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Volumn 39, Issue 12, 2006, Pages 1144-1151

Increase diagnostic efficacy by combined use of fingerprint markers in mass spectrometry-Plasma peptidomes from nasopharyngeal cancer patients for example

Author keywords

Complement 3; MALDI TOF; Nasopharyngeal cancer; Plasma proteome; Tumor marker

Indexed keywords

BIOLOGICAL MARKER; COMPLEMENT COMPONENT C3; COPPER; TUMOR MARKER;

EID: 33751520049     PISSN: 00099120     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2006.08.010     Document Type: Article
Times cited : (30)

References (34)
  • 2
    • 0036912457 scopus 로고    scopus 로고
    • Design of proteome-based studies in combination with serology for the identification of biomarkers and novel targets
    • Seliger B., and Kellner R. Design of proteome-based studies in combination with serology for the identification of biomarkers and novel targets. Proteomics 2 (2002) 1641-1651
    • (2002) Proteomics , vol.2 , pp. 1641-1651
    • Seliger, B.1    Kellner, R.2
  • 3
    • 0038555469 scopus 로고    scopus 로고
    • A strategy for the comparative analysis of serum proteomes for the discovery of biomarkers for hepatocellular carcinoma
    • Steel L.F., Shumpert D., Trotter M., Seeholzer S.H., Evans A.A., London W.T., et al. A strategy for the comparative analysis of serum proteomes for the discovery of biomarkers for hepatocellular carcinoma. Proteomics 3 (2003) 601-609
    • (2003) Proteomics , vol.3 , pp. 601-609
    • Steel, L.F.1    Shumpert, D.2    Trotter, M.3    Seeholzer, S.H.4    Evans, A.A.5    London, W.T.6
  • 4
    • 0036324715 scopus 로고    scopus 로고
    • Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer
    • Li J., Zhang Z., Rosenzweig J., Wang Y.Y., and Chan D.W. Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer. Clin. Chem. 48 (2002) 1296-1304
    • (2002) Clin. Chem. , vol.48 , pp. 1296-1304
    • Li, J.1    Zhang, Z.2    Rosenzweig, J.3    Wang, Y.Y.4    Chan, D.W.5
  • 5
    • 0036549707 scopus 로고    scopus 로고
    • The ProteinChip biomarker system from ciphergen biosystems: a novel proteomics platform for rapid biomarker discovery and validation
    • Chapman K. The ProteinChip biomarker system from ciphergen biosystems: a novel proteomics platform for rapid biomarker discovery and validation. Biochem. Soc. Trans. 30 (2002) 82-87
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 82-87
    • Chapman, K.1
  • 6
    • 0034013944 scopus 로고    scopus 로고
    • Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry
    • Merchant M., and Weinberger S.R. Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 21 (2000) 1164-1177
    • (2000) Electrophoresis , vol.21 , pp. 1164-1177
    • Merchant, M.1    Weinberger, S.R.2
  • 8
    • 0036079692 scopus 로고    scopus 로고
    • The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification
    • Issaq H.J., Veenstra T.D., Conrads T.P., and Felschow D. The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification. Biochem. Biophys. Res. Commun. 292 (2002) 587-592
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 587-592
    • Issaq, H.J.1    Veenstra, T.D.2    Conrads, T.P.3    Felschow, D.4
  • 9
    • 0035881634 scopus 로고    scopus 로고
    • Quantitation of serum prostate-specific membrane antigen by a novel protein biochip immunoassay discriminates benign from malignant prostate disease
    • Xiao Z., Adam B.L., Cazares L.H., Clements M.A., Davis J.W., Schellhammer P.F., et al. Quantitation of serum prostate-specific membrane antigen by a novel protein biochip immunoassay discriminates benign from malignant prostate disease. Cancer Res. 61 (2001) 6029-6033
