of alpha 5 and beta 1 subunits and concomitant loss of fibronectin binding activity. J Biol Chem (1994) 269:12325-31.
    • (1994) J Biol Chem , vol.269 , pp. 12325-12331
    • Zheng, M.1    Fang, H.2    Hakomori, S.3
  • 151
    • 0036894568 scopus 로고    scopus 로고
    • Aberrant N-glycosylation of beta1 integrin causes reduced alpha5beta1 integrin clustering and stimulates cell migration
    • Guo HB, Lee I, Kamar M, Akiyama SK, Pierce M. Aberrant N-glycosylation of beta1 integrin causes reduced alpha5beta1 integrin clustering and stimulates cell migration. Cancer Res (2002) 62:6837-45.
    • (2002) Cancer Res , vol.62 , pp. 6837-6845
    • Guo, H.B.1    Lee, I.2    Kamar, M.3    Akiyama, S.K.4    Pierce, M.5
  • 152
    • 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) 88:3259-87.
    • (1996) Blood , vol.88 , pp. 3259-3287
    • Kansas, G.S.1
  • 153
    • 0029793468 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation
    • Guyer DA, Moore KL, Lynam EB, Schammel CM, Rogelj S, McEver RP, et al. P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation. Blood (1996) 88:2415-21.
    • (1996) Blood , vol.88 , pp. 2415-2421
    • Guyer, D.A.1    Moore, K.L.2    Lynam, E.B.3    Schammel, C.M.4    Rogelj, S.5    McEver, R.P.6
  • 154
    • 0038190854 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 mediates L-selectin-dependent leukocyte rolling in venules
    • doi:10.1084/jem.20021854
    • Sperandio M, Smith ML, Forlow SB, Olson TS, Xia L, McEver RP, et al. P-selectin glycoprotein ligand-1 mediates L-selectin-dependent leukocyte rolling in venules. J Exp Med (2003) 197:1355-63. doi:10.1084/jem.20021854
    • (2003) J Exp Med , vol.197 , pp. 1355-1363
    • Sperandio, M.1    Smith, M.L.2    Forlow, S.B.3    Olson, T.S.4    Xia, L.5    McEver, R.P.6
  • 155
    • 20544439303 scopus 로고    scopus 로고
    • In vivo imaging of specialized bone marrow endothelial microdomains for tumour engraftment
    • doi:10.1038/nature03703
    • Sipkins DA, Wei X, Wu JW, Runnels JM, Cote D, Means TK, et al. In vivo imaging of specialized bone marrow endothelial microdomains for tumour engraftment. Nature (2005) 435:969-73. doi:10.1038/nature03703
    • (2005) Nature , vol.435 , pp. 969-973
    • Sipkins, D.A.1    Wei, X.2    Wu, J.W.3    Runnels, J.M.4    Cote, D.5    Means, T.K.6
  • 156
    • 0028197560 scopus 로고
    • Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells
    • doi:10.1083/jcb.125.2.471
    • Lenter M, Levinovitz A, Isenmann S, Vestweber D. Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells. J Cell Biol (1994) 125:471-81. doi:10.1083/jcb.125.2.471
    • (1994) J Cell Biol , vol.125 , pp. 471-481
    • Lenter, M.1    Levinovitz, A.2    Isenmann, S.3    Vestweber, D.4
  • 157
    • 0037376540 scopus 로고    scopus 로고
    • Colon carcinoma cell glycolipids, integrins, and other glycoproteins mediate adhesion to HUVECs under flow.
    • doi:10.1152/ajpcell.00423.2002
    • Burdick MM, McCaffery JM, Kim YS, Bochner BS, Konstantopoulos K. Colon carcinoma cell glycolipids, integrins, and other glycoproteins mediate adhesion to HUVECs under flow. Am J Physiol Cell Physiol (2003) 284:C977-87. doi:10.1152/ajpcell.00423.2002
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Burdick, M.M.1    McCaffery, J.M.2    Kim, Y.S.3    Bochner, B.S.4    Konstantopoulos, K.5
  • 158
    • 0032771908 scopus 로고    scopus 로고
    • Distinct selectin ligands on colon carcinoma mucins can mediate pathological interactions among platelets, leukocytes, and endothelium
    • doi:10.1016/S0002-9440(10)65142-5
    • Kim YJ, Borsig L, Han HL, Varki NM, Varki A. Distinct selectin ligands on colon carcinoma mucins can mediate pathological interactions among platelets, leukocytes, and endothelium. Am J Pathol (1999) 155:461-72. doi:10.1016/S0002-9440(10)65142-5
    • (1999) Am J Pathol , vol.155 , pp. 461-472
    • Kim, Y.J.1    Borsig, L.2    Han, H.L.3    Varki, N.M.4    Varki, A.5
  • 159
    • 0034283997 scopus 로고    scopus 로고
    • Immobilized platelets support human colon carcinoma cell tethering, rolling, and firm adhesion under dynamic flow conditions
    • McCarty OJ, Mousa SA, Bray PF, Konstantopoulos K. Immobilized platelets support human colon carcinoma cell tethering, rolling, and firm adhesion under dynamic flow conditions. Blood (2000) 96:1789-97.
    • (2000) Blood , vol.96 , pp. 1789-1797
    • McCarty, O.J.1    Mousa, S.A.2    Bray, P.F.3    Konstantopoulos, K.4
  • 160
    • 0028907310 scopus 로고
    • Up-regulation of the oligosaccharide sialyl LewisX: a new prognostic parameter in metastatic prostate cancer
    • Jorgensen T, Berner A, Kaalhus O, Tveter KJ, Danielsen HE, Bryne M. Up-regulation of the oligosaccharide sialyl LewisX: a new prognostic parameter in metastatic prostate cancer. Cancer Res (1995) 55:1817-9.
    • (1995) Cancer Res , vol.55 , pp. 1817-1819
    • Jorgensen, T.1    Berner, A.2    Kaalhus, O.3    Tveter, K.J.4    Danielsen, H.E.5    Bryne, M.6
  • 161
    • 0030049707 scopus 로고    scopus 로고
    • Expression of alpha-1,3-fucosyltransferase type IV and VII genes is related to poor prognosis in lung cancer
    • Ogawa J, Inoue H, Koide S. Expression of alpha-1,3-fucosyltransferase type IV and VII genes is related to poor prognosis in lung cancer. Cancer Res (1996) 56:325-9.
