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Volumn 31, Issue 6, 2014, Pages 509-521

Overexpression of α2,3sialyl T-antigen in breast cancer determined by miniaturized glycosyltransferase assays and confirmed using tissue microarray immunohistochemical analysis

Author keywords

Breast; Carbohydrate; Glycosyltransferase; O glycans; Tissue microarray; Tumor

Indexed keywords

ALPHA 1,3 FUCOSYLTRANSFERASE; ALPHA 1,4 FUCOSYLTRANSFERASE; ALPHA 2,3 SIALYLTRANSFERASE; BETA 1,3 GALACTOSYLTRANSFERASE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FUCOSYLTRANSFERASE; GALACTOSYLTRANSFERASE; GLYCOCONJUGATE; SIALYLTRANSFERASE; UNCLASSIFIED DRUG; GLUCOSYLTRANSFERASE; TUMOR ANTIGEN;

EID: 84926627451     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-014-9548-4     Document Type: Article
Times cited : (24)

References (37)
  • 1
    • 81855194825 scopus 로고    scopus 로고
    • Systems glycobiology: Biochemical reaction networks regulating glycan structure and function
    • Neelamegham, S., Liu, G.: Systems glycobiology: biochemical reaction networks regulating glycan structure and function. Glycobiology 21(12), 1541-1553 (2011)
    • (2011) Glycobiology , vol.21 , Issue.12 , pp. 1541-1553
    • Neelamegham, S.1    Liu, G.2
  • 2
    • 0034963231 scopus 로고    scopus 로고
    • Tumor-associated carbohydrate antigens defining tumormalignancy: Basis for development of anti-cancer vaccines
    • Hakomori, S.: Tumor-associated carbohydrate antigens defining tumormalignancy: basis for development of anti-cancer vaccines. Adv. Exp. Med. Biol. 491, 369-402 (2001)
    • (2001) Adv. Exp. Med. Biol , vol.491 , pp. 369-402
    • Hakomori, S.1
  • 3
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by Nacetylglucosaminyltransferase III gene transfection
    • Yoshimura, M., Nishikawa, A., Ihara, Y., Taniguchi, S., Taniguchi, N.: Suppression of lung metastasis of B16 mouse melanoma by Nacetylglucosaminyltransferase III gene transfection. Proc.Natl. Acad. Sci. U. S. A. 92(19), 8754-8758 (1995)
    • (1995) Proc.Natl. Acad. Sci. U. S. A. , vol.92 , Issue.19 , pp. 8754-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Taniguchi, S.4    Taniguchi, N.5
  • 6
    • 80052424869 scopus 로고    scopus 로고
    • Effect of sulfated glycosaminoglycans on tumor invasion and metastasis
    • Kozlowski, E.O., Pavao, M.S.: Effect of sulfated glycosaminoglycans on tumor invasion and metastasis. Front. Biosci. 3, 1541-1551 (2011)
    • (2011) Front. Biosci , vol.3 , pp. 1541-1551
    • Kozlowski, E.O.1    Pavao, M.S.2
  • 7
    • 36049013035 scopus 로고    scopus 로고
    • Heparin attenuates metastasis mainly due to inhibition of P- and L-selectin, but non-anticoagulant heparins can have additional effects
    • Stevenson, J.L., Varki, A., Borsig, L.: Heparin attenuates metastasis mainly due to inhibition of P- and L-selectin, but non-anticoagulant heparins can have additional effects. Thromb. Res. 120, Supplement 2(0), S107-S111 (2007)
    • (2007) Thromb. Res , vol.120 , pp. S107-S111
    • Stevenson, J.L.1    Varki, A.2    Borsig, L.3
  • 9
    • 79953298958 scopus 로고    scopus 로고
    • Next-generation mTOR inhibitors in clinical oncology: How pathway complexity informs therapeutic strategy
    • Wander, S.A., Hennessy, B.T., Slingerland, J.M.: Next-generation mTOR inhibitors in clinical oncology: how pathway complexity informs therapeutic strategy. J. Clin. Invest. 121(4), 1231-1241 (2011)
    • (2011) J. Clin. Invest , vol.121 , Issue.4 , pp. 1231-1241
    • Wander, S.A.1    Hennessy, B.T.2    Slingerland, J.M.3
  • 10
    • 33745325007 scopus 로고    scopus 로고
    • Mechanisms of drug inhibition of signalling molecules
    • Sebolt-Leopold, J.S., English, J.M.: Mechanisms of drug inhibition of signalling molecules. Nature 441(7092), 457-462 (2006)