    • (2001) Cancer Res. , vol.61 , pp. 6029-6033
    • Xiao, Z.1    Adam, B.L.2    Cazares, L.H.3    Clements, M.A.4    Davis, J.W.5    Schellhammer, P.F.6
  • 10
    • 0042736304 scopus 로고    scopus 로고
    • Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform
    • Shiwa M., Nishimura Y., Wakatabe R., Fukawa A., Arikuni H., Ota H., et al. Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform. Biochem. Biophys. Res. Commun. 309 (2003) 18-25
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 18-25
    • Shiwa, M.1    Nishimura, Y.2    Wakatabe, R.3    Fukawa, A.4    Arikuni, H.5    Ota, H.6
  • 11
    • 0036550241 scopus 로고    scopus 로고
    • Analysis of microdissected prostate tissue with ProteinChip arrays-A way to new insights into carcinogenesis and to diagnostic tools
    • Wellmann A., Wollscheid V., Lu H., Ma Z.L., Albers P., Schutze K., et al. Analysis of microdissected prostate tissue with ProteinChip arrays-A way to new insights into carcinogenesis and to diagnostic tools. Int. J. Mol. Med. 9 (2002) 341-347
    • (2002) Int. J. Mol. Med. , vol.9 , pp. 341-347
    • Wellmann, A.1    Wollscheid, V.2    Lu, H.3    Ma, Z.L.4    Albers, P.5    Schutze, K.6
  • 12
    • 0344236284 scopus 로고    scopus 로고
    • Prostate carcinoma tissue proteomics for biomarker discovery
    • Zheng Y., Xu Y., Ye B., Lei J., Weinstein M.H., O'Leary M.P., et al. Prostate carcinoma tissue proteomics for biomarker discovery. Cancer 98 (2003) 2576-2582
    • (2003) Cancer , vol.98 , pp. 2576-2582
    • Zheng, Y.1    Xu, Y.2    Ye, B.3    Lei, J.4    Weinstein, M.H.5    O'Leary, M.P.6
  • 13
    • 0142027764 scopus 로고    scopus 로고
    • Identification of biomarkers for ovarian cancer using strong anion-exchange Protein Chips: potential use in diagnosis and prognosis
    • Kozak K.R., Amneus M.W., Pusey S.M., Su F., Luong M.N., Luong S.A., et al. Identification of biomarkers for ovarian cancer using strong anion-exchange Protein Chips: potential use in diagnosis and prognosis. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 12343-12348
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12343-12348
    • Kozak, K.R.1    Amneus, M.W.2    Pusey, S.M.3    Su, F.4    Luong, M.N.5    Luong, S.A.6
  • 14
    • 1542722311 scopus 로고    scopus 로고
    • Amyloid beta peptides in cerebrospinal fluid as profiled with surface enhanced laser desorption/ionization time-of-flight mass spectrometry: evidence of novel biomarkers in Alzheimer's disease
    • Lewczuk P., Esselmann H., Groemer T.W., Bibl M., Maler J.M., Steinacker P., et al. Amyloid beta peptides in cerebrospinal fluid as profiled with surface enhanced laser desorption/ionization time-of-flight mass spectrometry: evidence of novel biomarkers in Alzheimer's disease. Biol. Psychiatry 55 (2004) 524-530
    • (2004) Biol. Psychiatry , vol.55 , pp. 524-530
    • Lewczuk, P.1    Esselmann, H.2    Groemer, T.W.3    Bibl, M.4    Maler, J.M.5    Steinacker, P.6
  • 15
    • 3042643404 scopus 로고    scopus 로고
    • Detection of prostate cancer using serum proteomics pattern in a histologically confirmed population
    • Li J., White N., Zhang Z., Rosenzweig J., Mangold L.A., Partin A.W., et al. Detection of prostate cancer using serum proteomics pattern in a histologically confirmed population. J. Urol. 171 (2004) 1782-1787
    • (2004) J. Urol. , vol.171 , pp. 1782-1787
    • Li, J.1    White, N.2    Zhang, Z.3    Rosenzweig, J.4    Mangold, L.A.5    Partin, A.W.6
  • 17
    • 0142250869 scopus 로고    scopus 로고
    • Proteomic profiling of urinary proteins in renal cancer by surface enhanced laser desorption ionization and neural-network analysis: identification of key issues affecting potential clinical utility
