메뉴 건너뛰기




Volumn 95, Issue 2, 2012, Pages 567-579

Proteomic analysis and immunodetection of the bovine milk osteopontin isoforms

Author keywords

Dairy milk; Gene expression; Osteopontin; Posttranslational modifications

Indexed keywords

ANTIBODY; EPITOPE; ISOPROTEIN; MILK PROTEIN; OSTEOPONTIN; RECOMBINANT PROTEIN;

EID: 84856134583     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2011-4750     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 0023465103 scopus 로고
    • Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients
    • Abraham D.J., Leo A.J. Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients. Proteins 1987, 2:130-152.
    • (1987) Proteins , vol.2 , pp. 130-152
    • Abraham, D.J.1    Leo, A.J.2
  • 2
    • 0035958935 scopus 로고    scopus 로고
    • Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin)
    • Agnihotri R., Crawford H.C., Haro H., Matrisian L.M., Havrda M.C., Liaw L. Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin). J. Biol. Chem. 2001, 276:28261-28267.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28261-28267
    • Agnihotri, R.1    Crawford, H.C.2    Haro, H.3    Matrisian, L.M.4    Havrda, M.C.5    Liaw, L.6
  • 3
    • 70350451734 scopus 로고    scopus 로고
    • Osteopontin: An early innate immune marker of Escherichia coli mastitis harbors genetic polymorphisms with possible links with resistance to mastitis
    • Alain K., Karrow N.A., Thibault C., St-Pierre J., Lessard M., Bissonnette N. Osteopontin: An early innate immune marker of Escherichia coli mastitis harbors genetic polymorphisms with possible links with resistance to mastitis. BMC Genomics 2009, 10:444.
    • (2009) BMC Genomics , vol.10 , pp. 444
    • Alain, K.1    Karrow, N.A.2    Thibault, C.3    St-Pierre, J.4    Lessard, M.5    Bissonnette, N.6
  • 5
    • 0031127344 scopus 로고    scopus 로고
    • Isolation and biological properties of osteopontin from bovine milk
    • Bayless K.J., Davis G.E., Meininger G.A. Isolation and biological properties of osteopontin from bovine milk. Protein Expr. Purif. 1997, 9:309-314.
    • (1997) Protein Expr. Purif. , vol.9 , pp. 309-314
    • Bayless, K.J.1    Davis, G.E.2    Meininger, G.A.3
  • 6
    • 79251551713 scopus 로고    scopus 로고
    • TRAPing a new gene for autoimmunity
    • Behrens T.W., Graham R.R. TRAPing a new gene for autoimmunity. Nat. Genet. 2011, 43:90-91.
    • (2011) Nat. Genet. , vol.43 , pp. 90-91
    • Behrens, T.W.1    Graham, R.R.2
  • 7
    • 77949293734 scopus 로고    scopus 로고
    • Effect of milking frequency on lactation persistency and mammary gland remodeling in mid-lactation cows
    • Bernier-Dodier P., Delbecchi L., Wagner G.F., Talbot B.G., Lacasse P. Effect of milking frequency on lactation persistency and mammary gland remodeling in mid-lactation cows. J. Dairy Sci. 2010, 93:555-564.
    • (2010) J. Dairy Sci. , vol.93 , pp. 555-564
    • Bernier-Dodier, P.1    Delbecchi, L.2    Wagner, G.F.3    Talbot, B.G.4    Lacasse, P.5
  • 8
    • 0024780540 scopus 로고
    • The nature and significance of osteopontin
    • Butler W.T. The nature and significance of osteopontin. Connect. Tissue Res. 1989, 23:123-136.
    • (1989) Connect. Tissue Res. , vol.23 , pp. 123-136
    • Butler, W.T.1
  • 9
    • 79960924193 scopus 로고    scopus 로고
    • Transcriptome analysis of epithelial and stromal contributions to mammogenesis in three week prepartum cows
    • Casey T., Dover H., Liesman J., Devries L., Kiupel M., Vandehaar M., Plaut K. Transcriptome analysis of epithelial and stromal contributions to mammogenesis in three week prepartum cows. PLoS ONE 2011, 6:e22541.
