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Volumn 11, Issue 7, 2012, Pages

Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; ASPARAGINE; GLYCAN; GLYCOPROTEIN; LECTIN; MANNOSE; TRIACYLGLYCEROL; AMINOSUGAR; FUCOSE; LECTIN, ALEURIA AURANTIA; POLYSACCHARIDE; TRIACYLGLYCEROL LIPASE;

EID: 84863794084     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.015792     Document Type: Article
Times cited : (47)

References (49)
  • 1
    • 77956341116 scopus 로고    scopus 로고
    • Prevalence of incidental pancreatic cysts in the adult population on MR imaging
    • Lee, K. S., Sekhar, A., Rofsky, N. M., and Pedrosa, I. (2010) Prevalence of incidental pancreatic cysts in the adult population on MR imaging. Am. J. Gastroenterol. 105, 2079-2084
    • (2010) Am. J. Gastroenterol. , vol.105 , pp. 2079-2084
    • Lee, K.S.1    Sekhar, A.2    Rofsky, N.M.3    Pedrosa, I.4
  • 2
    • 0029925475 scopus 로고    scopus 로고
    • Clinical assessment compared with cyst fluid analysis in the differential diagnosis of cystic lesions in the pancreas
    • DOI 10.1016/S0039-6060(96)80113-9
    • Sand, J. A., Hyoty, M. K., Mattila, J., Dagorn, J. C., and Nordback, I. H. (1996) Clinical assessment compared with cyst fluid analysis in the differential diagnosis of cystic lesions in the pancreas. Surgery 119, 275-280 (Pubitemid 26082662)
    • (1996) Surgery , vol.119 , Issue.3 , pp. 275-280
    • Sand, J.A.1    Hyoty, M.K.2    Mattila, J.3    Dagorn, J.-C.4    Nordback, I.H.5
  • 7
    • 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, I. J., Hollingsworth, M. A., Kaul, K., Brand, R. E., and Haab, B. B. (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    Haab, B.B.6
  • 8
    • 34249341648 scopus 로고    scopus 로고
    • Glycoprotein microarrays with multi-lectin detection: Unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera
    • DOI 10.1021/pr070062p
    • Zhao, J., Patwa, T. H., Qiu, W., Shedden, K., Hinderer, R., Misek, D. E., Anderson, M. A., Simeone, D. M., and Lubman, D. M. (2007) Glycoprotein microarrays with multi-lectin detection: Unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera. J. Proteome Res. 6, 1864-1874 (Pubitemid 46814510)
    • (2007) Journal of Proteome Research , vol.6 , Issue.5 , pp. 1864-1874
    • Zhao, J.1    Patwa, T.H.2    Qiu, W.3    Shedden, K.4    Hinderer, R.5    Misek, D.E.6    Anderson, M.A.7    Simeone, D.M.8    Lubman, D.M.9
  • 9
  • 10
    • 34447333697 scopus 로고    scopus 로고
    • Classification of pancreatic cystic lesions using SELDI-TOF mass spectrometry
    • DOI 10.1111/j.1445-2197.2007.04179.x
    • Scarlett, C. J., Samra, J. S., Xue, A., Baxter, R. C., and Smith, R. C. (2007) Classification of pancreatic cystic lesions using SELDI-TOF mass spectrometry. ANZ J. Surg. 77, 648-653 (Pubitemid 47063352)
    • (2007) ANZ Journal of Surgery , vol.77 , Issue.8 , pp. 648-653
    • Scarlett, C.J.1    Samra, J.S.2    Xue, A.3    Baxter, R.C.4    Smith, R.C.5
  • 13
    • 46349088505 scopus 로고    scopus 로고
    • Biological function of fucosylation in cancer biology
    • DOI 10.1093/jb/mvn011
    • Miyoshi, E., Moriwaki, K., and Nakagawa, T. (2008) Biological function of fucosylation in cancer biology. J. Biochem. 143, 725-729 (Pubitemid 351918934)