    • (2006) Nature , vol.441 , Issue.7092 , pp. 457-462
    • Sebolt-Leopold, J.S.1    English, J.M.2
  • 11
    • 33748171538 scopus 로고    scopus 로고
    • The pattern of glycosyl- and sulfotransferase activities in cancer cell lines: A predictor of individual cancer-associated distinct carbohydrate structures for the structural identification of signature glycans
    • Chandrasekaran, E.V., Xue, J., Neelamegham, S., Matta, K.L.: The pattern of glycosyl- and sulfotransferase activities in cancer cell lines: a predictor of individual cancer-associated distinct carbohydrate structures for the structural identification of signature glycans. Carbohydr. Res. 341(8), 983-994 (2006)
    • (2006) Carbohydr. Res , vol.341 , Issue.8 , pp. 983-994
    • Chandrasekaran, E.V.1    Xue, J.2    Neelamegham, S.3    Matta, K.L.4
  • 12
    • 79960415851 scopus 로고    scopus 로고
    • Engagement of I-branching β-1, 6-Nacetylglucosaminyltransferase 2 in breast cancer metastasis and TGF-β signaling
    • Zhang, H., Meng, F., Wu, S., Kreike, B., Sethi, S., Chen, W., Miller, F.R., Wu, G.: Engagement of I-branching β-1, 6-Nacetylglucosaminyltransferase 2 in breast cancer metastasis and TGF-β signaling. Cancer Res. 71(14), 4846-4856 (2011)
    • (2011) Cancer Res , vol.71 , Issue.14 , pp. 4846-4856
    • Zhang, H.1    Meng, F.2    Wu, S.3    Kreike, B.4    Sethi, S.5    Chen, W.6    Miller, F.R.7    Wu, G.8
  • 14
    • 70649087034 scopus 로고    scopus 로고
    • Differential expression of α-2,3-sialyltransferases and α-1,3/4- fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells. Int
    • Carvalho, A.S., Harduin-Lepers, A., Magalhães, A., Machado, E., Mendes, N., Costa, L.T.,Matthiesen, R., Almeida, R., Costa, J., Reis, C.A.: Differential expression of α-2,3-sialyltransferases and α-1,3/4- fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells. Int. J. Biochem. Cell Biol. 42(1), 80-89 (2010)
    • (2010) J. Biochem. Cell Biol , vol.42 , Issue.1 , pp. 80-89
    • Carvalho, A.S.1    Harduin-Lepers, A.2    Magalhães, A.3    Machado, E.4    Mendes, N.5    Costa, L.T.6    Matthiesen, R.7    Almeida, R.8    Costa, J.9    Reis, C.A.10
  • 15
    • 0032530423 scopus 로고    scopus 로고
    • Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer
    • Recchi, M.-A., Hebbar, M., Hornez, L., Harduin-Lepers, A., Peyrat, J.-P., Delannoy, P.: Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer. Cancer Res. 58(18), 4066-4070 (1998)
    • (1998) Cancer Res , vol.58 , Issue.18 , pp. 4066-4070
    • Recchi, M.-A.1    Hebbar, M.2    Hornez, L.3    Harduin-Lepers, A.4    Peyrat, J.-P.5    Delannoy, P.6
  • 16
    • 77955401818 scopus 로고    scopus 로고
    • GlcNAcylation plays an essential role in breast cancer metastasis
    • Gu, Y., Mi, W., Ge, Y., Liu, H., Fan, Q., Han, C., Yang, J., Han, F., Lu, X.,Yu,W.: GlcNAcylation plays an essential role in breast cancer metastasis. Cancer Res. 70(15), 6344-6351 (2010)
    • (2010) Cancer Res , vol.70 , Issue.15 , pp. 6344-6351
    • Gu, Y.1    Mi, W.2    Ge, Y.3    Liu, H.4    Fan, Q.5    Han, C.6    Yang, J.7    Han, F.8    Lu, X.9    Yu, W.10
  • 17
    • 0030003950 scopus 로고    scopus 로고
    • Quantitative differences in GlcNAc:β1->3 and GlcNAc:β1->4 galactosyltransferase activities between human colonic adenocarcinomas and normal colonic mucosa
    • Seko, A., Ohkura, T., Kitamura, H., Yonezawa, S., Sato, E., Yamashita, K.: Quantitative differences in GlcNAc:β1->3 and GlcNAc:β1->4 galactosyltransferase activities between human colonic adenocarcinomas and normal colonic mucosa. Cancer Res. 56(15), 3468-3473 (1996)
    • (1996) Cancer Res , vol.56 , Issue.15 , pp. 3468-3473
    • Seko, A.1    Ohkura, T.2    Kitamura, H.3    Yonezawa, S.4    Sato, E.5    Yamashita, K.6