    • (1996) Cancer Res , vol.56 , pp. 325-329
    • Ogawa, J.1    Inoue, H.2    Koide, S.3
  • 162
    • 0030761635 scopus 로고    scopus 로고
    • Endothelial and epithelial expression of sialyl Lewis(x) and sialyl Lewis(a) in lesions of breast carcinoma
    • doi:10.1002/(SICI)1097-0215(19970620)74:3<296::AID-IJC11>3.0.CO;2-A
    • Renkonen J, Paavonen T, Renkonen R. Endothelial and epithelial expression of sialyl Lewis(x) and sialyl Lewis(a) in lesions of breast carcinoma. Int J Cancer (1997) 74:296-300. doi:10.1002/(SICI)1097-0215(19970620)74:3<296::AID-IJC11>3.0.CO;2-A
    • (1997) Int J Cancer , vol.74 , pp. 296-300
    • Renkonen, J.1    Paavonen, T.2    Renkonen, R.3
  • 163
    • 18344376702 scopus 로고    scopus 로고
    • Overexpression of sialyl Lewis x antigen is associated with formation of extratumoral venous invasion and predicts postoperative development of massive hepatic metastasis in cases with pancreatic ductal adenocarcinoma
    • doi:10.1159/000048767
    • Takahashi S, Oda T, Hasebe T, Sasaki S, Kinoshita T, Konishi M, et al. Overexpression of sialyl Lewis x antigen is associated with formation of extratumoral venous invasion and predicts postoperative development of massive hepatic metastasis in cases with pancreatic ductal adenocarcinoma. Pathobiology (2001) 69:127-35. doi:10.1159/000048767
    • (2001) Pathobiology , vol.69 , pp. 127-135
    • Takahashi, S.1    Oda, T.2    Hasebe, T.3    Sasaki, S.4    Kinoshita, T.5    Konishi, M.6
  • 164
    • 0032418052 scopus 로고    scopus 로고
    • Immunohistochemical expression of the sialyl Lewis x antigen on gastric cancer cells correlates with the presence of liver metastasis
    • doi:10.1023/A:1006584829246
    • Tatsumi M, Watanabe A, Sawada H, Yamada Y, Shino Y, Nakano H. Immunohistochemical expression of the sialyl Lewis x antigen on gastric cancer cells correlates with the presence of liver metastasis. Clin Exp Metastasis (1998) 16:743-50. doi:10.1023/A:1006584829246
    • (1998) Clin Exp Metastasis , vol.16 , pp. 743-750
    • Tatsumi, M.1    Watanabe, A.2    Sawada, H.3    Yamada, Y.4    Shino, Y.5    Nakano, H.6
  • 165
    • 16244380471 scopus 로고    scopus 로고
    • Positive correlation between sialyl Lewis X expression and pathologic findings in renal cell carcinoma
    • doi:10.1111/j.1523-1755.2005.00216.x
    • Tozawa K, Okamoto T, Kawai N, Hashimoto Y, Hayashi Y, Kohri K. Positive correlation between sialyl Lewis X expression and pathologic findings in renal cell carcinoma. Kidney Int (2005) 67:1391-6. doi:10.1111/j.1523-1755.2005.00216.x
    • (2005) Kidney Int , vol.67 , pp. 1391-1396
    • Tozawa, K.1    Okamoto, T.2    Kawai, N.3    Hashimoto, Y.4    Hayashi, Y.5    Kohri, K.6
  • 166
    • 0242425929 scopus 로고    scopus 로고
    • Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells
    • doi:10.1002/ijc.11513
    • Inaba Y, Ohyama C, Kato T, Satoh M, Saito H, Hagisawa S, et al. Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells. Int J Cancer (2003) 107:949-57. doi:10.1002/ijc.11513
    • (2003) Int J Cancer , vol.107 , pp. 949-957
    • Inaba, Y.1    Ohyama, C.2    Kato, T.3    Satoh, M.4    Saito, H.5    Hagisawa, S.6
  • 167
    • 0029153610 scopus 로고
    • Differential colon cancer cell adhesion to E-, P-, and L-selectin: role of mucin-type glycoproteins
    • Mannori G, Crottet P, Cecconi O, Hanasaki K, Aruffo A, Nelson RM, et al. Differential colon cancer cell adhesion to E-, P-, and L-selectin: role of mucin-type glycoproteins. Cancer Res (1995) 55:4425-31.
    • (1995) Cancer Res , vol.55 , pp. 4425-4431
    • Mannori, G.1    Crottet, P.2    Cecconi, O.3    Hanasaki, K.4    Aruffo, A.5    Nelson, R.M.6
  • 168
    • 10444272413 scopus 로고    scopus 로고
    • Expression of the high-affinity selectin glycan ligand C2-O-sLeX by colon carcinoma cells
    • doi:10.1016/j.canlet.2004.06.038
    • St Hill CA, Bullard KM, Walcheck B. Expression of the high-affinity selectin glycan ligand C2-O-sLeX by colon carcinoma cells. Cancer Lett (2005) 217:105-13. doi:10.1016/j.canlet.2004.06.038
    • (2005) Cancer Lett , vol.217 , pp. 105-113
    • St Hill, C.A.1    Bullard, K.M.2    Walcheck, B.3
  • 169
    • 73349141180 scopus 로고    scopus 로고
    • Alpha 1,3 fucosyltransferases are master regulators of prostate cancer cell trafficking
    • doi:10.1073/pnas.0906074106
    • Barthel SR, Wiese GK, Cho J, Opperman MJ, Hays DL, Siddiqui J, et al. Alpha 1,3 fucosyltransferases are master regulators of prostate cancer cell trafficking. Proc Natl Acad Sci U S A (2009) 106:19491-6. doi:10.1073/pnas.0906074106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19491-19496
    • Barthel, S.R.1    Wiese, G.K.2    Cho, J.3    Opperman, M.J.4    Hays, D.L.5    Siddiqui, J.6
  • 170
    • 0028963272 scopus 로고
    • Characterization of human colon carcinoma variant cells selected for sialyl Lex carbohydrate antigen: liver colonization and adhesion to vascular endothelial cells
    • doi:10.1006/excr.1995.1027
    • Izumi Y, Taniuchi Y, Tsuji T, Smith CW, Nakamori S, Fidler IJ, et al. Characterization of human colon carcinoma variant cells selected for sialyl Lex carbohydrate antigen: liver colonization and adhesion to vascular endothelial cells. Exp Cell Res (1995) 216:215-21. doi:10.1006/excr.1995.1027
    • (1995) Exp Cell Res , vol.216 , pp. 215-221
    • Izumi, Y.1    Taniuchi, Y.2    Tsuji, T.3    Smith, C.W.4    Nakamori, S.5    Fidler, I.J.6
  • 171
    • 0033135594 scopus 로고    scopus 로고
    • Expression of human alpha(1,3)fucosyltransferase antisense sequences inhibits selectin-mediated adhesion and liver metastasis of colon carcinoma cells
    • Weston BW, Hiller KM, Mayben JP, Manousos GA, Bendt KM, Liu R, et al. Expression of human alpha(1,3)fucosyltransferase antisense sequences inhibits selectin-mediated adhesion and liver metastasis of colon carcinoma cells. Cancer Res (1999) 59:2127-35.
