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Volumn 78, Issue , 2013, Pages 172-187

Protein expression profiles of human lymph and plasma mapped by 2D-DIGE and 1D SDS-PAGE coupled with nanoLC-ESI-MS/MS bottom-up proteomics

Author keywords

2D DIGE; Biomarkers; Lymph; NanoLC ESI MS MS; Plasma; Proteomic

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA 2 ANTIPLASMIN; ANGIOTENSINOGEN; APOLIPOPROTEIN A1; BLOOD CLOTTING FACTOR; CALGRANULIN A; CALGRANULIN B; CASPASE 14; CATHEPSIN X; COMPLEMENT; COMPLEMENT COMPONENT C4B; COMPLEMENT COMPONENT C4B3; DESMOGLEIN 1; FETUIN B; FIBRINOGEN; FIBRINOGEN GAMMA CHAIN; GALECTIN 7; GELSOLIN; HAPTOGLOBIN; LUMICAN; PIGMENT EPITHELIUM DERIVED FACTOR; PREALBUMIN; PROTEIN; PROTEINASE INHIBITOR; PROTEOME; PROTHROMBIN; STEFIN A; TETRANECTIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VITAMIN D BINDING PROTEIN;

EID: 84871744989     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.11.013     Document Type: Article
Times cited : (61)

References (39)
  • 2
    • 12444297666 scopus 로고    scopus 로고
    • The conduit system transports soluble antigens from the afferent lymph to resident dendritic cells in the T cell area of the lymph node
    • Sixt M., Kanazawa N., Selg M., Samson T., Roos G., Reinhardt D.P., et al. The conduit system transports soluble antigens from the afferent lymph to resident dendritic cells in the T cell area of the lymph node. Immunity 2005, 22:19-29.
    • (2005) Immunity , vol.22 , pp. 19-29
    • Sixt, M.1    Kanazawa, N.2    Selg, M.3    Samson, T.4    Roos, G.5    Reinhardt, D.P.6
  • 3
    • 60149086845 scopus 로고    scopus 로고
    • Conduits mediate transport of low-molecular-weight antigen to lymph node follicles
    • Roozendaal R., Mempel T.R., Pitcher L.A., Gonzalez S.A., Verschoor S. Conduits mediate transport of low-molecular-weight antigen to lymph node follicles. Immunity 2009, 30:264-276.
    • (2009) Immunity , vol.30 , pp. 264-276
    • Roozendaal, R.1    Mempel, T.R.2    Pitcher, L.A.3    Gonzalez, S.A.4    Verschoor, S.5
  • 4
    • 0029902442 scopus 로고    scopus 로고
    • Sophisticated strategies for information encounter in the lymph node: the reticular network as a conduit of soluble information and a highway for cell traffic
    • Gretz J.E., Kaldjian E.P., Anderson A.O., Shaw S. Sophisticated strategies for information encounter in the lymph node: the reticular network as a conduit of soluble information and a highway for cell traffic. J Immunol 1996, 157:495-499.
    • (1996) J Immunol , vol.157 , pp. 495-499
    • Gretz, J.E.1    Kaldjian, E.P.2    Anderson, A.O.3    Shaw, S.4
  • 6
    • 3242658813 scopus 로고    scopus 로고
    • Profiling of normal human leg lymph proteins using the 2-D electrophoresis and SELDI-TOF mass spectrophotometry approach
    • Interewicz B., Olszewski W.L., Leak L.V., Petricoin E.F., Liotta L.A. Profiling of normal human leg lymph proteins using the 2-D electrophoresis and SELDI-TOF mass spectrophotometry approach. Lymphology 2004, 37:65-72.
    • (2004) Lymphology , vol.37 , pp. 65-72
    • Interewicz, B.1    Olszewski, W.L.2    Leak, L.V.3    Petricoin, E.F.4    Liotta, L.A.5
  • 7
    • 0033838347 scopus 로고    scopus 로고
    • Lipid and apolipoprotein concentrations in prenodal leg lymph of fasted humans. Associations with plasma concentrations in normal subjects, lipoprotein lipase deficiency, and LCAT deficiency
    • Nanjee M.N., Cooke C.J., Olszewski W.L., Miller N.L. Lipid and apolipoprotein concentrations in prenodal leg lymph of fasted humans. Associations with plasma concentrations in normal subjects, lipoprotein lipase deficiency, and LCAT deficiency. J Lipid Res 2000, 41:1317-1327.
