메뉴 건너뛰기




Volumn 82, Issue , 2013, Pages 141-154

Bovine milk proteome: Quantitative changes in normal milk exosomes, milk fat globule membranes and whey proteomes resulting from Staphylococcus aureus mastitis

Author keywords

Exosome; Mastitis; MFGM; Milk proteome; Neutrophil extracellular traps; Whey

Indexed keywords

AMYLOID A PROTEIN; MILK FAT; MILK PROTEIN;

EID: 84875798802     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.02.013     Document Type: Article
Times cited : (158)

References (52)
  • 1
    • 0019525766 scopus 로고
    • Review of the progress of dairy science: bovine mastitis: milk compositional changes and related diagnostic tests
    • Kitchen B.J. Review of the progress of dairy science: bovine mastitis: milk compositional changes and related diagnostic tests. J Dairy Res 1981, 48:167-188.
    • (1981) J Dairy Res , vol.48 , pp. 167-188
    • Kitchen, B.J.1
  • 2
    • 33645227813 scopus 로고    scopus 로고
    • Influence of raw milk quality on fluid milk shelf life
    • Barbano D.M., Ma Y., Santos M.V. Influence of raw milk quality on fluid milk shelf life. J Dairy Sci 2006, 89(Suppl. 1):E15-E19.
    • (2006) J Dairy Sci , vol.89 , Issue.SUPPL. 1
    • Barbano, D.M.1    Ma, Y.2    Santos, M.V.3
  • 3
    • 80054879140 scopus 로고    scopus 로고
    • Effect of storage and separation of milk at udder quarter level on milk composition, proteolysis, and coagulation properties in relation to somatic cell count
    • Forsback L., Lindmark-Mansson H., Svennersten-Sjaunja K., Bach Larsen L., Andren A. Effect of storage and separation of milk at udder quarter level on milk composition, proteolysis, and coagulation properties in relation to somatic cell count. J Dairy Sci 2011, 94:5341-5349.
    • (2011) J Dairy Sci , vol.94 , pp. 5341-5349
    • Forsback, L.1    Lindmark-Mansson, H.2    Svennersten-Sjaunja, K.3    Bach Larsen, L.4    Andren, A.5
  • 4
    • 77951258396 scopus 로고    scopus 로고
    • Evaluation of quality changes in udder quarter milk from cows with low-to-moderate somatic cell counts
    • Forsback L., Lindmark-Mansson H., Andren A., Svennersten-Sjaunja K. Evaluation of quality changes in udder quarter milk from cows with low-to-moderate somatic cell counts. Animal 2010, 4:617-626.
    • (2010) Animal , vol.4 , pp. 617-626
    • Forsback, L.1    Lindmark-Mansson, H.2    Andren, A.3    Svennersten-Sjaunja, K.4
  • 5
    • 78650304824 scopus 로고    scopus 로고
    • The proteomic advantage: label-free quantification of proteins expressed in bovine milk during experimentally induced coliform mastitis
    • Boehmer J.L., DeGrasse J.A., McFarland M.A., Tall E.A., Shefcheck K.J., Ward J.L., et al. The proteomic advantage: label-free quantification of proteins expressed in bovine milk during experimentally induced coliform mastitis. Vet Immunol Immunopathol 2010, 138:252-266.
    • (2010) Vet Immunol Immunopathol , vol.138 , pp. 252-266
    • Boehmer, J.L.1    DeGrasse, J.A.2    McFarland, M.A.3    Tall, E.A.4    Shefcheck, K.J.5    Ward, J.L.6
  • 6
    • 84855706363 scopus 로고    scopus 로고
    • Mastitis and its impact on structure and function in the ruminant mammary gland
    • Akers R.M., Nickerson S.C. Mastitis and its impact on structure and function in the ruminant mammary gland. J Mammary Gland Biol Neoplasia 2011, 16:275-289.
    • (2011) J Mammary Gland Biol Neoplasia , vol.16 , pp. 275-289
    • Akers, R.M.1    Nickerson, S.C.2
  • 8
    • 84855691564 scopus 로고    scopus 로고
    • Proteomic analyses of host and pathogen responses during bovine mastitis
    • Boehmer J.L. Proteomic analyses of host and pathogen responses during bovine mastitis. J Mammary Gland Biol Neoplasia 2011, 16:323-338.