    • (1999) Cancer Res , vol.59 , pp. 2127-2135
    • Weston, B.W.1    Hiller, K.M.2    Mayben, J.P.3    Manousos, G.A.4    Bendt, K.M.5    Liu, R.6
  • 172
    • 0028048830 scopus 로고
    • The selectins and their ligands
    • doi:10.1016/0955-0674(94)90092-2
    • Rosen SD, Bertozzi CR. The selectins and their ligands. Curr Opin Cell Biol (1994) 6:663-73. doi:10.1016/0955-0674(94)90092-2
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 663-673
    • Rosen, S.D.1    Bertozzi, C.R.2
  • 173
    • 0029809614 scopus 로고    scopus 로고
    • Mucin glycoproteins in neoplasia
    • doi:10.1007/BF00702333
    • Kim YS, Gum J Jr, Brockhausen I. Mucin glycoproteins in neoplasia. Glycoconj J (1996) 13:693-707. doi:10.1007/BF00702333
    • (1996) Glycoconj J , vol.13 , pp. 693-707
    • Kim, Y.S.1    Gum Jr, J.2    Brockhausen, I.3
  • 174
    • 67649743525 scopus 로고    scopus 로고
    • Glycosylation in immune cell trafficking
    • doi:10.1111/j.1600-065X.2009.00795.x
    • Sperandio M, Gleissner CA, Ley K. Glycosylation in immune cell trafficking. Immunol Rev (2009) 230:97-113. doi:10.1111/j.1600-065X.2009.00795.x
    • (2009) Immunol Rev , vol.230 , pp. 97-113
    • Sperandio, M.1    Gleissner, C.A.2    Ley, K.3
  • 175
    • 0031029280 scopus 로고    scopus 로고
    • Selectin ligands: will the real ones please stand up?
    • doi:10.1172/JCI119142
    • Varki A. Selectin ligands: will the real ones please stand up? J Clin Invest (1997) 99:158-62. doi:10.1172/JCI119142
    • (1997) J Clin Invest , vol.99 , pp. 158-162
    • Varki, A.1
  • 176
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: lectins that initiate cell adhesion under flow
    • doi:10.1016/S0955-0674(02)00367-8
    • McEver RP. Selectins: lectins that initiate cell adhesion under flow. Curr Opin Cell Biol (2002) 14:581-6. doi:10.1016/S0955-0674(02)00367-8
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 581-586
    • McEver, R.P.1
  • 177
    • 42049099903 scopus 로고    scopus 로고
    • Structure, evolution, and biology of the MUC4 mucin
    • doi:10.1096/fj.07-9673rev
    • Chaturvedi P, Singh AP, Batra SK. Structure, evolution, and biology of the MUC4 mucin. FASEB J (2008) 22:966-81. doi:10.1096/fj.07-9673rev
    • (2008) FASEB J , vol.22 , pp. 966-981
    • Chaturvedi, P.1    Singh, A.P.2    Batra, S.K.3
  • 178
    • 84863272678 scopus 로고    scopus 로고
    • Mucin 16 is a functional selectin ligand on pancreatic cancer cells
    • doi:10.1096/fj.11-195669
    • Chen SH, Dallas MR, Balzer EM, Konstantopoulos K. Mucin 16 is a functional selectin ligand on pancreatic cancer cells. FASEB J (2012) 26:1349-59. doi:10.1096/fj.11-195669
    • (2012) FASEB J , vol.26 , pp. 1349-1359
    • Chen, S.H.1    Dallas, M.R.2    Balzer, E.M.3    Konstantopoulos, K.4
  • 179
    • 17944401076 scopus 로고    scopus 로고
    • CD24, a mucin-type glycoprotein, is a ligand for P-selectin on human tumor cells
    • Aigner S, Sthoeger ZM, Fogel M, Weber E, Zarn J, Ruppert M, et al. CD24, a mucin-type glycoprotein, is a ligand for P-selectin on human tumor cells. Blood (1997) 89:3385-95.
    • (1997) Blood , vol.89 , pp. 3385-3395
    • Aigner, S.1    Sthoeger, Z.M.2    Fogel, M.3    Weber, E.4    Zarn, J.5    Ruppert, M.6
  • 180
    • 33744920615 scopus 로고    scopus 로고
    • HCELL is the major E- and L-selectin ligand expressed on LS174T colon carcinoma cells
    • doi:10.1074/jbc.M513617200
    • Burdick MM, Chu JT, Godar S, Sackstein R. HCELL is the major E- and L-selectin ligand expressed on LS174T colon carcinoma cells. J Biol Chem (2006) 281:13899-905. doi:10.1074/jbc.M513617200
    • (2006) J Biol Chem , vol.281 , pp. 13899-13905
    • Burdick, M.M.1    Chu, J.T.2    Godar, S.3    Sackstein, R.4
  • 181
    • 21344454667 scopus 로고    scopus 로고
    • Identification of leukocyte E-selectin ligands, P-selectin glycoprotein ligand-1 and E-selectin ligand-1, on human metastatic prostate tumor cells
    • doi:10.1158/0008-5472.CAN-04-4653
    • Dimitroff CJ, Descheny L, Trujillo N, Kim R, Nguyen V, Huang W, et al. Identification of leukocyte E-selectin ligands, P-selectin glycoprotein ligand-1 and E-selectin ligand-1, on human metastatic prostate tumor cells. Cancer Res (2005) 65:5750-60. doi:10.1158/0008-5472.CAN-04-4653
    • (2005) Cancer Res , vol.65 , pp. 5750-5760
    • Dimitroff, C.J.1    Descheny, L.2    Trujillo, N.3    Kim, R.4    Nguyen, V.5    Huang, W.6
  • 182
    • 33749499326 scopus 로고    scopus 로고
    • Death receptor-3, a new E-Selectin counter-receptor that confers migration and survival advantages to colon carcinoma cells by triggering p38 and ERK MAPK activation
    • doi:10.1158/0008-5472.CAN-05-4605
    • Gout S, Morin C, Houle F, Huot J. Death receptor-3, a new E-Selectin counter-receptor that confers migration and survival advantages to colon carcinoma cells by triggering p38 and ERK MAPK activation. Cancer Res (2006) 66:9117-24. doi:10.1158/0008-5472.CAN-05-4605
    • (2006) Cancer Res , vol.66 , pp. 9117-9124
    • Gout, S.1    Morin, C.2    Houle, F.3    Huot, J.4
  • 183
    • 65249108221 scopus 로고    scopus 로고
    • Podocalyxin-like protein is an E-/L-selectin ligand on colon carcinoma cells: comparative biochemical properties of selectin ligands in host and tumor cells.