  • 18
    • 34447531767 scopus 로고    scopus 로고
    • Potential tumor markers for human gastric cancer: An elevation of glycan:sulfotransferases and a concomitant loss of α1,2-fucosyltransferase activities
    • Chandrasekaran, E., Xue, J., Piskorz, C., Locke, R., Tóth, K., Slocum, H., Matta, K.: Potential tumor markers for human gastric cancer: an elevation of glycan:sulfotransferases and a concomitant loss of α1,2-fucosyltransferase activities. J. Cancer Res. Clin. Oncol. 133(9), 599-611 (2007)
    • (2007) J. Cancer Res. Clin. Oncol , vol.133 , Issue.9 , pp. 599-611
    • Chandrasekaran, E.1    Xue, J.2    Piskorz, C.3    Locke, R.4    Tóth, K.5    Slocum, H.6    Matta, K.7
  • 19
    • 84857881654 scopus 로고    scopus 로고
    • α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: A combinatorial approach for development of glycan biomarkers
    • Park, S.-Y., Lee, S.-H., Kawasaki, N., Itoh, S., Kang,K., Hee Ryu, S., Hashii, N., Kim, J.-M., Kim, J.-Y., Hoe Kim, J.: α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers. Int. J. Cancer 130(10), 2366-2376 (2012)
    • (2012) Int. J. Cancer , vol.130 , Issue.10 , pp. 2366-2376
    • Park, S.-Y.1    Lee, S.-H.2    Kawasaki, N.3    Itoh, S.4    Kang, K.5    Hee Ryu, S.6    Hashii, N.7    Kim, J.-M.8    Kim, J.-Y.9    Hoe Kim, J.10
  • 22
    • 77956530498 scopus 로고    scopus 로고
    • Levels of specific glycans significantly distinguish lymph node-positive from lymph node-negative breast cancer patients
    • Pierce, A., Saldova, R., Abd Hamid, U.M., Abrahams, J.L., McDermott, E.W., Evoy, D., Duffy, M.J., Rudd, P.M.: Levels of specific glycans significantly distinguish lymph node-positive from lymph node-negative breast cancer patients. Glycobiology 20(10), 1283-1288 (2010)
    • (2010) Glycobiology , vol.20 , Issue.10 , pp. 1283-1288
    • Pierce, A.1    Saldova, R.2    Abd Hamid, U.M.3    Abrahams, J.L.4    McDermott, E.W.5    Evoy, D.6    Duffy, M.J.7    Rudd, P.M.8
  • 23
    • 84859933834 scopus 로고    scopus 로고
    • Scaling down the size and increasing the throughput of glycosyltransferase assays: Activity changes on stem cell differentiation
    • Patil, S.A., Chandrasekaran, E.V., Matta, K.L., Parikh, A., Tzanakakis, E.S., Neelamegham, S.: Scaling down the size and increasing the throughput of glycosyltransferase assays: activity changes on stem cell differentiation. Anal. Biochem. 425(2), 135- 144 (2012)
    • (2012) Anal. Biochem , vol.425 , Issue.2 , pp. 135-144
    • Patil, S.A.1    Chandrasekaran, E.V.2    Matta, K.L.3    Parikh, A.4    Tzanakakis, E.S.5    Neelamegham, S.6
  • 24
    • 57349199782 scopus 로고    scopus 로고
    • Systems-level studies of glycosyltransferase gene expression and enzyme activity that are associated with the selectin binding function of human leukocytes
    • Marathe, D.D., Chandrasekaran, E.V., Lau, J.T., Matta, K.L., Neelamegham, S.: Systems-level studies of glycosyltransferase gene expression and enzyme activity that are associated with the selectin binding function of human leukocytes. FASEB J. 22(12), 4154-4167 (2008)
    • (2008) FASEB J , vol.22 , Issue.12 , pp. 4154-4167
    • Marathe, D.D.1    Chandrasekaran, E.V.2    Lau, J.T.3    Matta, K.L.4    Neelamegham, S.5
  • 25
    • 28244486825 scopus 로고    scopus 로고
    • Analysis of the specificity of sialyltransferases toward mucin core 2, globo, and related structures. Identification of the sialylation sequence and the effects of sulfate, fucose, methyl, and fluoro substituents of the carbohydrate chain in the biosynthesis of selectin and siglec ligands, and novel sialylation by cloned alpha2,3(O)sialyltransferase
