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Volumn 10, Issue 11, 2011, Pages 5059-5069

Global survey of the bovine salivary proteome: Integrating multidimensional prefractionation, targeted, and glycocapture strategies

Author keywords

bovine saliva; global proteome; multidimensional fractionation; N linked glycoproteins; proteomics; targeted proteomics

Indexed keywords

GLYCOPROTEIN; PROTEOME; SALIVA PROTEIN;

EID: 80655135399     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200516d     Document Type: Article
Times cited : (51)

References (52)
  • 1
    • 0038393048 scopus 로고
    • Saliva secretion and its relation to feeding in cattle. 2. the composition and rate of secretion of mixed saliva in the cow during rest
    • Bailey, C. B.; Balch, C. C. Saliva secretion and its relation to feeding in cattle. 2. The composition and rate of secretion of mixed saliva in the cow during rest Br. J. Nutr. 1961, 15, 383-402
    • (1961) Br. J. Nutr. , vol.15 , pp. 383-402
    • Bailey, C.B.1    Balch, C.C.2
  • 2
    • 0041015870 scopus 로고
    • Saliva secretion and its relation to feeding in cattle. 4. the relationship between the concentrations of sodium, potassium, chloride and inorganic phosphate in mixed saliva and rumen fluid
    • Bailey, C. B. Saliva secretion and its relation to feeding in cattle. 4. The relationship between the concentrations of sodium, potassium, chloride and inorganic phosphate in mixed saliva and rumen fluid Br. J. Nutr. 1961, 15, 489-98
    • (1961) Br. J. Nutr. , vol.15 , pp. 489-98
    • Bailey, C.B.1
  • 3
    • 0027179921 scopus 로고
    • Cross-sectional and longitudinal analyses of stimulated parotid salivary constituents in healthy, different-aged subjects
    • Wu, A. J.; Atkinson, J. C.; Fox, P. C.; Baum, B. J.; Ship, J. A. Cross-sectional and longitudinal analyses of stimulated parotid salivary constituents in healthy, different-aged subjects J. Gerontol. 1993, 48 (5) M219-24
    • (1993) J. Gerontol. , vol.48 , Issue.5 , pp. 219-24
    • Wu, A.J.1    Atkinson, J.C.2    Fox, P.C.3    Baum, B.J.4    Ship, J.A.5
  • 4
    • 0030898293 scopus 로고    scopus 로고
    • Future applications of oral fluid specimen technology
    • George, J. R.; Fitchen, J. H. Future applications of oral fluid specimen technology Am. J. Med. 1997, 102 (4A) 21-5 (Pubitemid 27262196)
    • (1997) American Journal of Medicine , vol.102 , Issue.4 A , pp. 21-25
    • George, J.R.1    Fitchen, J.H.2
  • 7
    • 66949131114 scopus 로고    scopus 로고
    • Preparing multiple-reaction monitoring for quantitative clinical proteomics
    • Kim, K.; Kim, Y. Preparing multiple-reaction monitoring for quantitative clinical proteomics Expert Rev. Proteomics 2009, 6 (3) 225-9
    • (2009) Expert Rev. Proteomics , vol.6 , Issue.3 , pp. 225-9
    • Kim, K.1    Kim, Y.2
  • 9
    • 0035260692 scopus 로고    scopus 로고
    • Genetic dissection of phenotypic diversity in farm animals
    • DOI 10.1038/35052563
    • Andersson, L. Genetic dissection of phenotypic diversity in farm animals Nat. Rev. Genet. 2001, 2 (2) 130-8 (Pubitemid 33674004)
    • (2001) Nature Reviews Genetics , vol.2 , Issue.2 , pp. 130-138
    • Andersson, L.1
  • 10
    • 66249122107 scopus 로고    scopus 로고
    • Mapping genes for complex traits in domestic animals and their use in breeding programmes
    • Goddard, M. E.; Hayes, B. J. Mapping genes for complex traits in domestic animals and their use in breeding programmes Nat. Rev. Genet. 2009, 10 (6) 381-91
    • (2009) Nat. Rev. Genet. , vol.10 , Issue.6 , pp. 381-91