    • doi:10.1152/ajpcell.00472.2008
    • Thomas SN, Schnaar RL, Konstantopoulos K. Podocalyxin-like protein is an E-/L-selectin ligand on colon carcinoma cells: comparative biochemical properties of selectin ligands in host and tumor cells. Am J Physiol Cell Physiol (2009) 296:C505-13. doi:10.1152/ajpcell.00472.2008
    • (2009) Am J Physiol Cell Physiol , vol.296
    • Thomas, S.N.1    Schnaar, R.L.2    Konstantopoulos, K.3
  • 184
    • 0027390740 scopus 로고
    • A human homologue of the rat metastasis-associated variant of CD44 is expressed in colorectal carcinomas and adenomatous polyps
    • doi:10.1083/jcb.120.1.227
    • Heider KH, Hofmann M, Hors E, van den Berg F, Ponta H, Herrlich P, et al. A human homologue of the rat metastasis-associated variant of CD44 is expressed in colorectal carcinomas and adenomatous polyps. J Cell Biol (1993) 120:227-33. doi:10.1083/jcb.120.1.227
    • (1993) J Cell Biol , vol.120 , pp. 227-233
    • Heider, K.H.1    Hofmann, M.2    Hors, E.3    van den Berg, F.4    Ponta, H.5    Herrlich, P.6
  • 186
    • 0028948666 scopus 로고
    • CD44 isoform expression in primary and metastatic pancreatic adenocarcinoma
    • Rall CJ, Rustgi AK. CD44 isoform expression in primary and metastatic pancreatic adenocarcinoma. Cancer Res (1995) 55:1831-5.
    • (1995) Cancer Res , vol.55 , pp. 1831-1835
    • Rall, C.J.1    Rustgi, A.K.2
  • 187
    • 0035199380 scopus 로고    scopus 로고
    • Introduction of antisense CD44S CDNA down-regulates expression of overall CD44 isoforms and inhibits tumor growth and metastasis in highly metastatic colon carcinoma cells
    • doi:10.1002/1097-0215(20010101)91:1<67::AID-IJC1011>3.0.CO;2-D
    • Harada N, Mizoi T, Kinouchi M, Hoshi K, Ishii S, Shiiba K, et al. Introduction of antisense CD44S CDNA down-regulates expression of overall CD44 isoforms and inhibits tumor growth and metastasis in highly metastatic colon carcinoma cells. Int J Cancer (2001) 91:67-75. doi:10.1002/1097-0215(20010101)91:1<67::AID-IJC1011>3.0.CO;2-D
    • (2001) Int J Cancer , vol.91 , pp. 67-75
    • Harada, N.1    Mizoi, T.2    Kinouchi, M.3    Hoshi, K.4    Ishii, S.5    Shiiba, K.6
  • 188
    • 0032529443 scopus 로고    scopus 로고
    • Expression of antisense CD44 variant 6 inhibits colorectal tumor metastasis and tumor growth in a wound environment
    • Reeder JA, Gotley DC, Walsh MD, Fawcett J, Antalis TM. Expression of antisense CD44 variant 6 inhibits colorectal tumor metastasis and tumor growth in a wound environment. Cancer Res (1998) 58:3719-26.
    • (1998) Cancer Res , vol.58 , pp. 3719-3726
    • Reeder, J.A.1    Gotley, D.C.2    Walsh, M.D.3    Fawcett, J.4    Antalis, T.M.5
  • 189
    • 21344446792 scopus 로고    scopus 로고
    • CD44 on LS174T colon carcinoma cells possesses E-selectin ligand activity
    • doi:10.1158/0008-5472.CAN-04-4557
    • Hanley WD, Burdick MM, Konstantopoulos K, Sackstein R. CD44 on LS174T colon carcinoma cells possesses E-selectin ligand activity. Cancer Res (2005) 65:5812-7. doi:10.1158/0008-5472.CAN-04-4557
    • (2005) Cancer Res , vol.65 , pp. 5812-5817
    • Hanley, W.D.1    Burdick, M.M.2    Konstantopoulos, K.3    Sackstein, R.4
  • 191
    • 84860390514 scopus 로고    scopus 로고
    • Chondroitin sulfates play a major role in breast cancer metastasis: a role for CSPG4 and CHST11 gene expression in forming surface P-selectin ligands in aggressive breast cancer cells.
    • doi:10.1186/bcr2895
    • Cooney CA, Jousheghany F, Yao-Borengasser A, Phanavanh B, Gomes T, Kieber-Emmons AM, et al. Chondroitin sulfates play a major role in breast cancer metastasis: a role for CSPG4 and CHST11 gene expression in forming surface P-selectin ligands in aggressive breast cancer cells. Breast Cancer Res (2011) 13:R58. doi:10.1186/bcr2895
    • (2011) Breast Cancer Res , vol.13
    • Cooney, C.A.1    Jousheghany, F.2    Yao-Borengasser, A.3    Phanavanh, B.4    Gomes, T.5    Kieber-Emmons, A.M.6
  • 192
    • 0032555123 scopus 로고    scopus 로고
    • P-selectin mediates adhesion of the human melanoma cell line NKI-4: identification of glycoprotein ligands
    • doi:10.1021/bi9730846
    • Kaytes PS, Geng JG. P-selectin mediates adhesion of the human melanoma cell line NKI-4: identification of glycoprotein ligands. Biochemistry (1998) 37:10514-21. doi:10.1021/bi9730846
    • (1998) Biochemistry , vol.37 , pp. 10514-10521
    • Kaytes, P.S.1    Geng, J.G.2
  • 193
    • 0027249917 scopus 로고
    • P-selectin mediates adhesion of platelets to neuroblastoma and small cell lung cancer
    • doi:10.1172/JCI116654
    • Stone JP, Wagner DD. P-selectin mediates adhesion of platelets to neuroblastoma and small cell lung cancer. J Clin Invest (1993) 92:804-13. doi:10.1172/JCI116654
    • (1993) J Clin Invest , vol.92 , pp. 804-813
    • Stone, J.P.1    Wagner, D.D.2
  • 194
    • 84890434135 scopus 로고    scopus 로고
    • Human fucosyltransferase 6 enables prostate cancer metastasis to bone
    • doi:10.1038/bjc.2013.690
    • Li J, Guillebon AD, Hsu JW, Barthel SR, Dimitroff CJ, Lee YF, et al. Human fucosyltransferase 6 enables prostate cancer metastasis to bone. Br J Cancer (2013) 109:3014-22. doi:10.1038/bjc.2013.690
    • (2013) Br J Cancer , vol.109 , pp. 3014-3022
    • Li, J.1    Guillebon, A.D.2    Hsu, J.W.3    Barthel, S.R.4    Dimitroff, C.J.5    Lee, Y.F.6
