메뉴 건너뛰기




Volumn 9, Issue 2, 2014, Pages

Discovery of specific metastasis-related N-glycan alterations in epithelial ovarian cancer based on quantitative glycomics

Author keywords

[No Author keywords available]

Indexed keywords

LECTIN; MANNOSYL (BETA 1,4) GLYCOPROTEIN BETA 1,4 N ACETYLGLUCOSAMINYLTRANSFERASE; MESSENGER RNA; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINYLTRANSFERASE; PROTEOME; STABLE ISOTOPE; UNCLASSIFIED DRUG; BETA-1,4-MANNOSYL-GLYCOPROTEIN BETA-1,4-N-ACETYLGLUCOSAMINYLTRANSFERASE; NITROGEN; POLYSACCHARIDE;

EID: 84895522938     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0087978     Document Type: Article
Times cited : (50)

References (80)
  • 2
    • 77958484951 scopus 로고    scopus 로고
    • The genesis and evolution of high-grade serous ovarian cancer
    • Bowtell DD (2010) The genesis and evolution of high-grade serous ovarian cancer. Nat Rev Cancer 10: 803-808.
    • (2010) Nat Rev Cancer , vol.10 , pp. 803-808
    • Bowtell, D.D.1
  • 4
    • 78649902935 scopus 로고    scopus 로고
    • LC-MS/MS analysis of ovarian cancer metastasis-related proteins using a nude mouse model: 14-3-3 Zeta as a candidate biomarker
    • He Y, Wu X, Liu X, Yan G, Xu C (2010) LC-MS/MS analysis of ovarian cancer metastasis-related proteins using a nude mouse model: 14-3-3 zeta as a candidate biomarker. J Proteome Res 9: 6180-6190.
    • (2010) J Proteome Res , vol.9 , pp. 6180-6190
    • He, Y.1    Wu, X.2    Liu, X.3    Yan, G.4    Xu, C.5
  • 6
    • 0037358831 scopus 로고    scopus 로고
    • A risk of malignancy index in preoperative diagnosis of ovarian cancer
    • Ma S, Shen K, Lang J (2003) A risk of malignancy index in preoperative diagnosis of ovarian cancer. Chin Med J (Engl) 116: 396-399. (Pubitemid 36432763)
    • (2003) Chinese Medical Journal , vol.116 , Issue.3 , pp. 396-399
    • Ma, S.1    Shen, K.2    Lang, J.3
  • 8
    • 33645378248 scopus 로고    scopus 로고
    • Sampling the omentum in ovarian neoplasia: When one block is enough
    • Doig T, Monaghan H (2006) Sampling the omentum in ovarian neoplasia: when one block is enough. Int J Gynecol Cancer 16: 36-40.
    • (2006) Int J Gynecol Cancer , vol.16 , pp. 36-40
    • Doig, T.1    Monaghan, H.2
  • 9
    • 41849105806 scopus 로고    scopus 로고
    • The initial steps of ovarian cancer cell metastasis are mediated by MMP-2 cleavage of vitronectin and fibronectin
    • DOI 10.1172/JCI33775
    • Kenny HA, Kaur S, Coussens LM, Lengyel E (2008) The initial steps of ovarian cancer cell metastasis are mediated by MMP-2 cleavage of vitronectin and fibronectin. J Clin Invest 118: 1367-1379. (Pubitemid 351500430)
    • (2008) Journal of Clinical Investigation , vol.118 , Issue.4 , pp. 1367-1379
    • Kenny, H.A.1    Kaur, S.2    Coussens, L.M.3    Lengyel, E.4
  • 10
    • 40749109360 scopus 로고    scopus 로고
    • The impact of comorbidity and stage on ovarian cancer mortality: A nationwide Danish cohort study
    • Tetsche MS, Dethlefsen C, Pedersen L, Sorensen HT, Norgaard M (2008) The impact of comorbidity and stage on ovarian cancer mortality: a nationwide Danish cohort study. BMC Cancer 8: 31.