    • Goddard, M.E.1    Hayes, B.J.2
  • 11
    • 34447249556 scopus 로고    scopus 로고
    • Ruminal nitrogen metabolism: Perspectives for integration of microbiology and nutrition for dairy
    • Firkins, J. L.; Yu, Z.; Morrison, M. Ruminal nitrogen metabolism: perspectives for integration of microbiology and nutrition for dairy J. Dairy Sci. 2007, 90 (Suppl 1) E1-16
    • (2007) J. Dairy Sci. , vol.90 , Issue.SUPPL. 1 , pp. 1-16
    • Firkins, J.L.1    Yu, Z.2    Morrison, M.3
  • 12
    • 0000184786 scopus 로고
    • Manipulating Rumen Fermentation
    • Chalupa, W. Manipulating Rumen Fermentation J. Anim. Sci. 1977, 45, 585-99
    • (1977) J. Anim. Sci. , vol.45 , pp. 585-99
    • Chalupa, W.1
  • 13
    • 0032716645 scopus 로고    scopus 로고
    • Reducing rumen methane emissions through elimination of rumen protozoa
    • Hegarty, R. Reducing rumen methane emissions through elimination of rumen protozoa Aust. J. Agric. Res. 1999, 1321-7
    • (1999) Aust. J. Agric. Res. , pp. 1321-7
    • Hegarty, R.1
  • 14
    • 0035843960 scopus 로고    scopus 로고
    • Factors that alter rumen microbial ecology
    • DOI 10.1126/science.1058830
    • Russell, J. B.; Rychlik, J. L. Factors that alter rumen microbial ecology Science 2001, 292 (5519) 1119-22 (Pubitemid 32440926)
    • (2001) Science , vol.292 , Issue.5519 , pp. 1119-1122
    • Russell, J.B.1    Rychlik, J.L.2
  • 15
    • 4444300414 scopus 로고    scopus 로고
    • Reducing methane emissions in sheep by immunization against rumen methanogens
    • DOI 10.1016/j.vaccine.2004.03.053, PII S0264410X04003196
    • Wright, A. D.; Kennedy, P.; O'Neill, C. J.; Toovey, A. F.; Popovski, S.; Rea, S. M.; Pimm, C. L.; Klein, L. Reducing methane emissions in sheep by immunization against rumen methanogens Vaccine 2004, 22 (29-30) 3976-85 (Pubitemid 39208761)
    • (2004) Vaccine , vol.22 , Issue.29-30 , pp. 3976-3985
    • Wright, A.D.G.1    Kennedy, P.2    O'Neill, C.J.3    Toovey, A.F.4    Popovski, S.5    Rea, S.M.6    Pimm, C.L.7    Klein, L.8
  • 16
    • 84988074823 scopus 로고
    • The purification and characterization of bovine salivary proteins by electrophoretic procedures
    • McLaren, R. D.; McIntosh, J. T.; Howe, G. W. The purification and characterization of bovine salivary proteins by electrophoretic procedures Electrophoresis 1987, 8 (7) 318-24
    • (1987) Electrophoresis , vol.8 , Issue.7 , pp. 318-24
    • McLaren, R.D.1    McIntosh, J.T.2    Howe, G.W.3
  • 17
    • 0030329937 scopus 로고    scopus 로고
    • The relative abundance of a salivary protein, bSP30, is correlated with susceptibility to bloat in cattle herds selected for high or low bloat susceptibility
    • Rajan, G. H.; Morris, C. A.; Carruthers, V. R.; Wilkins, R. J.; Wheeler, T. T. The relative abundance of a salivary protein, bSP30, is correlated with susceptibility to bloat in cattle herds selected for high or low bloat susceptibility Anim. Genet. 1996, 27 (6) 407-14 (Pubitemid 126447608)
    • (1996) Animal Genetics , vol.27 , Issue.6 , pp. 407-414
    • Rajan, G.H.1    Morris, C.A.2    Carruthers, V.R.3    Wilkins, R.J.4    Wheeler, T.T.5
  • 18
    • 13844276803 scopus 로고    scopus 로고
    • Prefractionation techniques in proteome analysis: The mining tools of the third millennium
    • DOI 10.1002/elps.200406189
    • Righetti, P. G.; Castagna, A.; Antonioli, P.; Boschetti, E. Prefractionation techniques in proteome analysis: the mining tools of the third millennium Electrophoresis 2005, 26 (2) 297-319 (Pubitemid 40253785)
