메뉴 건너뛰기




Volumn 9, Issue 8, 2009, Pages 2182-2192

Targeted serum glycoproteomics for the discovery of lung cancer-associated glycosylation disorders using lectin-coupled ProteinChip arrays

Author keywords

Biomarker; Glycoproteomics; Lung cancer; SELDI TOF MS; Sialic acid

Indexed keywords

APOLIPOPROTEIN C3; BETA N ACETYLGALACTOSAMINIDASE; GLYCAN; GLYCOPROTEIN; JACALIN; LECTIN; N ACETYLNEURAMINIC ACID; SIALIDASE;

EID: 65349180162     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800374     Document Type: Article
Times cited : (53)

References (32)
  • 2
    • 14744274613 scopus 로고    scopus 로고
    • Early diagnosis of lung cancer by detection of tumor liberated protein
    • Tarro, G., Perna, A., Esposito, C., Early diagnosis of lung cancer by detection of tumor liberated protein. J. Cell. Physiol. 2005, 203, 1-5.
    • (2005) J. Cell. Physiol , vol.203 , pp. 1-5
    • Tarro, G.1    Perna, A.2    Esposito, C.3
  • 3
    • 33745560074 scopus 로고    scopus 로고
    • The US Food and Drug Administration perspective on cancer biomarker development
    • Gutman, S., Kessler, L. G., The US Food and Drug Administration perspective on cancer biomarker development. Nat. Rev. Cancer 2006, 6, 565-571.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 565-571
    • Gutman, S.1    Kessler, L.G.2
  • 4
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • Bertozzi, C. R., Kiessling, L. L., Chemical glycobiology. Science 2001, 291, 2357-2364.
    • (2001) Science , vol.291 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 6
    • 0942287200 scopus 로고    scopus 로고
    • The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5
    • Gewinner, C., Hart, G., Zachara, N., Cole, R. et al., The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5. J. Biol. Chem. 2004, 279, 3563-3572.
    • (2004) J. Biol. Chem , vol.279 , pp. 3563-3572
    • Gewinner, C.1    Hart, G.2    Zachara, N.3    Cole, R.4
  • 7
    • 16844382710 scopus 로고    scopus 로고
    • Advanced glycation end products enhance expression of proapoptotic genes and stimulate fibroblast apoptosis through cytoplasmic and mitochondrial pathways
    • Alikhani, Z., Alikhani, M., Boyd, C. M., Nagao, K. et al., Advanced glycation end products enhance expression of proapoptotic genes and stimulate fibroblast apoptosis through cytoplasmic and mitochondrial pathways. J. Biol. Chem. 2005, 280, 12087-12095.
    • (2005) J. Biol. Chem , vol.280 , pp. 12087-12095
    • Alikhani, Z.1    Alikhani, M.2    Boyd, C.M.3    Nagao, K.4
  • 8
    • 33746163433 scopus 로고    scopus 로고
    • Remodeling of the lectin-EGF-like domain interface in P- and L-selectin increases adhesiveness and shear resistance under hydrodynamic force
    • Phan, U. T., Waldron, T. T., Springer, T. A., Remodeling of the lectin-EGF-like domain interface in P- and L-selectin increases adhesiveness and shear resistance under hydrodynamic force. Nat. Immunol. 2006, 7, 883-889.
    • (2006) Nat. Immunol , vol.7 , pp. 883-889
    • Phan, U.T.1    Waldron, T.T.2    Springer, T.A.3
  • 9
    • 6044239186 scopus 로고    scopus 로고
    • Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis
    • Partridge, E. A., Le Roy, C., Di Guglielmo, G. M., Pawling, J. et al., Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science 2004, 306, 120-124.
    • (2004) Science , vol.306 , pp. 120-124