    • (2008) BMC Cancer , vol.8 , pp. 31
    • Tetsche, M.S.1    Dethlefsen, C.2    Pedersen, L.3    Sorensen, H.T.4    Norgaard, M.5
  • 12
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • DOI 10.1038/nrc1649
    • Fuster MM, Esko JD (2005) The sweet and sour of cancer: glycans as novel therapeutic targets. Nat Rev Cancer 5: 526-542. (Pubitemid 40942829)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.7 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 13
    • 79251489778 scopus 로고    scopus 로고
    • Glycomics hits the big time
    • Hart GW, Copeland RJ (2010) Glycomics hits the big time. Cell 143: 672-676.
    • (2010) Cell , vol.143 , pp. 672-676
    • Hart, G.W.1    Copeland, R.J.2
  • 14
    • 84867741847 scopus 로고    scopus 로고
    • Glycosylation effects on cancer development
    • Hakomori SI, Cummings RD (2012) Glycosylation effects on cancer development. Glycoconj J 29: 565-566.
    • (2012) Glycoconj J , vol.29 , pp. 565-566
    • Hakomori, S.I.1    Cummings, R.D.2
  • 15
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in Cellular Mechanisms of Health and Disease
    • DOI 10.1016/j.cell.2006.08.019, PII S0092867406010865
    • Ohtsubo K, Marth JD (2006) Glycosylation in cellular mechanisms of health and disease. Cell 126: 855-867. (Pubitemid 44310784)
    • (2006) Cell , vol.126 , Issue.5 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 18
    • 0347993082 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase V Expression Levels Regulate Cadherin-associated Homotypic Cell-Cell Adhesion and Intracellular Signaling Pathways
    • DOI 10.1074/jbc.M308837200
    • Guo HB, Lee I, Kamar M, Pierce M (2003) N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways. J Biol Chem 278: 52412-52424. (Pubitemid 38035833)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52412-52424
    • Guo, H.-B.1    Lee, I.2    Kamar, M.3    Pierce, M.4
  • 19
    • 67649859659 scopus 로고    scopus 로고
    • The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin
    • Pinho SS, Reis CA, Paredes J, Magalhaes AM, Ferreira AC, et al. (2009) The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin. Hum Mol Genet 18: 2599-2608.
    • (2009) Hum Mol Genet , vol.18 , pp. 2599-2608
    • Pinho, S.S.1    Reis, C.A.2    Paredes, J.3    Magalhaes, A.M.4    Ferreira, A.C.5
  • 20
    • 17144430928 scopus 로고    scopus 로고
    • Beta1,6-branched oligosaccharides are increased in lymph node metastases and predict poor outcome in breast carcinoma
    • DOI 10.1158/1078-0432.CCR-04-2211
    • Handerson T, Camp R, Harigopal M, Rimm D, Pawelek J (2005) Beta1,6-branched oligosaccharides are increased in lymph node metastases and predict poor outcome in breast carcinoma. Clin Cancer Res 11: 2969-2973. (Pubitemid 40525200)
    • (2005) Clinical Cancer Research , vol.11 , Issue.8 , pp. 2969-2973
    • Handerson, T.1    Camp, R.2    Harigopal, M.3    Rimm, D.4    Pawelek, J.5
  • 21
    • 0035526267 scopus 로고    scopus 로고
    • Sialyltransferases in cancer
    • DOI 10.1023/A:1022288022969
    • Dall'Olio F, Chiricolo M (2001) Sialyltransferases in cancer. Glycoconj J 18: 841-850. (Pubitemid 36315048)
    • (2001) Glycoconjugate Journal , vol.18 , Issue.11-12 , pp. 841-850
    • Dall'Olio, F.1    Chiricolo, M.2
  • 22
    • 34547929295 scopus 로고    scopus 로고
    • Diversity in cell surface sialic acid presentations: Implications for biology and disease
    • DOI 10.1038/labinvest.3700656, PII 3700656
    • Varki NM, Varki A (2007) Diversity in cell surface sialic acid presentations: implications for biology and disease. Lab Invest 87: 851-857. (Pubitemid 47267816)
    • (2007) Laboratory Investigation , vol.87 , Issue.9 , pp. 851-857
    • Varki, N.M.1    Varki, A.2
  • 23
    • 84867965064 scopus 로고    scopus 로고
    • Regulation of the metastatic cell phenotype by sialylated glycans
    • Schultz MJ, Swindall AF, Bellis SL (2012) Regulation of the metastatic cell phenotype by sialylated glycans. Cancer Metastasis Rev 31: 501-518.