    • (2005) Electrophoresis , vol.26 , Issue.2 , pp. 297-319
    • Righetti, P.G.1    Castagna, A.2    Antonioli, P.3    Boschetti, E.4
  • 21
    • 42549084285 scopus 로고    scopus 로고
    • 18O reverse proteolytic labeling to determine the effect of biofilm culture on the cell envelope proteome of Porphyromonas gingivalis W50
    • DOI 10.1002/pmic.200700557
    • Ang, C. S.; Veith, P. D.; Dashper, S. G.; Reynolds, E. C. Application of 16O/18O reverse proteolytic labeling to determine the effect of biofilm culture on the cell envelope proteome of Porphyromonas gingivalis W50 Proteomics 2008, 8 (8) 1645-60 (Pubitemid 351580210)
    • (2008) Proteomics , vol.8 , Issue.8 , pp. 1645-1660
    • Ang, C.-S.1    Veith, P.D.2    Dashper, S.G.3    Reynolds, E.C.4
  • 22
    • 79960729952 scopus 로고    scopus 로고
    • Use of multiple reaction monitoring for multiplex analysis of colorectal cancer-associated proteins in human feces
    • Ang, C. S.; Rothacker, J.; Patsiouras, H.; Gibbs, P.; Burgess, A. W.; Nice, E. C. Use of multiple reaction monitoring for multiplex analysis of colorectal cancer-associated proteins in human feces Electrophoresis 2011, 32 (15) 1926-38
    • (2011) Electrophoresis , vol.32 , Issue.15 , pp. 1926-38
    • Ang, C.S.1    Rothacker, J.2    Patsiouras, H.3    Gibbs, P.4    Burgess, A.W.5    Nice, E.C.6
  • 23
    • 55049104915 scopus 로고    scopus 로고
    • Accurate inclusion mass screening: A bridge from unbiased discovery to targeted assay development for biomarker verification
    • Jaffe, J. D.; Keshishian, H.; Chang, B.; Addona, T. A.; Gillette, M. A.; Carr, S. A. Accurate inclusion mass screening: a bridge from unbiased discovery to targeted assay development for biomarker verification Mol. Cell. Proteomics 2008, 7 (10) 1952-62
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.10 , pp. 1952-62
    • Jaffe, J.D.1    Keshishian, H.2    Chang, B.3    Addona, T.A.4    Gillette, M.A.5    Carr, S.A.6
  • 25
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • DOI 10.1038/nbt827
    • Zhang, H.; Li, X. J.; Martin, D. B.; Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat. Biotechnol. 2003, 21 (6) 660-6 (Pubitemid 36638093)
    • (2003) Nature Biotechnology , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aebersold, R.4
  • 26
    • 77950662044 scopus 로고    scopus 로고
    • Optimizing performance of glycopeptide capture for plasma proteomics
    • Berven, F. S.; Ahmad, R.; Clauser, K. R.; Carr, S. A. Optimizing performance of glycopeptide capture for plasma proteomics J. Proteome Res. 2010, 9 (4) 1706-15
    • (2010) J. Proteome Res. , vol.9 , Issue.4 , pp. 1706-15
    • Berven, F.S.1    Ahmad, R.2    Clauser, K.R.3    Carr, S.A.4
  • 27
    • 77951943188 scopus 로고    scopus 로고
    • Murine fecal proteomics: A model system for the detection of potential biomarkers for colorectal cancer
    • Ang, C. S.; Rothacker, J.; Patsiouras, H.; Burgess, A. W.; Nice, E. C. Murine fecal proteomics: A model system for the detection of potential biomarkers for colorectal cancer J. Chromatogr., A 2010, 1217 (15) 3330-40
    • (2010) J. Chromatogr., A , vol.1217 , Issue.15 , pp. 3330-40
    • Ang, C.S.1    Rothacker, J.2    Patsiouras, H.3    Burgess, A.W.4    Nice, E.C.5
  • 29
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • DOI 10.1074/mcp.M500061-MCP200
    • Ishihama, Y.; Oda, Y.; Tabata, T.; Sato, T.; Nagasu, T.; Rappsilber, J.; Mann, M. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein Mol. Cell. Proteomics 2005, 4 (9) 1265-72 (Pubitemid 41448714)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 30