    • (2008) Journal of Biochemistry , vol.143 , Issue.6 , pp. 725-729
    • Miyoshi, E.1    Moriwaki, K.2    Nakagawa, T.3
  • 14
    • 77957750584 scopus 로고    scopus 로고
    • A sensitive assay to measure biomarker glycosylation demonstrates increased fucosylation of prostate specific antigen (PSA) in patients with prostate cancer compared with benign prostatic hyperplasia
    • Dwek, M. V., Jenks, A., and Leathem, A. J. (2010) A sensitive assay to measure biomarker glycosylation demonstrates increased fucosylation of prostate specific antigen (PSA) in patients with prostate cancer compared with benign prostatic hyperplasia. Clin. Chim. Acta 411, 1935-1939
    • (2010) Clin. Chim. Acta , vol.411 , pp. 1935-1939
    • Dwek, M.V.1    Jenks, A.2    Leathem, A.J.3
  • 15
    • 48249114327 scopus 로고    scopus 로고
    • Serum fucosylation changes in oral cancer and oral precancerous conditions: α-L-Fucosidase as a marker
    • Shah, M., Telang, S., Raval, G., Shah, P., and Patel, P. S. (2008) Serum fucosylation changes in oral cancer and oral precancerous conditions: α-L-Fucosidase as a marker. Cancer 113, 336-346
    • (2008) Cancer , vol.113 , pp. 336-346
    • Shah, M.1    Telang, S.2    Raval, G.3    Shah, P.4    Patel, P.S.5
  • 18
    • 28044433453 scopus 로고    scopus 로고
    • Solid-phase permethylation of glycans for mass spectrometric analysis
    • DOI 10.1002/rcm.2210
    • Kang, P., Mechref, Y., Klouckova, I., and Novotny, M. V. (2005) Solid-phase permethylation of glycans for mass spectrometric analysis. Rapid Commun. Mass Spectrom. 19, 3421-3428 (Pubitemid 41691916)
    • (2005) Rapid Communications in Mass Spectrometry , vol.19 , Issue.23 , pp. 3421-3428
    • Kang, P.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 19
    • 77953555196 scopus 로고    scopus 로고
    • Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: A potential methodology for cancer-biomarker discovery
    • Alley, W. R., Jr., Madera, M., Mechref, Y., and Novotny, M. V. (2010) Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: A potential methodology for cancer-biomarker discovery. Anal. Chem. 82, 5095-5106
    • (2010) Anal. Chem. , vol.82 , pp. 5095-5106
    • Alley Jr., W.R.1    Madera, M.2    Mechref, Y.3    Novotny, M.V.4
  • 20
    • 60149092781 scopus 로고    scopus 로고
    • ProteinQuant Suite: A bundle of automated software tools for label-free quantitative proteomics
    • Mann, B., Madera, M., Sheng, Q., Tang, H., Mechref, Y., and Novotny, M. V. (2008) ProteinQuant Suite: A bundle of automated software tools for label-free quantitative proteomics. Rapid Commun. Mass Spectrom. 22, 3823-3834
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 3823-3834
    • Mann, B.1    Madera, M.2    Sheng, Q.3    Tang, H.4    Mechref, Y.5    Novotny, M.V.6
  • 21
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • DOI 10.1038/nmeth1019, PII NMETH1019
    • Elias, J. E., and Gygi, S. P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4, 207-214 (Pubitemid 46358868)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 22
    • 70349479239 scopus 로고    scopus 로고
    • Serine protease inhibitor Kazal type 1 promotes proliferation of pancreatic cancer cells through the epidermal growth factor receptor