    • (2000) J Lipid Res , vol.41 , pp. 1317-1327
    • Nanjee, M.N.1    Cooke, C.J.2    Olszewski, W.L.3    Miller, N.L.4
  • 8
    • 0035080360 scopus 로고    scopus 로고
    • Lymph draining from foot joints in rheumatoid arthritis provides insight into local cytokine and chemokine production and transport to lymph nodes
    • Olszewski W.L., Pazdur J., Kubasiewicz E., Zaleska M., Cooke C.J., Miller N.E. Lymph draining from foot joints in rheumatoid arthritis provides insight into local cytokine and chemokine production and transport to lymph nodes. Arthritis Rheum 2001, 44:541-549.
    • (2001) Arthritis Rheum , vol.44 , pp. 541-549
    • Olszewski, W.L.1    Pazdur, J.2    Kubasiewicz, E.3    Zaleska, M.4    Cooke, C.J.5    Miller, N.E.6
  • 9
    • 77957892664 scopus 로고    scopus 로고
    • The gastrointestinal nematode Trichostrongylus colubriformis down-regulates immune gene expression in migratory cells in afferent lymph
    • Knight J.S., Baird D.B., Hein W.R., Pernthaner A. The gastrointestinal nematode Trichostrongylus colubriformis down-regulates immune gene expression in migratory cells in afferent lymph. BMC Immunol 2010, 11:51.
    • (2010) BMC Immunol , vol.11 , pp. 51
    • Knight, J.S.1    Baird, D.B.2    Hein, W.R.3    Pernthaner, A.4
  • 10
    • 67650541169 scopus 로고    scopus 로고
    • Proteome and system ontology of hemorrhagic shock: exploring early constitutive changes in postshock mesenteric lymph
    • Peltz E.D., Moore E.E., Zurawel A.A., Jordan J.R., Damle S.S., Redzic J.S., et al. Proteome and system ontology of hemorrhagic shock: exploring early constitutive changes in postshock mesenteric lymph. Surgery 2009, 146(2):347-357.
    • (2009) Surgery , vol.146 , Issue.2 , pp. 347-357
    • Peltz, E.D.1    Moore, E.E.2    Zurawel, A.A.3    Jordan, J.R.4    Damle, S.S.5    Redzic, J.S.6
  • 13
    • 78650729152 scopus 로고    scopus 로고
    • An expanded self-antigen peptidome is carried by the human lymph as compared to the plasma
    • Mar 26
    • Clement C.C., Cannizzo E.S., Nastke M.D., Sahu R., Olszewski W., Miller N.E., et al. An expanded self-antigen peptidome is carried by the human lymph as compared to the plasma. PLoS One Mar 26 2010, 5(3):e9863.
    • (2010) PLoS One , vol.5 , Issue.3
    • Clement, C.C.1    Cannizzo, E.S.2    Nastke, M.D.3    Sahu, R.4    Olszewski, W.5    Miller, N.E.6
  • 14
    • 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 2005, 13:3226-3245.
    • (2005) Proteomics , vol.13 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4    Menon, R.5    Hermjakob, H.6
  • 15
    • 33751008035 scopus 로고    scopus 로고
    • Sepsis plasma protein profiling with immunodepletion, three-dimensional liquid chromatography tandem mass spectrometry, and spectrum counting
    • Shen Z., Want E.J., Chen W., Keating W., Nussbaumer W., Moore R., et al. Sepsis plasma protein profiling with immunodepletion, three-dimensional liquid chromatography tandem mass spectrometry, and spectrum counting. J Proteome Res 2006, 5:3154-3160.
    • (2006) J Proteome Res , vol.5 , pp. 3154-3160
    • Shen, Z.1    Want, E.J.2    Chen, W.3    Keating, W.4    Nussbaumer, W.5    Moore, R.6
  • 16
    • 23944524368 scopus 로고    scopus 로고
    • Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma
    • Echan L.A., Tang H.Y., Li-Khan N., Lee K., Speicher D.W. Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma. Proteomics 2005, 13:3292-3303.