    • 0034056940 scopus 로고    scopus 로고
    • The dynamic range of protein expression: A challenge for proteomic research
    • DOI 10.1002/(SICI)1522-2683(20000401)21:6<1104::AID-ELPS1104>3.0. CO;2-C
    • Corthals, G. L.; Wasinger, V. C.; Hochstrasser, D. F.; Sanchez, J. C. The dynamic range of protein expression: a challenge for proteomic research Electrophoresis 2000, 21 (6) 1104-15 (Pubitemid 30230776)
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1104-1115
    • Corthals, C.L.1    Wasinger, V.C.2    Hochstrasser, D.F.3    Sanchez, J.-C.4
  • 31
    • 33845902530 scopus 로고    scopus 로고
    • Overcoming the dynamic range problem in mass spectrometry-based shotgun proteomics
    • DOI 10.1586/14789450.3.6.611
    • Wu, L.; Han, D. K. Overcoming the dynamic range problem in mass spectrometry-based shotgun proteomics Expert Rev. Proteomics 2006, 3 (6) 611-9 (Pubitemid 46023440)
    • (2006) Expert Review of Proteomics , vol.3 , Issue.6 , pp. 611-619
    • Wu, L.1    Han, D.K.2
  • 32
    • 33745000741 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
    • DOI 10.1021/pr050492k
    • Ramachandran, P.; Boontheung, P.; Xie, Y.; Sondej, M.; Wong, D. T.; Loo, J. A. Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry J. Proteome Res. 2006, 5 (6) 1493-503 (Pubitemid 43865819)
    • (2006) Journal of Proteome Research , vol.5 , Issue.6 , pp. 1493-1503
    • Ramachandran, P.1    Boontheung, P.2    Xie, Y.3    Sondej, M.4    Wong, D.T.5    Loo, J.A.6
  • 33
    • 17844368916 scopus 로고    scopus 로고
    • Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry
    • DOI 10.1002/pmic.200401037
    • Hu, S.; Xie, Y.; Ramachandran, P.; Ogorzalek Loo, R. R.; Li, Y.; Loo, J. A.; Wong, D. T. Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry Proteomics 2005, 5 (6) 1714-28 (Pubitemid 40593277)
    • (2005) Proteomics , vol.5 , Issue.6 , pp. 1714-1728
    • Hu, S.1    Xie, Y.2    Ramachandran, P.3    Loo, R.R.O.4    Li, Y.5    Loo, J.A.6    Wong, D.T.7
  • 35
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, D. W.; Sherman, B. T.; Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources Nat. Protoc. 2008, 4 (1) 44-57
    • (2008) Nat. Protoc. , vol.4 , Issue.1 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 36
    • 33746218840 scopus 로고    scopus 로고
    • Prediction of protein subcellular localization
    • Yu, C. S.; Chen, Y. C.; Lu, C. H.; Hwang, J. K. Prediction of protein subcellular localization Proteins 2006, 64 (3) 643-51
    • (2006) Proteins , vol.64 , Issue.3 , pp. 643-51
    • Yu, C.S.1    Chen, Y.C.2    Lu, C.H.3    Hwang, J.K.4
  • 37
    • 77958540775 scopus 로고    scopus 로고
    • Comparative human salivary and plasma proteomes
    • Loo, J. A.; Yan, W.; Ramachandran, P.; Wong, D. T. Comparative human salivary and plasma proteomes J. Dent. Res. 2010, 89 (10) 1016-23
    • (2010) J. Dent. Res. , vol.89 , Issue.10 , pp. 1016-23
    • Loo, J.A.1    Yan, W.2    Ramachandran, P.3    Wong, D.T.4
  • 39
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 1999, 20 (18) 3551-67 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 42
    • 0023878299 scopus 로고
    • The covalent structure of individual N-linked glycopeptides from ovomucoid and asialofetuin
    • Yet, M. G.; Chin, C. C.; Wold, F. The covalent structure of individual N-linked glycopeptides from ovomucoid and asialofetuin J. Biol. Chem. 1988, 263 (1) 111-7
    • (1988) J. Biol. Chem. , vol.263 , Issue.1 , pp. 111-7