    • Partridge, E.A.1    Le Roy, C.2    Di Guglielmo, G.M.3    Pawling, J.4
  • 10
    • 0021572879 scopus 로고
    • Tumor-associated carbohydrate antigens
    • Hakomori, S., Tumor-associated carbohydrate antigens. Annu. Rev. Immunol. 1984, 2, 103-126.
    • (1984) Annu. Rev. Immunol , vol.2 , pp. 103-126
    • Hakomori, S.1
  • 11
    • 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, 2405-2414.
    • (1985) Cancer Res , vol.45 , pp. 2405-2414
    • Hakomori, S.1
  • 12
    • 0020609986 scopus 로고
    • Glycosphingolipids as tumorassociated and differentiation markers
    • Hakomori, S., Kannagi, R., Glycosphingolipids as tumorassociated and differentiation markers. J. Natl. Cancer Inst. 1983, 71, 231-251.
    • (1983) J. Natl. Cancer Inst , vol.71 , pp. 231-251
    • Hakomori, S.1    Kannagi, R.2
  • 13
    • 0035167142 scopus 로고    scopus 로고
    • Biosynthesis of the cancer-related sialyl-7alpha;2,6-lactosaminyl epitope in colon cancer cell lines expressing β-galactoside α2,6-sialyltransferase under a constitutive promoter
    • Dall'Olio, F., Chiricolo, M., Mariani, E., Facchini, A., Biosynthesis of the cancer-related sialyl-7alpha;2,6-lactosaminyl epitope in colon cancer cell lines expressing β-galactoside α2,6-sialyltransferase under a constitutive promoter. Eur. J. Biochem. 2001, 268, 5876-5884.
    • (2001) Eur. J. Biochem , vol.268 , pp. 5876-5884
    • Dall'Olio, F.1    Chiricolo, M.2    Mariani, E.3    Facchini, A.4
  • 14
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • Hollingsworth, M. A., Swanson, B. J., Mucins in cancer: Protection and control of the cell surface. Nat. Rev. Cancer 2004, 4, 45-60.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 15
    • 33749989239 scopus 로고    scopus 로고
    • A mutant chaperone converts a wild-type protein into a tumorspecific antigen
    • Schietinger, A., Philip, M., Yoshida, B. A., Azadi, P. et al., A mutant chaperone converts a wild-type protein into a tumorspecific antigen. Science 2006, 314, 304-308.
    • (2006) Science , vol.314 , pp. 304-308
    • Schietinger, A.1    Philip, M.2    Yoshida, B.A.3    Azadi, P.4
  • 16
    • 17344368046 scopus 로고    scopus 로고
    • Gene expression of α1-6 fucosyltransferase in human hepatoma tissues: A possible implication for increased fucosylation of α-fetoprotein
    • Noda, K., Miyoshi, E., Uozumi, N., Yanagidani, S. et al., Gene expression of α1-6 fucosyltransferase in human hepatoma tissues: A possible implication for increased fucosylation of α-fetoprotein. Hepatology 1998, 28, 944-952.
    • (1998) Hepatology , vol.28 , pp. 944-952
    • Noda, K.1    Miyoshi, E.2    Uozumi, N.3    Yanagidani, S.4
  • 17
    • 0034749063 scopus 로고    scopus 로고
    • AFP-L3: A new generation of tumor marker for hepatocellular carcinoma
    • Li, D., Mallory, T., Satomura, S., AFP-L3: A new generation of tumor marker for hepatocellular carcinoma. Clin. Chim. Acta 2001, 313, 15-19.
    • (2001) Clin. Chim. Acta , vol.313 , pp. 15-19
    • Li, D.1    Mallory, T.2    Satomura, S.3
  • 18
    • 33646343959 scopus 로고    scopus 로고
    • Fucosylated haptoglobin is a novel marker for pancreatic cancer: A detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation
    • Okuyama, N., Ide, Y., Nakano, M., Nakagawa, T. et al., Fucosylated haptoglobin is a novel marker for pancreatic cancer: A detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation. Int. J. Cancer 2006, 118, 2803-2808.