    • (2012) Cancer Metastasis Rev , vol.31 , pp. 501-518
    • Schultz, M.J.1    Swindall, A.F.2    Bellis, S.L.3
  • 24
    • 0036351383 scopus 로고    scopus 로고
    • Cell surface alpha2,6-sialylation affects adhesion of breast carcinoma cells
    • DOI 10.1006/excr.2002.5521
    • Lin S, Kemmner W, Grigull S, Schlag PM (2002) Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells. Exp Cell Res 276: 101-110. (Pubitemid 34948355)
    • (2002) Experimental Cell Research , vol.276 , Issue.1 , pp. 101-110
    • Lin, S.1    Kemmner, W.2    Grigull, S.3    Schlag, P.M.4
  • 25
    • 19644364143 scopus 로고    scopus 로고
    • Hypersialylation of beta1 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility
    • Seales EC, Jurado GA, Brunson BA, Wakefield JK, Frost AR, et al. (2005) Hypersialylation of beta1 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility. Cancer Res 65: 4645-4652.
    • (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
  • 26
    • 67349087158 scopus 로고    scopus 로고
    • ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by altering integrin glycosylation and function
    • t
    • Christie DR, Shaikh FM, Lucas JAt, Lucas JA 3rd, Bellis SL (2008) ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by altering integrin glycosylation and function. J Ovarian Res 1: 3.
    • (2008) J Ovarian Res , vol.1 , pp. 3
    • Christie, D.R.1    Shaikh, F.M.2    Lucas, J.A.3    Lucas III, J.A.4    Bellis, S.L.5
  • 28
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: Their functions and target proteins
    • Takahashi M, Kuroki Y, Ohtsubo K, Taniguchi N (2009) Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydr Res 344: 1387-1390.
    • (2009) Carbohydr Res , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Taniguchi, N.4
  • 29
    • 61849083675 scopus 로고    scopus 로고
    • A mutual regulation between cell-cell adhesion and N-glycosylation: Implication of the bisecting GlcNAc for biological functions
    • Gu J, Sato Y, Kariya Y, Isaji T, Taniguchi N, et al. (2009) A mutual regulation between cell-cell adhesion and N-glycosylation: implication of the bisecting GlcNAc for biological functions. J Proteome Res 8: 431-435.
    • (2009) J Proteome Res , vol.8 , pp. 431-435
    • Gu, J.1    Sato, Y.2    Kariya, Y.3    Isaji, T.4    Taniguchi, N.5
  • 32
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression
    • Song Y, Aglipay JA, Bernstein JD, Goswami S, Stanley P (2010) The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression. Cancer Res 70: 3361-3371.
    • (2010) Cancer Res , vol.70 , pp. 3361-3371
    • Song, Y.1    Aglipay, J.A.2    Bernstein, J.D.3    Goswami, S.4    Stanley, P.5
  • 33
    • 84860239658 scopus 로고    scopus 로고
    • Aberrant glycosylation associated with enzymes as cancer biomarkers
    • Meany DL, Chan DW (2011) Aberrant glycosylation associated with enzymes as cancer biomarkers. Clin Proteomics 8: 7.
    • (2011) Clin Proteomics , vol.8 , pp. 7
    • Meany, D.L.1    Chan, D.W.2
  • 34
    • 81155132135 scopus 로고    scopus 로고
    • Glycomic analysis of ovarian cancer: Past, present, and future
    • Abbott KL (2010) Glycomic analysis of ovarian cancer: past, present, and future. Cancer Biomark 8: 273-280.