    • Yet, M.G.1    Chin, C.C.2    Wold, F.3
  • 43
    • 0026725328 scopus 로고
    • Complete primary structure of bovine beta 2-glycoprotein I: Localization of the disulfide bridges
    • Bendixen, E.; Halkier, T.; Magnusson, S.; Sottrup-Jensen, L.; Kristensen, T. Complete primary structure of bovine beta 2-glycoprotein I: localization of the disulfide bridges Biochemistry 1992, 31 (14) 3611-7
    • (1992) Biochemistry , vol.31 , Issue.14 , pp. 3611-7
    • Bendixen, E.1    Halkier, T.2    Magnusson, S.3    Sottrup-Jensen, L.4    Kristensen, T.5
  • 44
    • 0026348669 scopus 로고
    • Amino acid sequence and location of the disulfide bonds in bovine beta 2 glycoprotein I: The presence of five Sushi domains
    • Kato, H.; Enjyoji, K. Amino acid sequence and location of the disulfide bonds in bovine beta 2 glycoprotein I: the presence of five Sushi domains Biochemistry 1991, 30 (50) 11687-94
    • (1991) Biochemistry , vol.30 , Issue.50 , pp. 11687-94
    • Kato, H.1    Enjyoji, K.2
  • 45
    • 0025081307 scopus 로고
    • Identification of desmoglein, a constitutive desmosomal glycoprotein, as a member of the cadherin family of cell adhesion molecules
    • Koch, P. J.; Walsh, M. J.; Schmelz, M.; Goldschmidt, M. D.; Zimbelmann, R.; Franke, W. W. Identification of desmoglein, a constitutive desmosomal glycoprotein, as a member of the cadherin family of cell adhesion molecules Eur. J. Cell Biol. 1990, 53 (1) 1-12 (Pubitemid 20368179)
    • (1990) European Journal of Cell Biology , vol.53 , Issue.1 , pp. 1-12
    • Koch, P.J.1    Walsh, M.J.2    Schmelz, M.3    Goldschmidt, M.D.4    Zimbelmann, R.5    Franke, W.W.6
  • 46
    • 62149135362 scopus 로고    scopus 로고
    • Prediction of glycosylation sites using random forests
    • Hamby, S. E.; Hirst, J. D. Prediction of glycosylation sites using random forests BMC Bioinform. 2008, 9, 500
    • (2008) BMC Bioinform. , vol.9 , pp. 500
    • Hamby, S.E.1    Hirst, J.D.2
  • 47
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • Reis, C. A.; Osorio, H.; Silva, L.; Gomes, C.; David, L. Alterations in glycosylation as biomarkers for cancer detection J. Clin. Pathol. 2010, 63 (4) 322-9
    • (2010) J. Clin. Pathol. , vol.63 , Issue.4 , pp. 322-9
    • Reis, C.A.1    Osorio, H.2    Silva, L.3    Gomes, C.4    David, L.5
  • 48
    • 1642528831 scopus 로고    scopus 로고
    • Post-translational modifications and their biological functions: Proteomic analysis and systematic approaches
    • Seo, J.; Lee, K. J. Post-translational modifications and their biological functions: proteomic analysis and systematic approaches J. Biochem. Mol. Biol. 2004, 37 (1) 35-44 (Pubitemid 38402572)
    • (2004) Journal of Biochemistry and Molecular Biology , vol.37 , Issue.1 , pp. 35-44
    • Seo, J.1    Lee, K.-J.2
  • 49
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • Swaney, D. L.; McAlister, G. C.; Coon, J. J. Decision tree-driven tandem mass spectrometry for shotgun proteomics Nat. Methods 2008, 5 (11) 959-64
    • (2008) Nat. Methods , vol.5 , Issue.11 , pp. 959-64
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 52
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • DOI 10.1021/pr034112b
    • Hagglund, P.; Bunkenborg, J.; Elortza, F.; Jensen, O. N.; Roepstorff, P. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation J. Proteome Res. 2004, 3 (3) 556-66 (Pubitemid 39207360)
    • (2004) Journal of Proteome Research , vol.3 , Issue.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5


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