    • Ozaki, N., Ohmuraya, M., Hirota, M., Ida, S., Wang, J., Takamori, H., Higashiyama, S., Baba, H., and Yamamura, K. (2009) Serine protease inhibitor Kazal type 1 promotes proliferation of pancreatic cancer cells through the epidermal growth factor receptor. Mol. Cancer Res. 7, 1572-1581
    • (2009) Mol. Cancer Res. , vol.7 , pp. 1572-1581
    • Ozaki, N.1    Ohmuraya, M.2    Hirota, M.3    Ida, S.4    Wang, J.5    Takamori, H.6    Higashiyama, S.7    Baba, H.8    Yamamura, K.9
  • 23
    • 0023858353 scopus 로고
    • Structure elucidation of glycosphingolipids and gangliosides using high-performance tandem mass spectrometry
    • Domon, B., and Costello, C. E. (1988) Structure elucidation of glycosphingolipids and gangliosides using high-performance tandem mass spectrometry. Biochemistry 27, 1534-1543 (Pubitemid 18077449)
    • (1988) Biochemistry , vol.27 , Issue.5 , pp. 1534-1543
    • Domon, B.1    Costello, C.E.2
  • 25
    • 73249116888 scopus 로고    scopus 로고
    • Software tool for researching annotations of proteins: Open-source protein annotation software with data visualization
    • Bhatia, V. N., Perlman, D. H., Costello, C. E., and McComb, M. E. (2009) Software tool for researching annotations of proteins: Open-source protein annotation software with data visualization. Anal. Chem. 81, 9819-9823
    • (2009) Anal. Chem. , vol.81 , pp. 9819-9823
    • Bhatia, V.N.1    Perlman, D.H.2    Costello, C.E.3    McComb, M.E.4
  • 26
    • 1642580509 scopus 로고    scopus 로고
    • Suppression of β1,3galactosyltransferase β3Gal-T5 in cancer cells reduces sialyl-Lewis a and enhances poly N-acetyllactosamines and sialyl-Lewis x on O-glycans
    • DOI 10.1046/j.1432-1033.2003.03919.x
    • Mare, L., and Trinchera, M. (2004) Suppression of β-1, 3galactosyltransferase β3Gal-T5 in cancer cells reduces sialyl-Lewis a and enhances poly N-acetyllactosamines and sialyl-Lewis x on O-glycans. Eur. J. Biochem. 271, 186-194 (Pubitemid 38122177)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.1 , pp. 186-194
    • Mare, L.1    Trinchera, M.2
  • 27
    • 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., Ueda, T., Nakahashi, C., Ochiai, T., and Ochiai, A. (2001) 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 69, 127-135 (Pubitemid 34212083)
    • (2001) Pathobiology , vol.69 , Issue.3 , pp. 127-135
    • Takahashi, S.1    Oda, T.2    Hasebe, T.3    Sasaki, S.4    Kinoshita, T.5    Konishi, M.6    Ueda, T.7    Nakahashi, C.8    Ochiai, T.9    Ochiai, A.10
  • 29
    • 78651400829 scopus 로고    scopus 로고
    • Clinical value of serum neopterin, tissue polypeptide-specific antigen and CA19-9 levels in differential diagnosis between pancreatic cancer and chronic pancreatitis
    • Talar-Wojnarowska, R., Gasiorowska, A., Olakowski, M., Lekstan, A., Lampe, P., and Malecka-Panas, E. (2010) Clinical value of serum neopterin, tissue polypeptide-specific antigen and CA19-9 levels in differential diagnosis between pancreatic cancer and chronic pancreatitis. Pancreatology 10, 689-694
    • (2010) Pancreatology , vol.10 , pp. 689-694
    • Talar-Wojnarowska, R.1    Gasiorowska, A.2    Olakowski, M.3    Lekstan, A.4    Lampe, P.5    Malecka-Panas, E.6
  • 30
    • 0034062142 scopus 로고    scopus 로고