  • 195
    • 84255199499 scopus 로고    scopus 로고
    • Selectin ligand Sialyl-Lewis x antigen drives metastasis of hormone-dependent breast cancers
    • doi:10.1158/0008-5472.CAN-11-1139
    • Julien S, Ivetic A, Grigoriadis A, Qize D, Burford B, Sproviero D, et al. Selectin ligand Sialyl-Lewis x antigen drives metastasis of hormone-dependent breast cancers. Cancer Res (2011) 71:7683-93. doi:10.1158/0008-5472.CAN-11-1139
    • (2011) Cancer Res , vol.71 , pp. 7683-7693
    • Julien, S.1    Ivetic, A.2    Grigoriadis, A.3    Qize, D.4    Burford, B.5    Sproviero, D.6
  • 196
    • 80955179558 scopus 로고    scopus 로고
    • TNFalpha enhances the motility and invasiveness of prostatic cancer cells by stimulating the expression of selective glycosyl- and sulfotransferase genes involved in the synthesis of selectin ligands
    • doi:10.1016/j.bbrc.2011.05.019
    • Radhakrishnan P, Chachadi V, Lin MF, Singh R, Kannagi R, Cheng PW. TNFalpha enhances the motility and invasiveness of prostatic cancer cells by stimulating the expression of selective glycosyl- and sulfotransferase genes involved in the synthesis of selectin ligands. Biochem Biophys Res Commun (2011) 409:436-41. doi:10.1016/j.bbrc.2011.05.019
    • (2011) Biochem Biophys Res Commun , vol.409 , pp. 436-441
    • Radhakrishnan, P.1    Chachadi, V.2    Lin, M.F.3    Singh, R.4    Kannagi, R.5    Cheng, P.W.6
  • 197
    • 84872582388 scopus 로고    scopus 로고
    • Definition of molecular determinants of prostate cancer cell bone extravasation
    • doi:10.1158/0008-5472.CAN-12-3264
    • Barthel SR, Hays DL, Yazawa EM, Opperman M, Walley KC, Nimrichter L, et al. Definition of molecular determinants of prostate cancer cell bone extravasation. Cancer Res (2013) 73:942-52. doi:10.1158/0008-5472.CAN-12-3264
    • (2013) Cancer Res , vol.73 , pp. 942-952
    • Barthel, S.R.1    Hays, D.L.2    Yazawa, E.M.3    Opperman, M.4    Walley, K.C.5    Nimrichter, L.6
  • 198
    • 77958092075 scopus 로고    scopus 로고
    • Knockdown of fucosyltransferase III disrupts the adhesion of circulating cancer cells to E-selectin without affecting hematopoietic cell adhesion
    • doi:10.1016/j.carres.2010.07.028
    • Yin X, Rana K, Ponmudi V, King MR. Knockdown of fucosyltransferase III disrupts the adhesion of circulating cancer cells to E-selectin without affecting hematopoietic cell adhesion. Carbohydr Res (2010) 345:2334-42. doi:10.1016/j.carres.2010.07.028
    • (2010) Carbohydr Res , vol.345 , pp. 2334-2342
    • Yin, X.1    Rana, K.2    Ponmudi, V.3    King, M.R.4
  • 199
    • 54549107723 scopus 로고    scopus 로고
    • The role of platelet activation in tumor metastasis
    • doi:10.1586/14737140.8.8.1247
    • Borsig L. The role of platelet activation in tumor metastasis. Expert Rev Anticancer Ther (2008) 8:1247-55. doi:10.1586/14737140.8.8.1247
    • (2008) Expert Rev Anticancer Ther , vol.8 , pp. 1247-1255
    • Borsig, L.1
  • 200
    • 79251478398 scopus 로고    scopus 로고
    • Contribution of platelets to tumour metastasis
    • Gay LJ, Felding-Habermann B. Contribution of platelets to tumour metastasis. Nat Rev Cancer (2011) 11:123-34.
    • (2011) Nat Rev Cancer , vol.11 , pp. 123-134
    • Gay, L.J.1    Felding-Habermann, B.2
  • 201
    • 0026494476 scopus 로고
    • Platelets and cancer metastasis: a causal relationship?
    • doi:10.1007/BF01307186
    • Honn KV, Tang DG, Crissman JD. Platelets and cancer metastasis: a causal relationship? Cancer Metastasis Rev (1992) 11:325-51. doi:10.1007/BF01307186
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 325-351
    • Honn, K.V.1    Tang, D.G.2    Crissman, J.D.3
  • 202
    • 0019820999 scopus 로고
    • Role of platelets in tumor cell metastases
    • doi:10.7326/0003-4819-95-5-636
    • Karpatkin S, Pearlstein E. Role of platelets in tumor cell metastases. Ann Intern Med (1981) 95:636-41. doi:10.7326/0003-4819-95-5-636
    • (1981) Ann Intern Med , vol.95 , pp. 636-641
    • Karpatkin, S.1    Pearlstein, E.2
  • 203
    • 0035853111 scopus 로고    scopus 로고
    • Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis
    • doi:10.1073/pnas.061615598
    • Borsig L, Wong R, Feramisco J, Nadeau DR, Varki NM, Varki A. Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis. Proc Natl Acad Sci U S A (2001) 98:3352-7. doi:10.1073/pnas.061615598
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3352-3357
    • Borsig, L.1    Wong, R.2    Feramisco, J.3    Nadeau, D.R.4    Varki, N.M.5    Varki, A.6
  • 204
    • 3142592165 scopus 로고    scopus 로고
    • Platelets, protease-activated receptors, and fibrinogen in hematogenous metastasis
    • doi:10.1182/blood-2004-02-0434
    • Camerer E, Qazi AA, Duong DN, Cornelissen I, Advincula R, Coughlin SR. Platelets, protease-activated receptors, and fibrinogen in hematogenous metastasis. Blood (2004) 104:397-401. doi:10.1182/blood-2004-02-0434
    • (2004) Blood , vol.104 , pp. 397-401
    • Camerer, E.1    Qazi, A.A.2    Duong, D.N.3    Cornelissen, I.4    Advincula, R.5    Coughlin, S.R.6
  • 205
    • 0033559946 scopus 로고    scopus 로고
    • Lysis of tumor cells by natural killer cells in mice is impeded by platelets
    • Nieswandt B, Hafner M, Echtenacher B, Mannel DN. Lysis of tumor cells by natural killer cells in mice is impeded by platelets. Cancer Res (1999) 59:1295-300.