    • (2010) Cancer Biomark , vol.8 , pp. 273-280
    • Abbott, K.L.1
  • 35
    • 33750998782 scopus 로고    scopus 로고
    • Mesothelin-MUC16 binding is a high affinity, N-glycan dependent interaction that facilitates peritoneal metastasis of ovarian tumors
    • Gubbels JA, Belisle J, Onda M, Rancourt C, Migneault M, et al. (2006) Mesothelin-MUC16 binding is a high affinity, N-glycan dependent interaction that facilitates peritoneal metastasis of ovarian tumors. Mol Cancer 5: 50.
    • (2006) Mol Cancer , vol.5 , pp. 50
    • Gubbels, J.A.1    Belisle, J.2    Onda, M.3    Rancourt, C.4    Migneault, M.5
  • 37
    • 70349159332 scopus 로고    scopus 로고
    • The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays
    • Yue T, Goldstein IJ, Hollingsworth MA, Kaul K, Brand RE, et al. (2009) The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays. Mol Cell Proteomics 8: 1697-1707.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1697-1707
    • Yue, T.1    Goldstein, I.J.2    Hollingsworth, M.A.3    Kaul, K.4    Brand, R.E.5
  • 39
    • 84878655670 scopus 로고    scopus 로고
    • Quantitative analysis of glycoprotein glycans
    • Orlando R (2013) Quantitative analysis of glycoprotein glycans. Methods Mol Biol 951: 197-215.
    • (2013) Methods Mol Biol , vol.951 , pp. 197-215
    • Orlando, R.1
  • 41
    • 68549133585 scopus 로고    scopus 로고
    • IDAWG: Metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells
    • Orlando R, Lim JM, Atwood JA 3rd, Angel PM, Fang M, et al. (2009) IDAWG: Metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells. J Proteome Res 8: 3816-3823.
    • (2009) J Proteome Res , vol.8 , pp. 3816-3823
    • Orlando, R.1    Lim, J.M.2    Atwood III, J.A.3    Angel, P.M.4    Fang, M.5
  • 42
    • 84892665025 scopus 로고    scopus 로고
    • Quantitative Glycomics of Cultured Cells Using Isotopic Detection of Aminosugars with Glutamine (IDAWG)
    • Fang M, Lim JM, Wells L (2010) Quantitative Glycomics of Cultured Cells Using Isotopic Detection of Aminosugars with Glutamine (IDAWG). Curr Protoc Chem Biol 2: 55-69.
    • (2010) Curr Protoc Chem Biol , vol.2 , pp. 55-69
    • Fang, M.1    Lim, J.M.2    Wells, L.3
  • 43
    • 79959229101 scopus 로고    scopus 로고
    • Endoglycosidase-mediated incorporation of 18O into glycans for relative glycan quantitation
    • Zhang W, Wang H, Tang H, Yang P (2011) Endoglycosidase-mediated incorporation of 18O into glycans for relative glycan quantitation. Anal Chem 83: 4975-4981.
    • (2011) Anal Chem , vol.83 , pp. 4975-4981
    • Zhang, W.1    Wang, H.2    Tang, H.3    Yang, P.4
  • 44
    • 84865802104 scopus 로고    scopus 로고
    • Site-specific N-glycosylation identification of recombinant human lectin-like oxidized low density lipoprotein receptor-1 (LOX-1)
    • Qian Y, Zhang X, Zhou L, Yun X, Xie J, et al. (2012) Site-specific N-glycosylation identification of recombinant human lectin-like oxidized low density lipoprotein receptor-1 (LOX-1). Glycoconj J 29: 399-409.
    • (2012) Glycoconj J , vol.29 , pp. 399-409
    • Qian, Y.1    Zhang, X.2    Zhou, L.3    Yun, X.4    Xie, J.5
  • 46
    • 79551697660 scopus 로고    scopus 로고
    • N-Glycosylation of total cellular glycoproteins from the human ovarian carcinoma SKOV3 cell line and of recombinantly expressed human erythropoietin
    • Machado E, Kandzia S, Carilho R, Altevogt P, Conradt HS, et al. (2011) N-Glycosylation of total cellular glycoproteins from the human ovarian carcinoma SKOV3 cell line and of recombinantly expressed human erythropoietin. Glycobiology 21: 376-386.