    • (2011) J Mammary Gland Biol Neoplasia , vol.16 , pp. 323-338
    • Boehmer, J.L.1
  • 10
    • 33750362923 scopus 로고    scopus 로고
    • Bovine milk fat globule membrane proteome
    • Reinhardt T.A., Lippolis J.D. Bovine milk fat globule membrane proteome. J Dairy Res 2006, 73:406-416.
    • (2006) J Dairy Res , vol.73 , pp. 406-416
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 12
    • 77950517341 scopus 로고    scopus 로고
    • Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome
    • Affolter M., Grass L., Vanrobaeys F., Casado B., Kussmann M. Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome. J Proteomics 2010, 73:1079-1088.
    • (2010) J Proteomics , vol.73 , pp. 1079-1088
    • Affolter, M.1    Grass, L.2    Vanrobaeys, F.3    Casado, B.4    Kussmann, M.5
  • 14
    • 33645670516 scopus 로고    scopus 로고
    • Human colostrum: identification of minor proteins in the aqueous phase by proteomics
    • Palmer D.J., Kelly V.C., Smit A.M., Kuy S., Knight C.G., Cooper G.J. Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 2006, 6:2208-2216.
    • (2006) Proteomics , vol.6 , pp. 2208-2216
    • Palmer, D.J.1    Kelly, V.C.2    Smit, A.M.3    Kuy, S.4    Knight, C.G.5    Cooper, G.J.6
  • 15
    • 68549140373 scopus 로고    scopus 로고
    • In-depth exploration of cow's whey proteome via combinatorial peptide ligand libraries
    • D'Amato A., Bachi A., Fasoli E., Boschetti E., Peltre G., Senechal H., et al. In-depth exploration of cow's whey proteome via combinatorial peptide ligand libraries. J Proteome Res 2009, 8:3925-3936.
    • (2009) J Proteome Res , vol.8 , pp. 3925-3936
    • D'Amato, A.1    Bachi, A.2    Fasoli, E.3    Boschetti, E.4    Peltre, G.5    Senechal, H.6
  • 16
    • 44949253954 scopus 로고    scopus 로고
    • Developmental changes in the milk fat globule membrane proteome during the transition from colostrum to milk
    • Reinhardt T.A., Lippolis J.D. Developmental changes in the milk fat globule membrane proteome during the transition from colostrum to milk. J Dairy Sci 2008, 91:2307-2318.
    • (2008) J Dairy Sci , vol.91 , pp. 2307-2318
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 17
    • 79953697144 scopus 로고    scopus 로고
    • Proteomic characterization of human milk whey proteins during a twelve-month lactation period
    • Liao Y., Alvarado R., Phinney B., Lonnerdal B. Proteomic characterization of human milk whey proteins during a twelve-month lactation period. J Proteome Res 2011, 10:1746-1754.
    • (2011) J Proteome Res , vol.10 , pp. 1746-1754
    • Liao, Y.1    Alvarado, R.2    Phinney, B.3    Lonnerdal, B.4
  • 18
    • 33846623696 scopus 로고    scopus 로고
    • Characterisation of host defence proteins in milk using a proteomic approach
    • Smolenski G., Haines S., Kwan F.Y., Bond J., Farr V., Davis S.R., et al. Characterisation of host defence proteins in milk using a proteomic approach. J Proteome Res 2007, 6:207-215.
    • (2007) J Proteome Res , vol.6 , pp. 207-215
    • Smolenski, G.1    Haines, S.2    Kwan, F.Y.3    Bond, J.4    Farr, V.5    Davis, S.R.6
  • 19
    • 77956320469 scopus 로고    scopus 로고
    • Proteomics, genomics, and pathway analyses of Escherichia coli and Staphylococcus aureus infected milk whey reveal molecular pathways and networks involved in mastitis
    • Ibeagha-Awemu E.M., Ibeagha A.E., Messier S., Zhao X. Proteomics, genomics, and pathway analyses of Escherichia coli and Staphylococcus aureus infected milk whey reveal molecular pathways and networks involved in mastitis. J Proteome Res 2010, 9:4604-4619.