    • (1999) Cancer Res , vol.59 , pp. 1295-1300
    • Nieswandt, B.1    Hafner, M.2    Echtenacher, B.3    Mannel, D.N.4
  • 206
    • 11144230059 scopus 로고    scopus 로고
    • Platelets and fibrin(ogen) increase metastatic potential by impeding natural killer cell-mediated elimination of tumor cells
    • doi:10.1182/blood-2004-06-2272
    • Palumbo JS, Talmage KE, Massari JV, La Jeunesse CM, Flick MJ, Kombrinck KW, et al. Platelets and fibrin(ogen) increase metastatic potential by impeding natural killer cell-mediated elimination of tumor cells. Blood (2005) 105:178-85. doi:10.1182/blood-2004-06-2272
    • (2005) Blood , vol.105 , pp. 178-185
    • Palumbo, J.S.1    Talmage, K.E.2    Massari, J.V.3    La Jeunesse, C.M.4    Flick, M.J.5    Kombrinck, K.W.6
  • 207
    • 16544390675 scopus 로고    scopus 로고
    • Endothelial P-selectin as a target of heparin action in experimental melanoma lung metastasis
    • doi:10.1158/0008-5472.CAN-03-1054
    • Ludwig RJ, Boehme B, Podda M, Henschler R, Jager E, Tandi C, et al. Endothelial P-selectin as a target of heparin action in experimental melanoma lung metastasis. Cancer Res (2004) 64:2743-50. doi:10.1158/0008-5472.CAN-03-1054
    • (2004) Cancer Res , vol.64 , pp. 2743-2750
    • Ludwig, R.J.1    Boehme, B.2    Podda, M.3    Henschler, R.4    Jager, E.5    Tandi, C.6
  • 208
    • 84866385928 scopus 로고    scopus 로고
    • Platelets and P-selectin control tumor cell metastasis in an organ-specific manner and independently of NK cells
    • doi:10.1158/0008-5472.CAN-11-4010
    • Coupland LA, Chong BH, Parish CR. Platelets and P-selectin control tumor cell metastasis in an organ-specific manner and independently of NK cells. Cancer Res (2012) 72:4662-71. doi:10.1158/0008-5472.CAN-11-4010
    • (2012) Cancer Res , vol.72 , pp. 4662-4671
    • Coupland, L.A.1    Chong, B.H.2    Parish, C.R.3
  • 209
    • 81255205399 scopus 로고    scopus 로고
    • Direct signaling between platelets and cancer cells induces an epithelial-mesenchymal-like transition and promotes metastasis
    • doi:10.1016/j.ccr.2011.09.009
    • Labelle M, Begum S, Hynes RO. Direct signaling between platelets and cancer cells induces an epithelial-mesenchymal-like transition and promotes metastasis. Cancer Cell (2011) 20:576-90. doi:10.1016/j.ccr.2011.09.009
    • (2011) Cancer Cell , vol.20 , pp. 576-590
    • Labelle, M.1    Begum, S.2    Hynes, R.O.3
  • 210
    • 0035889894 scopus 로고    scopus 로고
    • Hydrodynamic shear regulates the kinetics and receptor specificity of polymorphonuclear leukocyte-colon carcinoma cell adhesive interactions
    • Jadhav S, Bochner BS, Konstantopoulos K. Hydrodynamic shear regulates the kinetics and receptor specificity of polymorphonuclear leukocyte-colon carcinoma cell adhesive interactions. J Immunol (2001) 167:5986-93.
    • (2001) J Immunol , vol.167 , pp. 5986-5993
    • Jadhav, S.1    Bochner, B.S.2    Konstantopoulos, K.3
  • 211
    • 63049104211 scopus 로고    scopus 로고
    • Microenvironmental regulation of metastasis
    • doi:10.1038/nrc2618
    • Joyce JA, Pollard JW. Microenvironmental regulation of metastasis. Nat Rev Cancer (2009) 9:239-52. doi:10.1038/nrc2618
    • (2009) Nat Rev Cancer , vol.9 , pp. 239-252
    • Joyce, J.A.1    Pollard, J.W.2
  • 212
    • 47949096781 scopus 로고    scopus 로고
    • Cancer-related inflammation
    • doi:10.1038/nature07205
    • Mantovani A, Allavena P, Sica A, Balkwill F. Cancer-related inflammation. Nature (2008) 454:436-44. doi:10.1038/nature07205
    • (2008) Nature , vol.454 , pp. 436-444
    • Mantovani, A.1    Allavena, P.2    Sica, A.3    Balkwill, F.4
  • 213
    • 73349128755 scopus 로고    scopus 로고
    • Selectin-mediated activation of endothelial cells induces expression of CCL5 and promotes metastasis through recruitment of monocytes
    • doi:10.1182/blood-2008-10-186585
    • Läubli H, Spanaus KS, Borsig L. Selectin-mediated activation of endothelial cells induces expression of CCL5 and promotes metastasis through recruitment of monocytes. Blood (2009) 114:4583-91. doi:10.1182/blood-2008-10-186585
    • (2009) Blood , vol.114 , pp. 4583-4591
    • Läubli, H.1    Spanaus, K.S.2    Borsig, L.3
  • 214
    • 1642433233 scopus 로고    scopus 로고
    • Increased primary tumor growth in mice null for beta3- or beta3/beta5-integrins or selectins
    • doi:10.1073/pnas.0307289101
    • Taverna D, Moher H, Crowley D, Borsig L, Varki A, Hynes RO. Increased primary tumor growth in mice null for beta3- or beta3/beta5-integrins or selectins. Proc Natl Acad Sci U S A (2004) 101:763-8. doi:10.1073/pnas.0307289101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 763-768
    • Taverna, D.1    Moher, H.2    Crowley, D.3    Borsig, L.4    Varki, A.5    Hynes, R.O.6
  • 215
    • 0035823598 scopus 로고    scopus 로고
    • Transendothelial migration of colon carcinoma cells requires expression of E-selectin by endothelial cells and activation of stress-activated protein kinase-2 (SAPK2/p38) in the tumor cells
    • doi:10.1074/jbc.M008564200
    • Laferriere J, Houle F, Taher MM, Valerie K, Huot J. Transendothelial migration of colon carcinoma cells requires expression of E-selectin by endothelial cells and activation of stress-activated protein kinase-2 (SAPK2/p38) in the tumor cells. J Biol Chem (2001) 276:33762-72. doi:10.1074/jbc.M008564200
    • (2001) J Biol Chem , vol.276 , pp. 33762-33772
    • Laferriere, J.1    Houle, F.2    Taher, M.M.3    Valerie, K.4    Huot, J.5
  • 216
    • 33749485053 scopus 로고    scopus 로고
    • Regulation of transendothelial migration of colon cancer cells by E-selectin-mediated activation of p38 and ERK MAP kinases
    • doi:10.1038/sj.onc.1209664