    • (2011) Glycobiology , vol.21 , pp. 376-386
    • Machado, E.1    Kandzia, S.2    Carilho, R.3    Altevogt, P.4    Conradt, H.S.5
  • 47
    • 84859560597 scopus 로고    scopus 로고
    • N-linked glycan structures and their expressions change in the blood sera of ovarian cancer patients
    • Alley WR Jr, Vasseur JA, Goetz JA, Svoboda M, Mann BF, et al. (2012) N-linked glycan structures and their expressions change in the blood sera of ovarian cancer patients. J Proteome Res 11: 2282-2300.
    • (2012) J Proteome Res , vol.11 , pp. 2282-2300
    • Alley Jr., W.R.1    Vasseur, J.A.2    Goetz, J.A.3    Svoboda, M.4    Mann, B.F.5
  • 48
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans
    • Ceroni A, Maass K, Geyer H, Geyer R, Dell A, et al. (2008) GlycoWorkbench: a tool for the computer-assisted annotation of mass spectra of glycans. J Proteome Res 7: 1650-1659.
    • (2008) J Proteome Res , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5
  • 50
    • 84855470323 scopus 로고    scopus 로고
    • Trihydrophobin 1 phosphorylation by c-Src regulates MAPK/ERK signaling and cell migration
    • Wu W, Sun Z, Wu J, Peng X, Gan H, et al. (2012) Trihydrophobin 1 phosphorylation by c-Src regulates MAPK/ERK signaling and cell migration. PLoS One 7: e29920.
    • (2012) PLoS One , vol.7
    • Wu, W.1    Sun, Z.2    Wu, J.3    Peng, X.4    Gan, H.5
  • 51
    • 84255200363 scopus 로고    scopus 로고
    • Hepatitis B virus large surface antigen promotes liver carcinogenesis by activating the Src/PI3K/Akt pathway
    • Liu H, Xu J, Zhou L, Yun X, Chen L, et al. (2011) Hepatitis B virus large surface antigen promotes liver carcinogenesis by activating the Src/PI3K/Akt pathway. Cancer Res 71: 7547-7557.
    • (2011) Cancer Res , vol.71 , pp. 7547-7557
    • Liu, H.1    Xu, J.2    Zhou, L.3    Yun, X.4    Chen, L.5
  • 52
    • 84867745540 scopus 로고    scopus 로고
    • The bisecting GlcNAc in cell growth control and tumor progression
    • Miwa HE, Song Y, Alvarez R, Cummings RD, Stanley P (2012) The bisecting GlcNAc in cell growth control and tumor progression. Glycoconj J 29: 609-618.
    • (2012) Glycoconj J , vol.29 , pp. 609-618
    • Miwa, H.E.1    Song, Y.2    Alvarez, R.3    Cummings, R.D.4    Stanley, P.5
  • 53
    • 0027409399 scopus 로고
    • Enhanced c-erbB-2/neu expression in human ovarian cancer cells correlates with more severe malignancy that can be suppressed by E1A
    • Yu D, Wolf JK, Scanlon M, Price JE, Hung MC (1993) Enhanced c-erbB-2/neu expression in human ovarian cancer cells correlates with more severe malignancy that can be suppressed by E1A. Cancer Res 53: 891-898. (Pubitemid 23077880)
    • (1993) Cancer Research , vol.53 , Issue.4 , pp. 891-898
    • Yu, D.1    Wolf, J.K.2    Scanlon, M.3    Price, J.E.4    Hung, M.-C.5
  • 55
    • 84871860708 scopus 로고    scopus 로고
    • Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples
    • Boersema PJ, Geiger T, Wisniewski JR, Mann M (2013) Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples. Mol Cell Proteomics 12: 158-171.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 158-171
    • Boersema, P.J.1    Geiger, T.2    Wisniewski, J.R.3    Mann, M.4
  • 56
    • 79951518985 scopus 로고    scopus 로고
    • Mining the plasma proteome for disease applications across seven logs of protein abundance
    • Zhang Q, Faca V, Hanash S (2011) Mining the plasma proteome for disease applications across seven logs of protein abundance. J Proteome Res 10: 46-50.