    • (2005) Proteomics , vol.13 , pp. 3292-3303
    • Echan, L.A.1    Tang, H.Y.2    Li-Khan, N.3    Lee, K.4    Speicher, D.W.5
  • 17
    • 16544391581 scopus 로고    scopus 로고
    • Serum/plasma depletion with chicken immunoglobulin Y antibodies for proteomic analysis from multiple Mammalian species
    • Hinerfeld D., Innamorati D., Pirro J., Tam S.W. Serum/plasma depletion with chicken immunoglobulin Y antibodies for proteomic analysis from multiple Mammalian species. J Biomol Tech 2004, 3:184-190.
    • (2004) J Biomol Tech , vol.3 , pp. 184-190
    • Hinerfeld, D.1    Innamorati, D.2    Pirro, J.3    Tam, S.W.4
  • 18
    • 34247627759 scopus 로고    scopus 로고
    • Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling
    • Tannu N.S., Hemby S.E. Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling. Nat Protoc 2006, 1:1732-1742.
    • (2006) Nat Protoc , vol.1 , pp. 1732-1742
    • Tannu, N.S.1    Hemby, S.E.2
  • 19
    • 23944503319 scopus 로고    scopus 로고
    • Application of two-dimensional difference gel electrophoresis to studying bone marrow macrophages and their in vivo responses to ionizing radiation
    • Chen C., Boylan M.T., Evans C.A., Whetton A.D., Wright E.G. Application of two-dimensional difference gel electrophoresis to studying bone marrow macrophages and their in vivo responses to ionizing radiation. J Proteome Res 2005, 4:1371-1380.
    • (2005) J Proteome Res , vol.4 , pp. 1371-1380
    • Chen, C.1    Boylan, M.T.2    Evans, C.A.3    Whetton, A.D.4    Wright, E.G.5
  • 20
    • 26844512938 scopus 로고    scopus 로고
    • Characterization of proteins in human pancreatic cancer serum using differential gel electrophoresis and tandem mass spectrometry
    • Yu K.H., Rustgi A.K., Blair I.A. Characterization of proteins in human pancreatic cancer serum using differential gel electrophoresis and tandem mass spectrometry. J Proteome Res 2005, 4:1742-1751.
    • (2005) J Proteome Res , vol.4 , pp. 1742-1751
    • Yu, K.H.1    Rustgi, A.K.2    Blair, I.A.3
  • 21
    • 0036463947 scopus 로고    scopus 로고
    • Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system
    • Gharbi S., Gaffney P., Yang A., Zvelebil M.J., Cramer R., Waterfield M.D., et al. Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system. Mol Cell Proteomics 2002, 1:91-98.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 91-98
    • Gharbi, S.1    Gaffney, P.2    Yang, A.3    Zvelebil, M.J.4    Cramer, R.5    Waterfield, M.D.6
  • 22
    • 38649083118 scopus 로고    scopus 로고
    • Assigning significance to peptides identified by tandem mass spectrometry using decoy databases
    • Kall L., Storey J.D., MacCoss M.J., Noble S.W. Assigning significance to peptides identified by tandem mass spectrometry using decoy databases. J Proteome Res 2008, 7:29-34.
    • (2008) J Proteome Res , vol.7 , pp. 29-34
    • Kall, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, S.W.4
  • 23
    • 70349912263 scopus 로고    scopus 로고
    • False discovery rates of protein identifications: a strike against the two-peptide rule
    • Gupta N., Pevzner P.A. False discovery rates of protein identifications: a strike against the two-peptide rule. J Proteome Res 2009, 8:4173-4181.
    • (2009) J Proteome Res , vol.8 , pp. 4173-4181
    • Gupta, N.1    Pevzner, P.A.2
  • 26
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002, 74(20):5383-5392.
    • (2002) Anal Chem , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 27
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I. A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 2003, 75(17):4646-4658.