    • Rogers M.A., Clarke P., Noble J., Munro N.P., Paul A., Selby P.J., et al. Proteomic profiling of urinary proteins in renal cancer by surface enhanced laser desorption ionization and neural-network analysis: identification of key issues affecting potential clinical utility. Cancer Res. 63 (2003) 6971-6983
    • (2003) Cancer Res. , vol.63 , pp. 6971-6983
    • Rogers, M.A.1    Clarke, P.2    Noble, J.3    Munro, N.P.4    Paul, A.5    Selby, P.J.6
  • 18
    • 28044447188 scopus 로고    scopus 로고
    • Oral cancer plasma tumor marker identified with bead-based affinity fractionated proteomic technology
    • Cheng A.J., Chen L.C., Chien K.Y., Chen J.Y., Chang J.TC., Wang H.M., et al. Oral cancer plasma tumor marker identified with bead-based affinity fractionated proteomic technology. Clin. Chem. 51 (2005) 2236-2244
    • (2005) Clin. Chem. , vol.51 , pp. 2236-2244
    • Cheng, A.J.1    Chen, L.C.2    Chien, K.Y.3    Chen, J.Y.4    Chang, J.TC.5    Wang, H.M.6
  • 21
    • 0042967757 scopus 로고    scopus 로고
    • Proteomics delivers on promise of cancer biomarkers
    • Powell K. Proteomics delivers on promise of cancer biomarkers. Nat. Med. 9 (2003) 980
    • (2003) Nat. Med. , vol.9 , pp. 980
    • Powell, K.1
  • 23
    • 2542640080 scopus 로고    scopus 로고
    • Mass spectrometry as a diagnostic and a cancer biomarker discovery tool
    • Diamandis E.P. Mass spectrometry as a diagnostic and a cancer biomarker discovery tool. Mol. Cell Proteomics 3 (2004) 367-378
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 367-378
    • Diamandis, E.P.1
  • 24
    • 20844448187 scopus 로고    scopus 로고
    • Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery
    • Moomen J.M., Li D., Xiao L.C., Liu T.C., Copmbes K.R., Abbruzzese J., et al. Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery. J. Proteome Res. 4 (2005) 972-981
    • (2005) J. Proteome Res. , vol.4 , pp. 972-981
    • Moomen, J.M.1    Li, D.2    Xiao, L.C.3    Liu, T.C.4    Copmbes, K.R.5    Abbruzzese, J.6
  • 25
    • 23944492134 scopus 로고    scopus 로고
    • Overview of the HUPO plasma proteome project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Omenn G.S., States D.J., Adamski M., Blackwell T.W., Menon R., Hermjakob H., et al. Overview of the HUPO plasma proteome project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics 5 (2005) 3226-3245
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4    Menon, R.5    Hermjakob, H.6
  • 26
    • 22544475902 scopus 로고    scopus 로고
    • Plasma chromogranin A in patients with prostate cancer improves the diagnostic efficacy of free/total prostate-specific antigen determination
    • Fracalanza S., Prayer-Galetti T., Pinto F., Navaglia F., Sacco E., Ciaccia M., et al. Plasma chromogranin A in patients with prostate cancer improves the diagnostic efficacy of free/total prostate-specific antigen determination. Urol. Int. 75 (2005) 57-61
    • (2005) Urol. Int. , vol.75 , pp. 57-61
    • Fracalanza, S.1    Prayer-Galetti, T.2    Pinto, F.3    Navaglia, F.4    Sacco, E.5    Ciaccia, M.6
  • 27
    • 12144291343 scopus 로고    scopus 로고
    • Utility of combined use of plasma levels of chromogranin A and pancreatic polypeptide in the diagnosis of gastrointestinal and pancreatic endocrine tumors
    • Panzuto F., Severi C., Cannizzaro R., Falconi M., Angeletti S., Pasquali A., et al. Utility of combined use of plasma levels of chromogranin A and pancreatic polypeptide in the diagnosis of gastrointestinal and pancreatic endocrine tumors. J. Endocrinol. Invest. 27 (2004) 6-11
    • (2004) J. Endocrinol. Invest. , vol.27 , pp. 6-11