    • (2010) J Proteome Res , vol.9 , pp. 4604-4619
    • Ibeagha-Awemu, E.M.1    Ibeagha, A.E.2    Messier, S.3    Zhao, X.4
  • 20
    • 77953855865 scopus 로고    scopus 로고
    • Quantitative milk proteomics-host responses to lipopolysaccharide-mediated inflammation of bovine mammary gland
    • Danielsen M., Codrea M.C., Ingvartsen K.L., Friggens N.C., Bendixen E., Rontved C.M. Quantitative milk proteomics-host responses to lipopolysaccharide-mediated inflammation of bovine mammary gland. Proteomics 2010, 10:2240-2249.
    • (2010) Proteomics , vol.10 , pp. 2240-2249
    • Danielsen, M.1    Codrea, M.C.2    Ingvartsen, K.L.3    Friggens, N.C.4    Bendixen, E.5    Rontved, C.M.6
  • 21
    • 80052306116 scopus 로고    scopus 로고
    • Proteomics and pathway analyses of the milk fat globule in sheep naturally infected by Mycoplasma agalactiae provide indications of the in vivo response of the mammary epithelium to bacterial infection
    • Addis M.F., Pisanu S., Ghisaura S., Pagnozzi D., Marogna G., Tanca A., et al. Proteomics and pathway analyses of the milk fat globule in sheep naturally infected by Mycoplasma agalactiae provide indications of the in vivo response of the mammary epithelium to bacterial infection. Infect Immun 2011, 79:3833-3845.
    • (2011) Infect Immun , vol.79 , pp. 3833-3845
    • Addis, M.F.1    Pisanu, S.2    Ghisaura, S.3    Pagnozzi, D.4    Marogna, G.5    Tanca, A.6
  • 22
    • 79951640840 scopus 로고    scopus 로고
    • The bovine milk proteome: cherishing, nourishing and fostering molecular complexity. An interactomics and functional overview
    • D'Alessandro A., Zolla L., Scaloni A. The bovine milk proteome: cherishing, nourishing and fostering molecular complexity. An interactomics and functional overview. Mol Biosyst 2011, 7:579-597.
    • (2011) Mol Biosyst , vol.7 , pp. 579-597
    • D'Alessandro, A.1    Zolla, L.2    Scaloni, A.3
  • 24
    • 79955765955 scopus 로고    scopus 로고
    • Developmental regulation of mitochondrial biogenesis and function in the mouse mammary gland during a prolonged lactation cycle
    • Hadsell D.L., Olea W., Wei J., Fiorotto M.L., Matsunami R.K., Engler D.A., et al. Developmental regulation of mitochondrial biogenesis and function in the mouse mammary gland during a prolonged lactation cycle. Physiol Genomics 2011, 43:271-285.
    • (2011) Physiol Genomics , vol.43 , pp. 271-285
    • Hadsell, D.L.1    Olea, W.2    Wei, J.3    Fiorotto, M.L.4    Matsunami, R.K.5    Engler, D.A.6
  • 25
    • 33746279643 scopus 로고    scopus 로고
    • Neutrophil extracellular trap formation by bovine neutrophils is not inhibited by milk
    • Lippolis J.D., Reinhardt T.A., Goff J.P., Horst R.L. Neutrophil extracellular trap formation by bovine neutrophils is not inhibited by milk. Vet Immunol Immunopathol 2006, 113:248-255.
    • (2006) Vet Immunol Immunopathol , vol.113 , pp. 248-255
    • Lippolis, J.D.1    Reinhardt, T.A.2    Goff, J.P.3    Horst, R.L.4
  • 27
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J Cell Biol 1982, 93:97-102.
    • (1982) J Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 28
    • 43049130709 scopus 로고    scopus 로고
    • Sodium-deoxycholate-assisted tryptic digestion and identification of proteolytically resistant proteins
    • Lin Y., Zhou J., Bi D., Chen P., Wang X., Liang S. Sodium-deoxycholate-assisted tryptic digestion and identification of proteolytically resistant proteins. Anal Biochem 2008, 377:259-266.