    • (2003) Anal Chem , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1
  • 29
    • 0035987523 scopus 로고    scopus 로고
    • Comparison of one-dimensional and two-dimensional gel electrophoresis as a separation tool for proteomic analysis of rat liver microsomes: cytochromes P450 and other membrane proteins
    • Galeva N., Altermann M. Comparison of one-dimensional and two-dimensional gel electrophoresis as a separation tool for proteomic analysis of rat liver microsomes: cytochromes P450 and other membrane proteins. Proteomics 2002, 2:713-722.
    • (2002) Proteomics , vol.2 , pp. 713-722
    • Galeva, N.1    Altermann, M.2
  • 30
    • 77950641486 scopus 로고    scopus 로고
    • Workflow comparison for label-free, quantitative secretome proteomics for cancer biomarker discovery: method evaluation, differential analysis, and verification in serum
    • Piersma S.R., Fiedler U., Span S., Lingnau A., Pham T.V., Hoffmann S., et al. Workflow comparison for label-free, quantitative secretome proteomics for cancer biomarker discovery: method evaluation, differential analysis, and verification in serum. J Proteome Res 2010, 9(4):1913-1922.
    • (2010) J Proteome Res , vol.9 , Issue.4 , pp. 1913-1922
    • Piersma, S.R.1    Fiedler, U.2    Span, S.3    Lingnau, A.4    Pham, T.V.5    Hoffmann, S.6
  • 31
    • 38349097360 scopus 로고    scopus 로고
    • Body fluid proteomics: prospects for biomarker discovery
    • Ahn S.-M., Simpson R.J. Body fluid proteomics: prospects for biomarker discovery. Proteomics Clin Appl 2007, 1(9):1004-1015.
    • (2007) Proteomics Clin Appl , vol.1 , Issue.9 , pp. 1004-1015
    • Ahn, S.-M.1    Simpson, R.J.2
  • 32
    • 38349150933 scopus 로고    scopus 로고
    • Proteomic analysis of serum, plasma, and lymph for the identification of biomarkers
    • Meng Z., Veenstra T.D. Proteomic analysis of serum, plasma, and lymph for the identification of biomarkers. Proteomics Clin Appl 2007, 1(8):747-757.
    • (2007) Proteomics Clin Appl , vol.1 , Issue.8 , pp. 747-757
    • Meng, Z.1    Veenstra, T.D.2
  • 33
    • 25144467417 scopus 로고    scopus 로고
    • Proteome profiling in body fluids and in cancer cell signaling
    • Armandola E.A. Proteome profiling in body fluids and in cancer cell signaling. MedGenMed 2003, 5(2):18.
    • (2003) MedGenMed , vol.5 , Issue.2 , pp. 18
    • Armandola, E.A.1
  • 35
    • 84875259273 scopus 로고    scopus 로고
    • Proteomic profiling of the mesenteric lymph after hemorrhagic shock: differential gel electrophoresis and mass spectrometry analysis
    • Zurawel A., Moore Ernest E., Peltz Erik D., Jordan Janeen R., Damle Sagar, Dzieciatkowska Monika, et al. Proteomic profiling of the mesenteric lymph after hemorrhagic shock: differential gel electrophoresis and mass spectrometry analysis. Clin Proteomics 2011, 8(1):1-14.
    • (2011) Clin Proteomics , vol.8 , Issue.1 , pp. 1-14
    • Zurawel, A.1    Moore, E.E.2    Peltz, E.D.3    Jordan, J.R.4    Damle, S.5    Dzieciatkowska, M.6
  • 37
    • 79959499115 scopus 로고    scopus 로고
    • A high confidence human plasma proteome reference set with estimated concentrations in PeptideAtlas
    • Farrah T., Deutsch E.W., Omenn G.S., Campbell D.S., Sun Z., Bletz J.A., et al. A high confidence human plasma proteome reference set with estimated concentrations in PeptideAtlas. Mol Cell Proteomics 2011, 10(9):6353-14.
    • (2011) Mol Cell Proteomics , vol.10 , Issue.9 , pp. 6353-6414
    • Farrah, T.1    Deutsch, E.W.2    Omenn, G.S.3    Campbell, D.S.4    Sun, Z.5    Bletz, J.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.