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Volumn 137, Issue 7, 2015, Pages 1652-1660

Expression of mucin 1 possessing a 3′-sulfated core1 in recurrent and metastatic breast cancer

Author keywords

3 sulfated core1; breast cancer; galectin 4; metastasis; MUC1; tumor marker

Indexed keywords

3' SULFATED CORE1 PROTEIN; CA 15-3 ANTIGEN; MUCIN 1; TRANSCRIPTION FACTOR GAL4; TUMOR MARKER; TUMOR PROTEIN; UNCLASSIFIED DRUG; GALECTIN 4; MONOCLONAL ANTIBODY; MUC1 PROTEIN, HUMAN;

EID: 84943389954     PISSN: 00207136     EISSN: 10970215     Source Type: Journal    
DOI: 10.1002/ijc.29520     Document Type: Article
Times cited : (33)

References (31)
  • 1
    • 0021132973 scopus 로고
    • Monoclonal antibodies against human milk-fat globule membranes detecting differentiation antigens of the mammary gland and its tumors
    • Hilkens J, Buijs F, Hilgers J, et al., Monoclonal antibodies against human milk-fat globule membranes detecting differentiation antigens of the mammary gland and its tumors. Int J Cancer 1984; 34: 197-206.
    • (1984) Int J Cancer , vol.34 , pp. 197-206
    • Hilkens, J.1    Buijs, F.2    Hilgers, J.3
  • 2
    • 70450247207 scopus 로고    scopus 로고
    • Mucins in cancer function, prognosis and therapy
    • Kufe DW,. Mucins in cancer function, prognosis and therapy. Nat Rev Cancer 2009; 9: 874-5.
    • (2009) Nat Rev Cancer , vol.9 , pp. 874-875
    • Kufe, D.W.1
  • 3
    • 0026659195 scopus 로고
    • Tumor selective reactivity of a monoclonal antibody prepared against a recombinant peptide derived from the DF3 human breast carcinoma-associated antigen
    • Perey L, Hayes DF, Maimonis P, et al., Tumor selective reactivity of a monoclonal antibody prepared against a recombinant peptide derived from the DF3 human breast carcinoma-associated antigen. Cancer Res 1992; 52: 2563-8.
    • (1992) Cancer Res , vol.52 , pp. 2563-2568
    • Perey, L.1    Hayes, D.F.2    Maimonis, P.3
  • 5
    • 0024798333 scopus 로고
    • Oligosaccharide differences in the DF3 sialomucin antigen from normal human milk and the BT-20 human breast carcinoma cell line
    • Hull SR, Bright A, Carraway KL, et al., Oligosaccharide differences in the DF3 sialomucin antigen from normal human milk and the BT-20 human breast carcinoma cell line. Cancer Commun 1989; 1: 261-7.
    • (1989) Cancer Commun , vol.1 , pp. 261-267
    • Hull, S.R.1    Bright, A.2    Carraway, K.L.3
  • 6
    • 0026495694 scopus 로고
    • Effects of differentiating agents on cell surface expression of the breast carcinoma-associated DF3-Pepitope
    • Perey L, Hayes DF, Kufe D,. Effects of differentiating agents on cell surface expression of the breast carcinoma-associated DF3-Pepitope. Cancer Res 1992; 52: 6365-70.
    • (1992) Cancer Res , vol.52 , pp. 6365-6370
    • Perey, L.1    Hayes, D.F.2    Kufe, D.3
  • 7
    • 84855879682 scopus 로고    scopus 로고
    • Novel O-linked glycans containing 6'-sulfo-gal/GalNAc of MUC1 secreted from human breast cancer YMB-S cells: Possible carbohydrate epitopes of KL-6(MUC1) monoclonal antibody
    • Seko A, Ohkura T, Ideo H, et al., Novel O-linked glycans containing 6'-sulfo-gal/GalNAc of MUC1 secreted from human breast cancer YMB-S cells: possible carbohydrate epitopes of KL-6(MUC1) monoclonal antibody. Glycobiology 2012; 22: 181-95.
    • (2012) Glycobiology , vol.22 , pp. 181-195
    • Seko, A.1    Ohkura, T.2    Ideo, H.3
  • 8
    • 0030884997 scopus 로고    scopus 로고