    • (2006) Int. J. Cancer , vol.118 , pp. 2803-2808
    • Okuyama, N.1    Ide, Y.2    Nakano, M.3    Nakagawa, T.4
  • 19
    • 34948905277 scopus 로고    scopus 로고
    • A new approach for the novel biomarker discovery for cancer
    • Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2-nitrobenzensulfenyl (NBS) stable isotope labeling
    • Ueda, K., Katagiri, T., Shimada, T., Irie, S. et al., Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2-nitrobenzensulfenyl (NBS) stable isotope labeling: A new approach for the novel biomarker discovery for cancer. J. Proteome Res. 2007, 6, 3475-3483.
    • (2007) J. Proteome Res , vol.6 , pp. 3475-3483
    • Ueda, K.1    Katagiri, T.2    Shimada, T.3    Irie, S.4
  • 20
    • 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
    • Miyazaki, K., Ohmori, K., Izawa, M., Koike, T. 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, 4498-4505.
    • (2004) Cancer Res , vol.64 , pp. 4498-4505
    • Miyazaki, K.1    Ohmori, K.2    Izawa, M.3    Koike, T.4
  • 21
    • 0034161897 scopus 로고    scopus 로고
    • Expression of sialyl 6-sulfo Lewis X is inversely correlated with conventional sialyl Lewis X expression in human colorectal cancer
    • Izawa, M., Kumamoto, K., Mitsuoka, C., Kanamori, C. et al., Expression of sialyl 6-sulfo Lewis X is inversely correlated with conventional sialyl Lewis X expression in human colorectal cancer. Cancer Res. 2000, 60, 1410-1416.
    • (2000) Cancer Res , vol.60 , pp. 1410-1416
    • Izawa, M.1    Kumamoto, K.2    Mitsuoka, C.3    Kanamori, C.4
  • 22
    • 33845267469 scopus 로고    scopus 로고
    • The blood peptidome: A higher dimension of information content for cancer biomarker discovery
    • Petricoin, E. F., Belluco, C., Araujo, R. P., Liotta, L. A., The blood peptidome: A higher dimension of information content for cancer biomarker discovery. Nat. Rev. Cancer 2006, 6, 961-967.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 961-967
    • Petricoin, E.F.1    Belluco, C.2    Araujo, R.P.3    Liotta, L.A.4
  • 23
    • 0037086181 scopus 로고    scopus 로고
    • Identification of hepatocarcinoma-intestine-pancreas/pancreatitis-associated protein I as a biomarker for pancreatic ductal adenocarcinoma by protein biochip technology
    • Rosty, C., Christa, L., Kuzdzal, S., Baldwin, W. M. et al., Identification of hepatocarcinoma-intestine-pancreas/pancreatitis-associated protein I as a biomarker for pancreatic ductal adenocarcinoma by protein biochip technology. Cancer Res. 2002, 62, 1868-1875.
    • (2002) Cancer Res , vol.62 , pp. 1868-1875
    • Rosty, C.1    Christa, L.2    Kuzdzal, S.3    Baldwin, W.M.4
  • 24
    • 0024237298 scopus 로고
    • Mutagenesis of the glycosylation site of human ApoCIII. O-linked glycosylation is not required for ApoCIII secretion and lipid binding
    • Roghani, A., Zannis, V. I., Mutagenesis of the glycosylation site of human ApoCIII. O-linked glycosylation is not required for ApoCIII secretion and lipid binding. J. Biol. Chem. 1988, 263, 17925-17932.
    • (1988) J. Biol. Chem , vol.263 , pp. 17925-17932
    • Roghani, A.1    Zannis, V.I.2
  • 25
    • 0033218504 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
    • Harvey, D. J., Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates. Mass Spectrom. Rev. 1999, 18, 349-450.