    • Tremblay PL, Auger FA, Huot J. Regulation of transendothelial migration of colon cancer cells by E-selectin-mediated activation of p38 and ERK MAP kinases. Oncogene (2006) 25:6563-73. doi:10.1038/sj.onc.1209664
    • (2006) Oncogene , vol.25 , pp. 6563-6573
    • Tremblay, P.L.1    Auger, F.A.2    Huot, J.3
  • 217
    • 0030029220 scopus 로고    scopus 로고
    • Redirection of tumor metastasis by expression of E-selectin in vivo
    • doi:10.1084/jem.183.2.581
    • Biancone L, Araki M, Araki K, Vassalli P, Stamenkovic I. Redirection of tumor metastasis by expression of E-selectin in vivo. J Exp Med (1996) 183:581-7. doi:10.1084/jem.183.2.581
    • (1996) J Exp Med , vol.183 , pp. 581-587
    • Biancone, L.1    Araki, M.2    Araki, K.3    Vassalli, P.4    Stamenkovic, I.5
  • 218
    • 0031011610 scopus 로고    scopus 로고
    • Liver endothelial E-selectin mediates carcinoma cell adhesion and promotes liver metastasis
    • doi:10.1002/(SICI)1097-0215(19970516)71:4<612::AID-IJC17>3.3.CO;2-1
    • Brodt P, Fallavollita L, Bresalier RS, Meterissian S, Norton CR, Wolitzky BA. Liver endothelial E-selectin mediates carcinoma cell adhesion and promotes liver metastasis. Int J Cancer (1997) 71:612-9. doi:10.1002/(SICI)1097-0215(19970516)71:4<612::AID-IJC17>3.3.CO;2-1
    • (1997) Int J Cancer , vol.71 , pp. 612-619
    • Brodt, P.1    Fallavollita, L.2    Bresalier, R.S.3    Meterissian, S.4    Norton, C.R.5    Wolitzky, B.A.6
  • 219
    • 78649657094 scopus 로고    scopus 로고
    • Selectins as mediators of lung metastasis
    • doi:10.1007/s12307-010-0043-6
    • Läubli H, Borsig L. Selectins as mediators of lung metastasis. Cancer Microenviron (2010) 3:97-105. doi:10.1007/s12307-010-0043-6
    • (2010) Cancer Microenviron , vol.3 , pp. 97-105
    • Läubli, H.1    Borsig, L.2
  • 220
    • 84860349839 scopus 로고    scopus 로고
    • Selectin-deficiency reduces the number of spontaneous metastases in a xenograft model of human breast cancer
    • doi:10.1016/j.canlet.2012.02.019
    • Stubke K, Wicklein D, Herich L, Schumacher U, Nehmann N. Selectin-deficiency reduces the number of spontaneous metastases in a xenograft model of human breast cancer. Cancer Lett (2012) 321:89-99. doi:10.1016/j.canlet.2012.02.019
    • (2012) Cancer Lett , vol.321 , pp. 89-99
    • Stubke, K.1    Wicklein, D.2    Herich, L.3    Schumacher, U.4    Nehmann, N.5
  • 221
    • 79952756887 scopus 로고    scopus 로고
    • Endothelial focal adhesion kinase mediates cancer cell homing to discrete regions of the lungs via E-selectin up-regulation
    • doi:10.1073/pnas.1100446108
    • Hiratsuka S, Goel S, Kamoun WS, Maru Y, Fukumura D, Duda DG, et al. Endothelial focal adhesion kinase mediates cancer cell homing to discrete regions of the lungs via E-selectin up-regulation. Proc Natl Acad Sci U S A (2011) 108:3725-30. doi:10.1073/pnas.1100446108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3725-3730
    • Hiratsuka, S.1    Goel, S.2    Kamoun, W.S.3    Maru, Y.4    Fukumura, D.5    Duda, D.G.6
  • 222
    • 0142155574 scopus 로고    scopus 로고
    • Selectin-mucin interactions as a probable molecular explanation for the association of Trousseau syndrome with mucinous adenocarcinomas
    • doi:10.1172/JCI200318882
    • Wahrenbrock M, Borsig L, Le D, Varki N, Varki A. Selectin-mucin interactions as a probable molecular explanation for the association of Trousseau syndrome with mucinous adenocarcinomas. J Clin Invest (2003) 112:853-62. doi:10.1172/JCI200318882
    • (2003) J Clin Invest , vol.112 , pp. 853-862
    • Wahrenbrock, M.1    Borsig, L.2    Le, D.3    Varki, N.4    Varki, A.5
  • 223
    • 80054108831 scopus 로고    scopus 로고
    • Carcinoma mucins trigger reciprocal activation of platelets and neutrophils in a murine model of Trousseau syndrome
    • doi:10.1182/blood-2011-07-368514
    • Shao B, Wahrenbrock MG, Yao L, David T, Coughlin SR, Xia L, et al. Carcinoma mucins trigger reciprocal activation of platelets and neutrophils in a murine model of Trousseau syndrome. Blood (2011) 118:4015-23. doi:10.1182/blood-2011-07-368514
    • (2011) Blood , vol.118 , pp. 4015-4023
    • Shao, B.1    Wahrenbrock, M.G.2    Yao, L.3    David, T.4    Coughlin, S.R.5    Xia, L.6
  • 224
    • 84859305668 scopus 로고    scopus 로고
    • Recruitment of monocytes/macrophages by tissue factor-mediated coagulation is essential for metastatic cell survival and premetastatic niche establishment in mice
    • doi:10.1182/blood-2011-08-376426
    • Gil-Bernabe AM, Ferjancic S, Tlalka M, Zhao L, Allen PD, Im JH, et al. Recruitment of monocytes/macrophages by tissue factor-mediated coagulation is essential for metastatic cell survival and premetastatic niche establishment in mice. Blood (2012) 119:3164-75. doi:10.1182/blood-2011-08-376426
    • (2012) Blood , vol.119 , pp. 3164-3175
    • Gil-Bernabe, A.M.1    Ferjancic, S.2    Tlalka, M.3    Zhao, L.4    Allen, P.D.5    Im, J.H.6
  • 225
    • 84879177512 scopus 로고    scopus 로고
    • VCAM-1 and VAP-1 recruit myeloid cells that promote pulmonary metastasis in mice
    • doi:10.1182/blood-2012-08-449819
    • Ferjancic S, Gil-Bernabe AM, Hill SA, Allen PD, Richardson P, Sparey T, et al. VCAM-1 and VAP-1 recruit myeloid cells that promote pulmonary metastasis in mice. Blood (2013) 121:3289-97. doi:10.1182/blood-2012-08-449819
    • (2013) Blood , vol.121 , pp. 3289-3297
    • Ferjancic, S.1    Gil-Bernabe, A.M.2    Hill, S.A.3    Allen, P.D.4    Richardson, P.5    Sparey, T.6
  • 226
    • 0033559617 scopus 로고    scopus 로고
    • Rapid induction of cytokine and E-selectin expression in the liver in response to metastatic tumor cells
    • Khatib AM, Kontogiannea M, Fallavollita L, Jamison B, Meterissian S, Brodt P. Rapid induction of cytokine and E-selectin expression in the liver in response to metastatic tumor cells. Cancer Res (1999) 59:1356-61.