    • (2008) Anal Biochem , vol.377 , pp. 259-266
    • Lin, Y.1    Zhou, J.2    Bi, D.3    Chen, P.4    Wang, X.5    Liang, S.6
  • 29
    • 36348936820 scopus 로고    scopus 로고
    • Two-dimensional reversed-phase x ion-pair reversed-phase HPLC: an alternative approach to high-resolution peptide separation for shotgun proteome analysis
    • Delmotte N., Lasaosa M., Tholey A., Heinzle E., Huber C.G. Two-dimensional reversed-phase x ion-pair reversed-phase HPLC: an alternative approach to high-resolution peptide separation for shotgun proteome analysis. J Proteome Res 2007, 6:4363-4373.
    • (2007) J Proteome Res , vol.6 , pp. 4363-4373
    • Delmotte, N.1    Lasaosa, M.2    Tholey, A.3    Heinzle, E.4    Huber, C.G.5
  • 30
    • 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, 74:5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 31
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., Keller A., Kolker E., Aebersold R. A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 2003, 75:4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 32
    • 27744450286 scopus 로고    scopus 로고
    • Bessant C. i-Tracker: for quantitative proteomics using iTRAQ
    • Shadforth I.P., Dunkley T.P., Lilley K.S. Bessant C. i-Tracker: for quantitative proteomics using iTRAQ. BMC Genomics 2005, 6:145.
    • (2005) BMC Genomics , vol.6 , pp. 145
    • Shadforth, I.P.1    Dunkley, T.P.2    Lilley, K.S.3
  • 35
    • 0037541161 scopus 로고    scopus 로고
    • Serum biomarkers of hepatitis B virus infected liver inflammation: a proteomic study
    • He Q.Y., Lau G.K., Zhou Y., Yuen S.T., Lin M.C., Kung H.F., et al. Serum biomarkers of hepatitis B virus infected liver inflammation: a proteomic study. Proteomics 2003, 3:666-674.
    • (2003) Proteomics , vol.3 , pp. 666-674
    • He, Q.Y.1    Lau, G.K.2    Zhou, Y.3    Yuen, S.T.4    Lin, M.C.5    Kung, H.F.6
  • 36
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W., Sherman B.T., Lempicki R.A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 2009, 4:44-57.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 37
    • 34547589578 scopus 로고    scopus 로고
    • DAVID bioinformatics resources: expanded annotation database and novel algorithms to better extract biology from large gene lists
    • Huang da W., Sherman B.T., Tan Q., Kir J., Liu D., Bryant D., et al. DAVID bioinformatics resources: expanded annotation database and novel algorithms to better extract biology from large gene lists. Nucleic Acids Res 2007, 35:W169-W175.
    • (2007) Nucleic Acids Res , vol.35
    • Huang da, W.1    Sherman, B.T.2    Tan, Q.3    Kir, J.4    Liu, D.5    Bryant, D.6
  • 39
    • 0242575194 scopus 로고    scopus 로고
    • The bovine neutrophil: structure and function in blood and milk
    • Paape M.J., Bannerman D.D., Zhao X., Lee J.W. The bovine neutrophil: structure and function in blood and milk. Vet Res 2003, 34:597-627.
    • (2003) Vet Res , vol.34 , pp. 597-627
    • Paape, M.J.1    Bannerman, D.D.2    Zhao, X.3    Lee, J.W.4
  • 40
    • 84860140596 scopus 로고    scopus 로고
    • Proteomic study of proteolysis during ripening of Cheddar cheese made from milk over a lactation cycle
    • Hinz K., O'Connor P.M., O'Brien B., Huppertz T., Ross R.P., Kelly A.L. Proteomic study of proteolysis during ripening of Cheddar cheese made from milk over a lactation cycle. J Dairy Res 2012, 79:176-184.
    • (2012) J Dairy Res , vol.79 , pp. 176-184
    • Hinz, K.1    O'Connor, P.M.2    O'Brien, B.3    Huppertz, T.4    Ross, R.P.5    Kelly, A.L.6
  • 41
    • 84864532433 scopus 로고    scopus 로고
    • Protein degradation in bovine milk caused by Streptococcus agalactiae
    • Akerstedt M., Wredle E., Lam V., Johansson M. Protein degradation in bovine milk caused by Streptococcus agalactiae. J Dairy Res 2012, 79:297-303.