    • (1999) Mass Spectrom. Rev , vol.18 , pp. 349-450
    • Harvey, D.J.1
  • 26
    • 0031944497 scopus 로고    scopus 로고
    • Analyses of IgA1 hinge glycopeptides in IgA nephropathy by matrixassisted laser desorption/ionization time-of-flight mass spectrometry
    • Hiki, Y., Tanaka, A., Kokubo, T., Iwase, H. et al., Analyses of IgA1 hinge glycopeptides in IgA nephropathy by matrixassisted laser desorption/ionization time-of-flight mass spectrometry. J. Am. Soc. Nephrol. 1998, 9, 577-582.
    • (1998) J. Am. Soc. Nephrol , vol.9 , pp. 577-582
    • Hiki, Y.1    Tanaka, A.2    Kokubo, T.3    Iwase, H.4
  • 27
    • 33646429751 scopus 로고    scopus 로고
    • Three-layer matrix/sample preparation method for MALDI MS analysis of low nanomolar protein samples
    • Keller, B. O., Li, L., Three-layer matrix/sample preparation method for MALDI MS analysis of low nanomolar protein samples. J. Am. Soc. Mass Spectrom. 2006, 17, 780-785.
    • (2006) J. Am. Soc. Mass Spectrom , vol.17 , pp. 780-785
    • Keller, B.O.1    Li, L.2
  • 28
    • 33847238426 scopus 로고    scopus 로고
    • Ionic liquid matrix for direct UV-MALDI-TOF-MS analysis of dermatan sulfate and chondroitin sulfate oligosaccharides
    • Laremore, T. N., Zhang, F., Linhardt, R. J., Ionic liquid matrix for direct UV-MALDI-TOF-MS analysis of dermatan sulfate and chondroitin sulfate oligosaccharides. Anal. Chem. 2007, 79, 1604-1610.
    • (2007) Anal. Chem , vol.79 , pp. 1604-1610
    • Laremore, T.N.1    Zhang, F.2    Linhardt, R.J.3
  • 29
    • 0037093547 scopus 로고    scopus 로고
    • Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose
    • Bourne, Y., Astoul, C. H., Zamboni, V., Peumans, W. J. et al., Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose. Biochem. J. 2002, 364, 173-180.
    • (2002) Biochem. J , vol.364 , pp. 173-180
    • Bourne, Y.1    Astoul, C.H.2    Zamboni, V.3    Peumans, W.J.4
  • 30
    • 0023644482 scopus 로고
    • The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(7alpha;2-6)Gal/GalNAc sequence
    • Shibuya, N., Goldstein, I. J., Broekaert, W. F., Nsimba-Lubaki, M. et al., The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(7alpha;2-6)Gal/GalNAc sequence. J. Biol. Chem. 1987, 262, 1596-1601.
    • (1987) J. Biol. Chem , vol.262 , pp. 1596-1601
    • Shibuya, N.1    Goldstein, I.J.2    Broekaert, W.F.3    Nsimba-Lubaki, M.4
  • 31
    • 33749598630 scopus 로고    scopus 로고
    • Structural analyses of O-glycan sugar chains on IgA1 hinge region using SELDI-TOF MS with various lectins
    • Takahashi, K., Hiki, Y., Odani, H., Shimozato, S. et al., Structural analyses of O-glycan sugar chains on IgA1 hinge region using SELDI-TOF MS with various lectins. Biochem. Biophys. Res. Commun. 2006, 350, 580-587.
    • (2006) Biochem. Biophys. Res. Commun , vol.350 , pp. 580-587
    • Takahashi, K.1    Hiki, Y.2    Odani, H.3    Shimozato, S.4
  • 32
    • 33947281817 scopus 로고    scopus 로고
    • Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: Downregulation of ST6GalNAc VI in renal cancers
    • Senda, M., Ito, A., Tsuchida, A., Hagiwara, T. et al., Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: Downregulation of ST6GalNAc VI in renal cancers. Biochem. J. 2007, 402, 459-470.
    • (2007) Biochem. J , vol.402 , pp. 459-470
    • Senda, M.1    Ito, A.2    Tsuchida, A.3    Hagiwara, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.