    • (2011) J Proteome Res , vol.10 , pp. 46-50
    • Zhang, Q.1    Faca, V.2    Hanash, S.3
  • 57
    • 77952909304 scopus 로고    scopus 로고
    • Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas
    • Wu CC, Hsu CW, Chen CD, Yu CJ, Chang KP, et al. (2010) Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas. Mol Cell Proteomics 9: 1100-1117.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1100-1117
    • Wu, C.C.1    Hsu, C.W.2    Chen, C.D.3    Yu, C.J.4    Chang, K.P.5
  • 58
    • 79551493048 scopus 로고    scopus 로고
    • Conditioned media from cell lines: A complementary model to clinical specimens for the discovery of disease-specific biomarkers
    • Dowling P, Clynes M (2011) Conditioned media from cell lines: a complementary model to clinical specimens for the discovery of disease-specific biomarkers. Proteomics 11: 794-804.
    • (2011) Proteomics , vol.11 , pp. 794-804
    • Dowling, P.1    Clynes, M.2
  • 59
    • 78349311747 scopus 로고    scopus 로고
    • Cancer secretomics reveal pathophysiological pathways in cancer molecular oncology
    • Karagiannis GS, Pavlou MP, Diamandis EP (2010) Cancer secretomics reveal pathophysiological pathways in cancer molecular oncology. Mol Oncol 4: 496-510.
    • (2010) Mol Oncol , vol.4 , pp. 496-510
    • Karagiannis, G.S.1    Pavlou, M.P.2    Diamandis, E.P.3
  • 60
    • 77957755656 scopus 로고    scopus 로고
    • Secretome proteomics for discovery of cancer biomarkers
    • Makridakis M, Vlahou A (2010) Secretome proteomics for discovery of cancer biomarkers. J Proteomics 73: 2291-2305.
    • (2010) J Proteomics , vol.73 , pp. 2291-2305
    • Makridakis, M.1    Vlahou, A.2
  • 61
    • 77956419405 scopus 로고    scopus 로고
    • The cancer cell secretome: A good source for discovering biomarkers?
    • Pavlou MP, Diamandis EP (2010) The cancer cell secretome: a good source for discovering biomarkers? J Proteomics 73: 1896-1906.
    • (2010) J Proteomics , vol.73 , pp. 1896-1906
    • Pavlou, M.P.1    Diamandis, E.P.2
  • 62
    • 84875204783 scopus 로고    scopus 로고
    • Comparative glycomic profiling of isotopically permethylated N-glycans by liquid chromatography/electrospray ionization mass spectrometry
    • Hu Y, Desantos-Garcia JL, Mechref Y (2013) Comparative glycomic profiling of isotopically permethylated N-glycans by liquid chromatography/electrospray ionization mass spectrometry. Rapid Commun Mass Spectrom 27: 865-877.
    • (2013) Rapid Commun Mass Spectrom , vol.27 , pp. 865-877
    • Hu, Y.1    Desantos-Garcia, J.L.2    Mechref, Y.3
  • 63
    • 0033135747 scopus 로고    scopus 로고
    • Protein glycosylation in development and disease
    • DOI 10.1002/(SICI)1521-1878(199905)21:5<412::AID-B
    • Dennis JW, Granovsky M, Warren CE (1999) Protein glycosylation in development and disease. Bioessays 21: 412-421. (Pubitemid 29223313)
    • (1999) BioEssays , vol.21 , Issue.5 , pp. 412-421
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 64
    • 84872304068 scopus 로고    scopus 로고
    • Glycogenes mediate the invasive properties and chemosensitivity of human hepatocarcinoma cells
    • Guo R, Cheng L, Zhao Y, Zhang J, Liu C, et al. (2013) Glycogenes mediate the invasive properties and chemosensitivity of human hepatocarcinoma cells. Int J Biochem Cell Biol 45: 347-358.