    • (2012) J Dairy Res , vol.79 , pp. 297-303
    • Akerstedt, M.1    Wredle, E.2    Lam, V.3    Johansson, M.4
  • 42
    • 33746869286 scopus 로고    scopus 로고
    • Effect of protein composition on the cheese-making properties of milk from individual dairy cows
    • Wedholm A., Larsen L.B., Lindmark-Mansson H., Karlsson A.H., Andren A. Effect of protein composition on the cheese-making properties of milk from individual dairy cows. J Dairy Sci 2006, 89:3296-3305.
    • (2006) J Dairy Sci , vol.89 , pp. 3296-3305
    • Wedholm, A.1    Larsen, L.B.2    Lindmark-Mansson, H.3    Karlsson, A.H.4    Andren, A.5
  • 43
  • 44
    • 84863819823 scopus 로고    scopus 로고
    • Proteomics of inflammatory and oxidative stress response in cows with subclinical and clinical mastitis
    • Turk R., Piras C., Kovacic M., Samardzija M., Ahmed H., De Canio M., et al. Proteomics of inflammatory and oxidative stress response in cows with subclinical and clinical mastitis. J Proteomics 2012, 75:4412-4428.
    • (2012) J Proteomics , vol.75 , pp. 4412-4428
    • Turk, R.1    Piras, C.2    Kovacic, M.3    Samardzija, M.4    Ahmed, H.5    De Canio, M.6
  • 45
    • 71549117271 scopus 로고    scopus 로고
    • Gene network and pathway analysis of bovine mammary tissue challenged with Streptococcus uberis reveals induction of cell proliferation and inhibition of PPARgamma signaling as potential mechanism for the negative relationships between immune response and lipid metabolism
    • Moyes K.M., Drackley J.K., Morin D.E., Bionaz M., Rodriguez-Zas S.L., Everts R.E., et al. Gene network and pathway analysis of bovine mammary tissue challenged with Streptococcus uberis reveals induction of cell proliferation and inhibition of PPARgamma signaling as potential mechanism for the negative relationships between immune response and lipid metabolism. BMC Genomics 2009, 10:542.
    • (2009) BMC Genomics , vol.10 , pp. 542
    • Moyes, K.M.1    Drackley, J.K.2    Morin, D.E.3    Bionaz, M.4    Rodriguez-Zas, S.L.5    Everts, R.E.6
  • 46
    • 84855659425 scopus 로고    scopus 로고
    • Functional adaptations of the transcriptome to mastitis-causing pathogens: the mammary gland and beyond
    • Loor J.J., Moyes K.M., Bionaz M. Functional adaptations of the transcriptome to mastitis-causing pathogens: the mammary gland and beyond. J Mammary Gland Biol Neoplasia 2011, 16:305-322.
    • (2011) J Mammary Gland Biol Neoplasia , vol.16 , pp. 305-322
    • Loor, J.J.1    Moyes, K.M.2    Bionaz, M.3
  • 48
    • 73649099522 scopus 로고    scopus 로고
    • Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans
    • Urban C.F., Ermert D., Schmid M., Abu-Abed U., Goosmann C., Nacken W., et al. Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans. PLoS Pathog 2009, 5:e1000639.
    • (2009) PLoS Pathog , vol.5
    • Urban, C.F.1    Ermert, D.2    Schmid, M.3    Abu-Abed, U.4    Goosmann, C.5    Nacken, W.6
  • 50
    • 77950262727 scopus 로고    scopus 로고
    • Broad-spectrum activity against bacterial mastitis pathogens and activation of mammary epithelial cells support a protective role of neutrophil cathelicidins in bovine mastitis
    • Tomasinsig L., De Conti G., Skerlavaj B., Piccinini R., Mazzilli M., D'Este F., et al. Broad-spectrum activity against bacterial mastitis pathogens and activation of mammary epithelial cells support a protective role of neutrophil cathelicidins in bovine mastitis. Infect Immun 2010, 78:1781-1788.
    • (2010) Infect Immun , vol.78 , pp. 1781-1788
    • Tomasinsig, L.1    De Conti, G.2    Skerlavaj, B.3    Piccinini, R.4    Mazzilli, M.5    D'Este, F.6
  • 51
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol 2004, 75:39-48.
    • (2004) J Leukoc Biol , vol.75 , pp. 39-48
    • Zanetti, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.