    • The enzymatic sulfation of glycoprotein carbohydrate units: Blood group T-hapten specific and two other distinct gal: 3-O-sulfotransferases as evident from specificities and kinetics and the influence of sulfate and fucose residues occurring in the carbohydrate chain on C-3 sulfation of terminal Gal
    • Chandrasekaran EV, Jain RK, Vig R, et al., The enzymatic sulfation of glycoprotein carbohydrate units: blood group T-hapten specific and two other distinct gal: 3-O-sulfotransferases as evident from specificities and kinetics and the influence of sulfate and fucose residues occurring in the carbohydrate chain on C-3 sulfation of terminal Gal. Glycobiology 1997; 7: 753-68.
    • (1997) Glycobiology , vol.7 , pp. 753-768
    • Chandrasekaran, E.V.1    Jain, R.K.2    Vig, R.3
  • 9
    • 3042845879 scopus 로고    scopus 로고
    • Differential expression of MUC1, MUC2, and MUC5Ac in carcinomas of various sites: An immunohistochemical study
    • Lau SK, Weiss LM, Chu PG,. Differential expression of MUC1, MUC2, and MUC5Ac in carcinomas of various sites: an immunohistochemical study. Am J Clin Pathol 2004; 122: 61-9.
    • (2004) Am J Clin Pathol , vol.122 , pp. 61-69
    • Lau, S.K.1    Weiss, L.M.2    Chu, P.G.3
  • 11
    • 0016396340 scopus 로고
    • Production of microbial neuraminidase induced by colominic acid
    • Uchida Y, Tsukada Y, Sugimori T,. Production of microbial neuraminidase induced by colominic acid. Biochim Biophy Acta 1974; 350: 425-31.
    • (1974) Biochim Biophy Acta , vol.350 , pp. 425-431
    • Uchida, Y.1    Tsukada, Y.2    Sugimori, T.3
  • 12
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • Ideo H, Seko A, Ishizuka I, et al., The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology 2003; 13: 713-23.
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3
  • 13
    • 0025801937 scopus 로고
    • Double wavelength measurement of 3,3,5,5′- tetramethylbenzidine (TMB) provides a three-fold enhancement of the ELISA measuring range
    • Madersbacher S, Berger P,. Double wavelength measurement of 3,3,5,5′- tetramethylbenzidine (TMB) provides a three-fold enhancement of the ELISA measuring range. J Immunol Methods 1991; 138: 121-4.
    • (1991) J Immunol Methods , vol.138 , pp. 121-124
    • Madersbacher, S.1    Berger, P.2
  • 14
    • 0027457620 scopus 로고
    • Receiver-operating characteristic (ROC) plots: A fundamental evaluation tool in clinical medicine
    • Zweig MH, Campbell G,. Receiver-operating characteristic (ROC) plots: a fundamental evaluation tool in clinical medicine. Clin Chem 1993; 39: 561-77.
    • (1993) Clin Chem , vol.39 , pp. 561-577
    • Zweig, M.H.1    Campbell, G.2
  • 15
    • 84965179011 scopus 로고    scopus 로고
    • R Foundation for Statistical Computing 2005. Vienna, Austria
    • R Development Core Team. R: A language and environment for statistical computing. R Foundation for Statistical Computing 2005. Vienna, Austria. ISBN 3-900051-07-0. Available at: http://www.R-project.org.
    • R: A Language and Environment for Statistical Computing
  • 16
    • 33645529696 scopus 로고    scopus 로고
    • General rules for clinical and pathological recording of breast cancer
    • Japanese breast cancer society.
    • Sakamoto G, Inaji H, Akiyama F, et al., Japanese breast cancer society. General rules for clinical and pathological recording of breast cancer. Breast Cancer 2005; 12: S1-27.