    • The usefulness of serial changes in serum CA19-9 levels in the diagnosis of pancreatic cancer
    • DOI 10.1097/00006676-200005000-00007
    • Tanaka, N., Okada, S., Ueno, H., Okusaka, T., and Ikeda, M. (2000) The usefulness of serial changes in serum CA19-9 levels in the diagnosis of pancreatic cancer. Pancreas 20, 378-381 (Pubitemid 30253650)
    • (2000) Pancreas , vol.20 , Issue.4 , pp. 378-381
    • Tanaka, N.1    Okada, S.2    Ueno, H.3    Okusaka, T.4    Ikeda, M.5
  • 31
    • 0030745388 scopus 로고    scopus 로고
    • Preoperative differential diagnosis of benign and malignant pancreatic lesions - The value of pancreatic secretory trypsin inhibitor, Procarboxypeptidase B, CA19-9 and CEA
    • Cerwenka, H., Aigner, R., Quehenberger, F., Werkgartner, G., Bacher, H., Hauser, H., and Mischinger, H. J. (1997) Preoperative differential diagnosis of benign and malignant pancreatic lesions: The value of pancreatic secretory trypsin inhibitor, procarboxypeptidase B, CA19-9 and CEA. Hepatogastroenterology 44, 1117-1121 (Pubitemid 27326168)
    • (1997) Hepato-Gastroenterology , vol.44 , Issue.16 , pp. 1117-1121
    • Cerwenka, H.1    Aigner, R.2    Quehenberger, F.3    Werkgartner, G.4    Bacher, H.5    Hauser, H.6    Mischinger, H..7
  • 32
    • 48849090158 scopus 로고    scopus 로고
    • Prognosis of resected ampullary adenocarcinoma by preoperative serum CA19-9 levels and platelet-lymphocyte ratio
    • Smith, R. A., Ghaneh, P., Sutton, R., Raraty, M., Campbell, F., and Neoptolemos, J. P. (2008) Prognosis of resected ampullary adenocarcinoma by preoperative serum CA19-9 levels and platelet-lymphocyte ratio. J. Gastrointest. Surg. 12, 1422-1428
    • (2008) J. Gastrointest. Surg. , vol.12 , pp. 1422-1428
    • Smith, R.A.1    Ghaneh, P.2    Sutton, R.3    Raraty, M.4    Campbell, F.5    Neoptolemos, J.P.6
  • 33
    • 27144435114 scopus 로고    scopus 로고
    • CA19-9 as a prognostic factor in inoperable pancreatic cancer: The implication for clinical trials
    • DOI 10.1038/sj.bjc.6602760, PII 6602760
    • Maisey, N. R., Norman, A. R., Hill, A., Massey, A., Oates, J., and Cunningham, D. (2005) CA19-9 as a prognostic factor in inoperable pancreatic cancer: The implication for clinical trials. Br. J. Cancer. 93, 740-743 (Pubitemid 41486431)
    • (2005) British Journal of Cancer , vol.93 , Issue.7 , pp. 740-743
    • Maisey, N.R.1    Norman, A.R.2    Hill, A.3    Massey, A.4    Oates, J.5    Cunningham, D.6
  • 37
    • 23944431914 scopus 로고    scopus 로고
    • Cyst fluid analysis in the differential diagnosis of pancreatic cystic lesions: A pooled analysis
    • van der Waaij, L. A., van Dullemen, H. M., and Porte, R. J. (2005) Cyst fluid analysis in the differential diagnosis of pancreatic cystic lesions: A pooled analysis. Gastrointest. Endosc. 62, 383-389
    • (2005) Gastrointest. Endosc. , vol.62 , pp. 383-389
    • Van Der Waaij, L.A.1    Van Dullemen, H.M.2    Porte, R.J.3
  • 40
    • 0022560022 scopus 로고
    • Quantitiative and qualitative characterization of human cancer-associated serum glycoprotein antigens expressing fucosyl or sialyl-fucosyl type 2 chain polylactosamine