    • (2013) Int J Biochem Cell Biol , vol.45 , pp. 347-358
    • Guo, R.1    Cheng, L.2    Zhao, Y.3    Zhang, J.4    Liu, C.5
  • 65
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection
    • Yoshimura M, Nishikawa A, Ihara Y, Taniguchi S, Taniguchi N (1995) Suppression of lung metastasis of B16 mouse melanoma by N- acetylglucosaminyltransferase III gene transfection. Proc Natl Acad Sci U S A 92: 8754-8758.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8754-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Taniguchi, S.4    Taniguchi, N.5
  • 66
    • 84862919698 scopus 로고    scopus 로고
    • Glycan-related gene expression signatures in human metastatic hepatocellular carcinoma cells
    • Kang X, Wang N, Pei C, Sun L, Sun R, et al. (2012) Glycan-related gene expression signatures in human metastatic hepatocellular carcinoma cells. Exp Ther Med 3: 415-422.
    • (2012) Exp Ther Med , vol.3 , pp. 415-422
    • Kang, X.1    Wang, N.2    Pei, C.3    Sun, L.4    Sun, R.5
  • 67
    • 0035853845 scopus 로고    scopus 로고
    • Overexpression of N-acetylglucosaminyltransferase III enhances the epidermal growth factor-induced phosphorylation of ERK in HeLaS3 cells by upregulation of the internalization rate of the receptors
    • Sato Y, Takahashi M, Shibukawa Y, Jain SK, Hamaoka R, et al. (2001) Overexpression of N-acetylglucosaminyltransferase III enhances the epidermal growth factor-induced phosphorylation of ERK in HeLaS3 cells by upregulation of the internalization rate of the receptors. J Biol Chem 276: 11956-11962.
    • (2001) J Biol Chem , vol.276 , pp. 11956-11962
    • Sato, Y.1    Takahashi, M.2    Shibukawa, Y.3    Jain, S.K.4    Hamaoka, R.5
  • 69
    • 76649133774 scopus 로고    scopus 로고
    • Identification of candidate biomarkers with cancer-specific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis
    • Abbott KL, Lim JM, Wells L, Benigno BB, McDonald JF, et al. (2010) Identification of candidate biomarkers with cancer-specific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis. Proteomics 10: 470-481.
    • (2010) Proteomics , vol.10 , pp. 470-481
    • Abbott, K.L.1    Lim, J.M.2    Wells, L.3    Benigno, B.B.4    McDonald, J.F.5
  • 70
    • 77957946398 scopus 로고    scopus 로고
    • ARID1A mutations in endometriosis-associated ovarian carcinomas
    • Wiegand KC, Shah SP, Al-Agha OM, Zhao Y, Tse K, et al. (2010) ARID1A mutations in endometriosis-associated ovarian carcinomas. N Engl J Med 363: 1532-1543.
    • (2010) N Engl J Med , vol.363 , pp. 1532-1543
    • Wiegand, K.C.1    Shah, S.P.2    Al-Agha, O.M.3    Zhao, Y.4    Tse, K.5
  • 71
    • 0027196125 scopus 로고
    • Purification and Characterization of UDP-N-Acetylglucosamine: alpha-6-D-Mannoside beta1-6-N-Acetylglucosaminyltransferase (N- Acetylglucosaminetransferase V) from a Human Lung Cancer Cell Line
    • Gu J, Nishikawa A, Tsuruoka N, Ohno M, Yamaguchi N, et al. (1993) Purification and characterization of UDP-N-acetylglucosamine: alpha-6-D-mannoside beta 1-6N-acetylglucosaminyltransferase (N- acetylglucosaminyltransferase V) from a human lung cancer cell line. J Biochem 113: 614-619. (Pubitemid 23166993)
    • (1993) Journal of Biochemistry , vol.113 , Issue.5 , pp. 614-619
    • Gu, J.1    Nishikawa, A.2    Tsuruoka, N.3    Ohno, M.4    Yamaguchi, N.5    Kangawa, K.6    Taniguchi, N.7
  • 72
    • 0022960932 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • Schachter H (1986) Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Adv Exp Med Biol 205: 53-85.