    • (2005) Breast Cancer , vol.12 , pp. S1-S27
    • Sakamoto, G.1    Inaji, H.2    Akiyama, F.3
  • 17
    • 38449105118 scopus 로고    scopus 로고
    • Clinicopathologic significance of an immunohistochemical expression of p27 in scirrhous carcinoma of the breast
    • Nozoe T, Oyama T, Mori E, et al., Clinicopathologic significance of an immunohistochemical expression of p27 in scirrhous carcinoma of the breast. Breast Cancer 2007; 14: 277-80.
    • (2007) Breast Cancer , vol.14 , pp. 277-280
    • Nozoe, T.1    Oyama, T.2    Mori, E.3
  • 18
    • 0345390284 scopus 로고    scopus 로고
    • Tissue and serum sialidase levels in breast cancer
    • Sönmez H, Süer S, Güngör Z, et al., Tissue and serum sialidase levels in breast cancer. Cancer Lett 1999; 136: 75-8.
    • (1999) Cancer Lett , vol.136 , pp. 75-78
    • Sönmez, H.1    Süer, S.2    Güngör, Z.3
  • 19
    • 0026439093 scopus 로고
    • 3-6Galβ1-4GlcNAc specific lectin in tuberous roots of trichosanthes japonica
    • 3-6Galβ1-4GlcNAc specific lectin in tuberous roots of trichosanthes japonica. Biochemistry 1992; 31: 11647-50.
    • (1992) Biochemistry , vol.31 , pp. 11647-11650
    • Yamashita, K.1    Umetsu, K.2    Suzuki, T.3
  • 20
    • 0023644482 scopus 로고
    • The elderberry (Sambucus Nigra L.) Bark lectin recognizes the Neu5Ac(α2-6) Gal/GalNAc sequence
    • Shibuya N, Goldstein IJ, Broekaert WF, et al., The elderberry (Sambucus Nigra L.) Bark lectin recognizes the Neu5Ac(α2-6) Gal/GalNAc sequence. J Biol Chem 1987; 262: 1596-601.
    • (1987) J Biol Chem , vol.262 , pp. 1596-1601
    • Shibuya, N.1    Goldstein, I.J.2    Broekaert, W.F.3
  • 21
    • 0026020575 scopus 로고
    • Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins
    • Knibbs RN, Goldstein IJ, Ratcliffe RM, et al., Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins. J Biol Chem 1991; 266: 83-8.
    • (1991) J Biol Chem , vol.266 , pp. 83-88
    • Knibbs, R.N.1    Goldstein, I.J.2    Ratcliffe, R.M.3
  • 22
    • 0036952311 scopus 로고    scopus 로고
    • Occurrence of secretory glycoprotein specific GalNAcβ1-4GlcNAc sequence in N-glycans in MDCK cells
    • Ohkura T, Seko A, Hara-Kuge S, et al., Occurrence of secretory glycoprotein specific GalNAcβ1-4GlcNAc sequence in N-glycans in MDCK cells. J Biochem 2002; 132: 891-901.
    • (2002) J Biochem , vol.132 , pp. 891-901
    • Ohkura, T.1    Seko, A.2    Hara-Kuge, S.3
  • 23
    • 34547111331 scopus 로고    scopus 로고
    • Recognition mechanism of galectin-4 for sulfated compounds
    • Ideo H, Seko A, Yamashita K,. Recognition mechanism of galectin-4 for sulfated compounds. J Biol Chem 2007; 282: 21081-9.
    • (2007) J Biol Chem , vol.282 , pp. 21081-21089
    • Ideo, H.1    Seko, A.2    Yamashita, K.3
  • 24
    • 0032545476 scopus 로고    scopus 로고
    • Novel carbohydrate specificity of monoclonal antibody 91.9H prepared against human colonic sulfomucin: Recognition of sulfo-lewis(a) structure
    • Tsuji H, Hong JC, Kim YS, et al., Novel carbohydrate specificity of monoclonal antibody 91.9H prepared against human colonic sulfomucin: recognition of sulfo-lewis(a) structure. Biochem Biophys Res Commun 1998; 253: 374-81.
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 374-381
    • Tsuji, H.1    Hong, J.C.2    Kim, Y.S.3
  • 25
    • 0035967869 scopus 로고    scopus 로고
    • Novel sulfated lymphocyte homing receptors and their control by a core 1 extension beta 1,3-N-acetylglucosaminyltransferase