    • Kannagi, R., Fukushi, Y., Tachikawa, T., Noda, A., Shin, S., Shigeta, K., Hiraiwa, N., Fukuda, Y., Inamoto, T., Hakomori, S., and et al. (1986) Quantitative and qualitative characterization of human cancer-associated serum glycoprotein antigens expressing fucosyl or sialyl-fucosyl type 2 chain polylactosamine. Cancer Res. 46, 2619-2626 (Pubitemid 16120742)
    • (1986) Cancer Research , vol.46 , Issue.5 , pp. 2619-2626
    • Kannagi, R.1    Fukushi, Y.2    Tachikawa, T.3
  • 41
    • 0021256064 scopus 로고
    • Novel fucolipids accumulating in human adenocarcinoma. II. Selective isolation of hybridoma antibodies that differentially recognize mono-DI- and trifucosylated type 2 chain
    • Fukushi, Y., Hakomori, S., Nudelman, E., and Cochran, N. (1984) Novel fucolipids accumulating in human adenocarcinoma. II. Selective isolation of hybridoma antibodies that differentially recognize mono-, di-, and trifucosylated type 2 chain. J. Biol. Chem. 259, 4681-4685 (Pubitemid 14131379)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.7 , pp. 4681-4685
    • Fukushi, Y.1    Hakomori, S.2    Nudelman, E.3    Cochran, N.4
  • 45
    • 0025737638 scopus 로고
    • Carbohydrate structure of human pancreatic elastase 1
    • Wendorf, P., Linder, D., Sziegoleit, A., and Geyer, R. (1991) Carbohydrate structure of human pancreatic elastase 1. Biochem. J. 278, 505-514
    • (1991) Biochem. J. , vol.278 , pp. 505-514
    • Wendorf, P.1    Linder, D.2    Sziegoleit, A.3    Geyer, R.4
  • 46
    • 34547437254 scopus 로고    scopus 로고
    • Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: Identity with Rinderknecht's enzyme Y
    • DOI 10.1073/pnas.0703714104
    • Szmola, R., and Sahin-Tóth, M. (2007) Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: Identity with Rinderknecht's enzyme Y. Proc. Natl. Acad. Sci. U.S.A. 104, 11227-11232 (Pubitemid 47175123)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.27 , pp. 11227-11232
    • Szmola, R.1    Sahin-Toth, M.2
  • 47
    • 0025607899 scopus 로고
    • Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: Its hydrolysis and protection by intraluminal factors
    • Freeman, T. C., Davies, R., and Calam, J. (1990) Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: Its hydrolysis and protection by intraluminal factors. Clin. Chim. Acta 195, 27-39
    • (1990) Clin. Chim. Acta , vol.195 , pp. 27-39
    • Freeman, T.C.1    Davies, R.2    Calam, J.3
  • 48
    • 29744456182 scopus 로고    scopus 로고
    • Application of proteomic technology in identifying pancreatic secretory trypsin inhibitor variants in urine of patients with pancreatitis
    • DOI 10.1373/clinchem.2005.056861
    • Valmu, L., Paju, A., Lempinen, M., Kemppainen, E., and Stenman, U. H. (2006) Application of proteomic technology in identifying pancreatic secretory trypsin inhibitor variants in urine of patients with pancreatitis. Clin. Chem. 52, 73-81 (Pubitemid 43032469)
    • (2006) Clinical Chemistry , vol.52 , Issue.1 , pp. 73-81
    • Valmu, L.1    Paju, A.2    Lempinen, M.3    Kemppainen, E.4    Stenman, U.-H.5
  • 49
    • 0036325798 scopus 로고    scopus 로고
    • Tumor-associated trypsin inhibitor
    • Stenman, U. H. (2002) Tumor-associated trypsin inhibitor. Clin. Chem. 48, 1206-1209
    • (2002) Clin. Chem. , vol.48 , pp. 1206-1209
    • Stenman, U.H.1


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