    • Chandrasekaran, E.V., Xue, J., Xia, J., Chawda, R., Piskorz, C., Locke, R.D., Neelamegham, S., Matta, K.L.: Analysis of the specificity of sialyltransferases toward mucin core 2, globo, and related structures. identification of the sialylation sequence and the effects of sulfate, fucose, methyl, and fluoro substituents of the carbohydrate chain in the biosynthesis of selectin and siglec ligands, and novel sialylation by cloned alpha2,3(O)sialyltransferase. Biochemistry 44(47), 15619-15635 (2005)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15619-15635
    • Chandrasekaran, E.V.1    Xue, J.2    Xia, J.3    Chawda, R.4    Piskorz, C.5    Locke, R.D.6    Neelamegham, S.7    Matta, K.L.8
  • 26
    • 77949514632 scopus 로고    scopus 로고
    • Fluorinated per-acetylated GalNAc metabolically alters glycan structures on leukocyte PSGL-1 and reduces cell binding to selectins
    • Marathe,D.D., Buffone Jr., A., Chandrasekaran, E.V., Xue, J., Locke, R.D., Nasirikenari, M., Lau, J.T., Matta, K.L., Neelamegham, S.: Fluorinated per-acetylated GalNAc metabolically alters glycan structures on leukocyte PSGL-1 and reduces cell binding to selectins. Blood 115(6), 1303-1312 (2010)
    • (2010) Blood , vol.115 , Issue.6 , pp. 1303-1312
    • Marathe, D.D.1    Buffone, A.2    Chandrasekaran, E.V.3    Xue, J.4    Locke, R.D.5    Nasirikenari, M.6    Lau, J.T.7    Matta, K.L.8    Neelamegham, S.9
  • 27
    • 0028914045 scopus 로고
    • A new monoclonal antibody (A78-G/A7) to the Thomsen-Friedenreich pantumor antigen
    • Karsten, U., Butschak, G., Cao, Y., Goletz, S., Hanisch, F.G.: A new monoclonal antibody (A78-G/A7) to the Thomsen-Friedenreich pantumor antigen. Hybridoma 14(1), 37-44 (1995)
    • (1995) Hybridoma , vol.14 , Issue.1 , pp. 37-44
    • Karsten, U.1    Butschak, G.2    Cao, Y.3    Goletz, S.4    Hanisch, F.G.5
  • 29
    • 58249096139 scopus 로고    scopus 로고
    • Prognostic utility of glycosyltransferase expression in breast cancer
    • Patani, N., Jiang,W.E.N., Mokbel, K.: Prognostic utility of glycosyltransferase expression in breast cancer. Cancer Genomics Proteomics 5(6), 333-340 (2008)
    • (2008) Cancer Genomics Proteomics , vol.5 , Issue.6 , pp. 333-340
    • Patani, N.1    Jiang, W.E.N.2    Mokbel, K.3
  • 31
    • 0030466993 scopus 로고    scopus 로고
    • Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines
    • Lloyd, K.O., Burchell, J., Kudryashov, V., Yin, B.W.T., Taylor- Papadimitriou, J.: Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. J. Biol. Chem. 271(52), 33325-33334 (1996)
    • (1996) J. Biol. Chem , vol.271 , Issue.52 , pp. 33325-33334
    • Lloyd, K.O.1    Burchell, J.2    Kudryashov, V.3    Yin, B.W.T.4    Taylor- Papadimitriou, J.5
  • 36
    • 0037135544 scopus 로고    scopus 로고
    • Recombinant MUC1 probe authentically reflects cell-specific O-glycosylation profiles of endogenous breast cancer mucin
    • Muller, S., Hanisch, F.-G.: Recombinant MUC1 probe authentically reflects cell-specific O-glycosylation profiles of endogenous breast cancer mucin. J. Biol. Chem. 277(29), 26103-26112 (2002)
    • (2002) J. Biol. Chem , vol.277 , Issue.29 , pp. 26103-26112
    • Muller, S.1    Hanisch, F.-G.2
  • 37
    • 27944438104 scopus 로고    scopus 로고
    • Transmembrane and secreted MUC1 probes show trafficking-dependent changes in O-glycan core profiles
    • Engelmann, K., Kinlough, C.L., Muller, S., Razawi, H., Baldus, S.E., Hughey, R.P., Hanisch, F.-G.: Transmembrane and secreted MUC1 probes show trafficking-dependent changes in O-glycan core profiles. Glycobiology 15(11), 1111-1124 (2005)
    • (2005) Glycobiology , vol.15 , Issue.11 , pp. 1111-1124
    • Engelmann, K.1    Kinlough, C.L.2    Muller, S.3    Razawi, H.4    Baldus, S.E.5    Hughey, R.P.6    Hanisch, F.-G.7


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