    • Panzuto, F.1    Severi, C.2    Cannizzaro, R.3    Falconi, M.4    Angeletti, S.5    Pasquali, A.6
  • 28
    • 0344642968 scopus 로고    scopus 로고
    • The expression of mammaglobin mRNA in peripheral blood of metastatic breast cancer patients as an adjunct to serum tumor markers
    • Lin Y.C., Chou Y.HW., Liao I.C., and Cheng A.J. The expression of mammaglobin mRNA in peripheral blood of metastatic breast cancer patients as an adjunct to serum tumor markers. Cancer Lett. 191 (2003) 93-99
    • (2003) Cancer Lett. , vol.191 , pp. 93-99
    • Lin, Y.C.1    Chou, Y.HW.2    Liao, I.C.3    Cheng, A.J.4
  • 29
    • 0038693797 scopus 로고    scopus 로고
    • Beyond lysis: how complement influences cell fate
    • Cole D.S., and Morgan B.P. Beyond lysis: how complement influences cell fate. Clin. Sci. (Lond) 104 (2003) 455-466
    • (2003) Clin. Sci. (Lond) , vol.104 , pp. 455-466
    • Cole, D.S.1    Morgan, B.P.2
  • 30
    • 0023949729 scopus 로고
    • Structure of C3f, a small peptide specifically released during inactivation of the third component of complement
    • Harrison R.A., Farries T.C., Northrop F.D., Lachmann P.J., and Davis A.E. Structure of C3f, a small peptide specifically released during inactivation of the third component of complement. Complement 5 (1988) 27-32
    • (1988) Complement , vol.5 , pp. 27-32
    • Harrison, R.A.1    Farries, T.C.2    Northrop, F.D.3    Lachmann, P.J.4    Davis, A.E.5
  • 31
    • 8744244478 scopus 로고    scopus 로고
    • Cellular membrane type-1 matrix metalloproteinase (MT1-MMP) cleaves C3b, an essential component of the complement system
    • Rozanov D.V., Savinov A.Y., Golubkov V.S., Postnova T.I., Remacle A., Tomlinson S., et al. Cellular membrane type-1 matrix metalloproteinase (MT1-MMP) cleaves C3b, an essential component of the complement system. J. Biol. Chem. 279 (2004) 46551-46557
    • (2004) J. Biol. Chem. , vol.279 , pp. 46551-46557
    • Rozanov, D.V.1    Savinov, A.Y.2    Golubkov, V.S.3    Postnova, T.I.4    Remacle, A.5    Tomlinson, S.6
  • 32
    • 4644366103 scopus 로고    scopus 로고
    • Complement inhibitor membrane cofactor protein (MCP; CD46) is constitutively shed from cancer cell membranes in vesicles and converted by a metalloproteinase to a functionally active soluble form
    • Hakulinen J., Junnikkala S., Sorsa T., and Meri S. Complement inhibitor membrane cofactor protein (MCP; CD46) is constitutively shed from cancer cell membranes in vesicles and converted by a metalloproteinase to a functionally active soluble form. Eur. J. Immunol. 34 (2004) 2620-2629
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2620-2629
    • Hakulinen, J.1    Junnikkala, S.2    Sorsa, T.3    Meri, S.4
  • 33
    • 0038555469 scopus 로고    scopus 로고
    • A strategy for the comparative analysis of serum proteomes for the discovery of biomarkers for hepatocellular carcinoma
    • Steel L.F., Shumpert D., Trotter M., Seeholzer S.H., Evans A.A., London W.T., et al. A strategy for the comparative analysis of serum proteomes for the discovery of biomarkers for hepatocellular carcinoma. Proteomics 3 (2003) 601-609
    • (2003) Proteomics , vol.3 , pp. 601-609
    • Steel, L.F.1    Shumpert, D.2    Trotter, M.3    Seeholzer, S.H.4    Evans, A.A.5    London, W.T.6
  • 34
    • 21644462508 scopus 로고    scopus 로고
    • Immunoglobulins and complement components in patients with lung cancer
    • Oner F., Savas I., and Numanoglu N. Immunoglobulins and complement components in patients with lung cancer. Tuberk Toraks 52 (2004) 19-23
    • (2004) Tuberk Toraks , vol.52 , pp. 19-23
    • Oner, F.1    Savas, I.2    Numanoglu, N.3


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