    • Yeh JC, Hiraoka N, Petryniak B, et al., Novel sulfated lymphocyte homing receptors and their control by a core 1 extension beta 1,3-N-acetylglucosaminyltransferase. Cell 2001; 105: 957-69.
    • (2001) Cell , vol.105 , pp. 957-969
    • Yeh, J.C.1    Hiraoka, N.2    Petryniak, B.3
  • 26
    • 27544432131 scopus 로고    scopus 로고
    • N-acetylglucosamine-6-O- sulfotransferases 1 and 2 cooperatively control lymphocyte homing through L-selectin ligand biosynthesis in high endothelial venules
    • Kawashima H, Petryniak B, Hiraoka N, et al., N-acetylglucosamine-6-O- sulfotransferases 1 and 2 cooperatively control lymphocyte homing through L-selectin ligand biosynthesis in high endothelial venules. Nat Immunol 2005; 6: 1096-104.
    • (2005) Nat Immunol , vol.6 , pp. 1096-1104
    • Kawashima, H.1    Petryniak, B.2    Hiraoka, N.3
  • 27
    • 27544487771 scopus 로고    scopus 로고
    • A major class of L-selectin ligands is eliminated in mice deficient in two sulfotransferases expressed in high endothelial venules
    • Uchimura K, Gauguet JM, Singer MS, et al., A major class of L-selectin ligands is eliminated in mice deficient in two sulfotransferases expressed in high endothelial venules. Nat Immunol 2005; 6: 1105-13.
    • (2005) Nat Immunol , vol.6 , pp. 1105-1113
    • Uchimura, K.1    Gauguet, J.M.2    Singer, M.S.3
  • 28
    • 84887950623 scopus 로고    scopus 로고
    • Phosphorylation and externalization of galectin-4 is controlled by src family kinases
    • Ideo H, Hoshi I, Yamashita K, et al., Phosphorylation and externalization of galectin-4 is controlled by src family kinases. Glycobiology 2013; 23: 1452-62.
    • (2013) Glycobiology , vol.23 , pp. 1452-1462
    • Ideo, H.1    Hoshi, I.2    Yamashita, K.3
  • 29
    • 50449111478 scopus 로고    scopus 로고
    • Expression profiles of MUC1, MUC2, and MUC4 mucins in human neoplasms and their relationship with biological behavior
    • Yonezawa S, Goto M, Yamada N, et al., Expression profiles of MUC1, MUC2, and MUC4 mucins in human neoplasms and their relationship with biological behavior. Proteomics 2008; 8: 3329-41.
    • (2008) Proteomics , vol.8 , pp. 3329-3341
    • Yonezawa, S.1    Goto, M.2    Yamada, N.3
  • 30
    • 0024077916 scopus 로고
    • Detection of soluble tumor-associated antigens in sera and effusion using novel monoclonal antibodies, KL-3 and KL-6, against lung adenocarcinoma
    • Kohno N, Akiyama M, Kyoizumi S, et al., Detection of soluble tumor-associated antigens in sera and effusion using novel monoclonal antibodies, KL-3 and KL-6, against lung adenocarcinoma. Jpn J Clin Oncol 1988; 18: 203-16.
    • (1988) Jpn J Clin Oncol , vol.18 , pp. 203-216
    • Kohno, N.1    Akiyama, M.2    Kyoizumi, S.3
  • 31
    • 79960980007 scopus 로고    scopus 로고
    • Panel members. Strategies for subtypes-dealing with the diversity of breast cancer: Highlights of the st. Gallen international expert consensus on the primary therapy of early breast cancer 2011
    • Goldhirch A, Wood WC, Coates AS, et al., Panel members. Strategies for subtypes-dealing with the diversity of breast cancer: highlights of the st. Gallen international expert consensus on the primary therapy of early breast cancer 2011. Ann Oncol 2011; 22: 1736-47.
    • (2011) Ann Oncol , vol.22 , pp. 1736-1747
    • Goldhirch, A.1    Wood, W.C.2    Coates, A.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.