    • (1999) Cancer Res , vol.59 , pp. 1356-1361
    • Khatib, A.M.1    Kontogiannea, M.2    Fallavollita, L.3    Jamison, B.4    Meterissian, S.5    Brodt, P.6
  • 227
    • 33845982933 scopus 로고    scopus 로고
    • Involvement of p38alpha mitogen-activated protein kinase in lung metastasis of tumor cells
    • doi:10.1074/jbc.M604371200
    • Matsuo Y, Amano S, Furuya M, Namiki K, Sakurai K, Nishiyama M, et al. Involvement of p38alpha mitogen-activated protein kinase in lung metastasis of tumor cells. J Biol Chem (2006) 281:36767-75. doi:10.1074/jbc.M604371200
    • (2006) J Biol Chem , vol.281 , pp. 36767-36775
    • Matsuo, Y.1    Amano, S.2    Furuya, M.3    Namiki, K.4    Sakurai, K.5    Nishiyama, M.6
  • 228
    • 12944254582 scopus 로고    scopus 로고
    • IL-18 regulates IL-1beta-dependent hepatic melanoma metastasis via vascular cell adhesion molecule-1
    • doi:10.1073/pnas.97.2.734
    • Vidal-Vanaclocha F, Fantuzzi G, Mendoza L, Fuentes AM, Anasagasti MJ, Martin J, et al. IL-18 regulates IL-1beta-dependent hepatic melanoma metastasis via vascular cell adhesion molecule-1. Proc Natl Acad Sci U S A (2000) 97:734-9. doi:10.1073/pnas.97.2.734
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 734-739
    • Vidal-Vanaclocha, F.1    Fantuzzi, G.2    Mendoza, L.3    Fuentes, A.M.4    Anasagasti, M.J.5    Martin, J.6
  • 229
    • 0034660854 scopus 로고    scopus 로고
    • Cimetidine inhibits cancer cell adhesion to endothelial cells and prevents metastasis by blocking E-selectin expression
    • Kobayashi K, Matsumoto S, Morishima T, Kawabe T, Okamoto T. Cimetidine inhibits cancer cell adhesion to endothelial cells and prevents metastasis by blocking E-selectin expression. Cancer Res (2000) 60:3978-84.
    • (2000) Cancer Res , vol.60 , pp. 3978-3984
    • Kobayashi, K.1    Matsumoto, S.2    Morishima, T.3    Kawabe, T.4    Okamoto, T.5
  • 230
    • 70350381008 scopus 로고    scopus 로고
    • Chemokine (C-C motif) ligand 2 engages CCR2+ stromal cells of monocytic origin to promote breast cancer metastasis to lung and bone
    • doi:10.1074/jbc.M109.035899
    • Lu X, Kang Y. Chemokine (C-C motif) ligand 2 engages CCR2+ stromal cells of monocytic origin to promote breast cancer metastasis to lung and bone. J Biol Chem (2009) 284:29087-96. doi:10.1074/jbc.M109.035899
    • (2009) J Biol Chem , vol.284 , pp. 29087-29096
    • Lu, X.1    Kang, Y.2
  • 231
    • 68749109536 scopus 로고    scopus 로고
    • A distinct macrophage population mediates metastatic breast cancer cell extravasation, establishment and growth.
    • doi:10.1371/journal.pone.0006562
    • Qian B, Deng Y, Im JH, Muschel RJ, Zou Y, Li J, et al. A distinct macrophage population mediates metastatic breast cancer cell extravasation, establishment and growth. PLoS One (2009) 4:e6562. doi:10.1371/journal.pone.0006562
    • (2009) PLoS One , vol.4
    • Qian, B.1    Deng, Y.2    Im, J.H.3    Muschel, R.J.4    Zou, Y.5    Li, J.6
  • 232
    • 84863756518 scopus 로고    scopus 로고
    • Endothelial CCR2 signaling induced by colon carcinoma cells enables extravasation via the JAK2-Stat5 and p38MAPK pathway
    • doi:10.1016/j.ccr.2012.05.023
    • Wolf MJ, Hoos A, Bauer J, Boettcher S, Knust M, Weber A, et al. Endothelial CCR2 signaling induced by colon carcinoma cells enables extravasation via the JAK2-Stat5 and p38MAPK pathway. Cancer Cell (2012) 22:91-105. doi:10.1016/j.ccr.2012.05.023
    • (2012) Cancer Cell , vol.22 , pp. 91-105
    • Wolf, M.J.1    Hoos, A.2    Bauer, J.3    Boettcher, S.4    Knust, M.5    Weber, A.6
  • 233
    • 84881010019 scopus 로고    scopus 로고
    • Renewed interest in basic and applied research involving monoclonal antibodies against an oncofetal Tn-antigen
    • doi:10.1093/jb/mvt052
    • Fujita-Yamaguchi Y. Renewed interest in basic and applied research involving monoclonal antibodies against an oncofetal Tn-antigen. J Biochem (2013) 154:103-5. doi:10.1093/jb/mvt052
    • (2013) J Biochem , vol.154 , pp. 103-105
    • Fujita-Yamaguchi, Y.1
  • 234
    • 67349288453 scopus 로고    scopus 로고
    • Sialyl-Tn vaccine induces antibody-mediated tumour protection in a relevant murine model
    • doi:10.1038/sj.bjc.6605083
    • Julien S, Picco G, Sewell R, Vercoutter-Edouart AS, Tarp M, Miles D, et al. Sialyl-Tn vaccine induces antibody-mediated tumour protection in a relevant murine model. Br J Cancer (2009) 100:1746-54. doi:10.1038/sj.bjc.6605083
    • (2009) Br J Cancer , vol.100 , pp. 1746-1754
    • Julien, S.1    Picco, G.2    Sewell, R.3    Vercoutter-Edouart, A.S.4    Tarp, M.5    Miles, D.6
  • 235
    • 84893057242 scopus 로고    scopus 로고
    • Survival advantage in patients with metastatic breast cancer receiving endocrine therapy plus Sialyl Tn-KLH vaccine: post hoc analysis of a large randomized trial
    • doi:10.7150/jca.7028
    • Ibrahim NK, Murray JL, Zhou D, Mittendorf EA, Sample D, Tautchin M, et al. Survival advantage in patients with metastatic breast cancer receiving endocrine therapy plus Sialyl Tn-KLH vaccine: post hoc analysis of a large randomized trial. J Cancer (2013) 4:577-84. doi:10.7150/jca.7028
    • (2013) J Cancer , vol.4 , pp. 577-584
    • Ibrahim, N.K.1    Murray, J.L.2    Zhou, D.3    Mittendorf, E.A.4    Sample, D.5    Tautchin, M.6
  • 236
    • 85179272500 scopus 로고    scopus 로고
    • Heparin in cancer: role of selectin interactions.
    • Khorana AA, Francis CW, editors. New York: Informa Healthcare
    • Borsig L, Stevenson JL, Varki A. Heparin in cancer: role of selectin interactions. In: Khorana AA, Francis CW, editors. Cancer-Associated Thrombosis. New York: Informa Healthcare (2007). p. 97-113.
    • (2007) Cancer-Associated Thrombosis. , pp. 97-113
    • Borsig, L.1    Stevenson, J.L.2    Varki, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.