    • (1986) Adv Exp Med Biol , vol.205 , pp. 53-85
    • Schachter, H.1
  • 73
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • DOI 10.1074/jbc.271.23.13811
    • Yoshimura M, Ihara Y, Matsuzawa Y, Taniguchi N (1996) Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis. J Biol Chem 271: 13811-13815. (Pubitemid 26185425)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.23 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4
  • 74
    • 0030983084 scopus 로고    scopus 로고
    • Gene transfection-mediated overexpression of beta1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function
    • DOI 10.1074/jbc.272.14.9275
    • Rebbaa A, Yamamoto H, Saito T, Meuillet E, Kim P, et al. (1997) Gene transfection-mediated overexpression of beta1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function. J Biol Chem 272: 9275-9279. (Pubitemid 27154938)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9275-9279
    • Rebbaa, A.1    Yamamoto, H.2    Saito, T.3    Meuillet, E.4    Kim, P.5    Kersey, D.S.6    Bremer, E.G.7    Taniguchi, N.8    Moskal, J.R.9
  • 75
    • 5144224424 scopus 로고    scopus 로고
    • Beta1,4-N-Acetylglucosaminyltransferase III down-regulates neurite outgrowth induced by costimulation of epidermal growth factor and integrins through the Ras/ERK signaling pathway in PC12 cells
    • DOI 10.1093/glycob/cwh016
    • Gu J, Zhao Y, Isaji T, Shibukawa Y, Ihara H, et al. (2004) Beta1,4-N-Acetylglucosaminyltransferase III down-regulates neurite outgrowth induced by costimulation of epidermal growth factor and integrins through the Ras/ERK signaling pathway in PC12 cells. Glycobiology 14: 177-186. (Pubitemid 38263102)
    • (2004) Glycobiology , vol.14 , Issue.2 , pp. 177-186
    • Gu, J.1    Zhao, Y.2    Isaji, T.3    Shibukawa, Y.4    Ihara, H.5    Takahashi, M.6    Ikeda, Y.7    Miyoshi, E.8    Honke, K.9    Taniguchi, N.10
  • 76
    • 77949325755 scopus 로고    scopus 로고
    • Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity
    • North SJ, Huang HH, Sundaram S, Jang-Lee J, Etienne AT, et al. (2010) Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J Biol Chem 285: 5759-5775.
    • (2010) J Biol Chem , vol.285 , pp. 5759-5775
    • North, S.J.1    Huang, H.H.2    Sundaram, S.3    Jang-Lee, J.4    Etienne, A.T.5
  • 77
    • 70350685770 scopus 로고    scopus 로고
    • Adaptive regulation at the cell surface by N-glycosylation
    • Dennis JW, Lau KS, Demetriou M, Nabi IR (2009) Adaptive regulation at the cell surface by N-glycosylation. Traffic 10: 1569-1578.
    • (2009) Traffic , vol.10 , pp. 1569-1578
    • Dennis, J.W.1    Lau, K.S.2    Demetriou, M.3    Nabi, I.R.4
  • 80
    • 3042783981 scopus 로고    scopus 로고
    • In search of the carbohydrate structures on CD44 critical for hyaluronic acid binding - Roles of sialylation and sulfation
    • Kannagi R, Goto Y, Fukui F (2004) In search of the carbohydrate structures on CD44 critical for hyaluronic acid binding - Roles of sialylation and sulfation. Trends in Glycoscience and Glycotechnology 16: 211-23. (Pubitemid 38850600)
    • (2004) Trends in Glycoscience and Glycotechnology , vol.16 , Issue.89 , pp. 211-223
    • Kannagi, R.1    Goto, Y.2    Fukui, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.