    • (2011) PLoS ONE , vol.6
    • Casey, T.1    Dover, H.2    Liesman, J.3    Devries, L.4    Kiupel, M.5    Vandehaar, M.6    Plaut, K.7
  • 11
    • 73949146624 scopus 로고    scopus 로고
    • Osteopontin splice variants differentially modulate the migratory activity of hepatocellular carcinoma cell lines
    • Chae S., Jun H.O., Lee E.G., Yang S.J., Lee D.C., Jung J.K., Park K.C., Yeom Y.I., Kim K.W. Osteopontin splice variants differentially modulate the migratory activity of hepatocellular carcinoma cell lines. Int. J. Oncol. 2009, 35:1409-1416.
    • (2009) Int. J. Oncol. , vol.35 , pp. 1409-1416
    • Chae, S.1    Jun, H.O.2    Lee, E.G.3    Yang, S.J.4    Lee, D.C.5    Jung, J.K.6    Park, K.C.7    Yeom, Y.I.8    Kim, K.W.9
  • 12
    • 23944440915 scopus 로고    scopus 로고
    • Post-translationally modified residues of native human osteopontin are located in clusters: Identification of 36 phosphorylation and five O-glycosylation sites and their biological implications
    • Christensen B., Nielsen M.S., Haselmann K.F., Petersen T.E., Sorensen E.S. Post-translationally modified residues of native human osteopontin are located in clusters: Identification of 36 phosphorylation and five O-glycosylation sites and their biological implications. Biochem. J. 2005, 390:285-292.
    • (2005) Biochem. J. , vol.390 , pp. 285-292
    • Christensen, B.1    Nielsen, M.S.2    Haselmann, K.F.3    Petersen, T.E.4    Sorensen, E.S.5
  • 13
    • 0026642947 scopus 로고
    • Isolation and characterization of a cDNA for osteopontin-k: A kidney cell adhesion molecule with high homology to osteopontins
    • Crivello J.F., Delvin E. Isolation and characterization of a cDNA for osteopontin-k: A kidney cell adhesion molecule with high homology to osteopontins. J. Bone Miner. Res. 1992, 7:693-699.
    • (1992) J. Bone Miner. Res. , vol.7 , pp. 693-699
    • Crivello, J.F.1    Delvin, E.2
  • 14
    • 0028237439 scopus 로고
    • Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro
    • Ek-Rylander B., Flores M., Wendel M., Heinegard D., Andersson G. Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro. J. Biol. Chem. 1994, 269:14853-14856.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14853-14856
    • Ek-Rylander, B.1    Flores, M.2    Wendel, M.3    Heinegard, D.4    Andersson, G.5
  • 15
    • 0024713072 scopus 로고
    • Localization of the mouse gene for secreted phosphoprotein 1 (Spp-1) (2ar, osteopontin, bone sialoprotein 1, 44-kDa bone phosphoprotein, tumor-secreted phosphoprotein) to chromosome 5, closely linked to Ric (Rickettsia resistance)
    • Fet V., Dickinson M.E., Hogan B.L. Localization of the mouse gene for secreted phosphoprotein 1 (Spp-1) (2ar, osteopontin, bone sialoprotein 1, 44-kDa bone phosphoprotein, tumor-secreted phosphoprotein) to chromosome 5, closely linked to Ric (Rickettsia resistance). Genomics 1989, 5:375-377.
    • (1989) Genomics , vol.5 , pp. 375-377
    • Fet, V.1    Dickinson, M.E.2    Hogan, B.L.3
  • 16
    • 33645743036 scopus 로고    scopus 로고
    • An osteopontin splice variant induces anchorage independence in human breast cancer cells
    • He B., Mirza M., Weber G.F. An osteopontin splice variant induces anchorage independence in human breast cancer cells. Oncogene 2006, 25:2192-2202.
    • (2006) Oncogene , vol.25 , pp. 2192-2202
    • He, B.1    Mirza, M.2    Weber, G.F.3
  • 17
    • 0034963551 scopus 로고    scopus 로고
    • Phosphorylated osteopontin peptides suppress crystallization by inhibiting the growth of calcium oxalate crystals
    • Hoyer J.R., Asplin J.R., Otvos L. Phosphorylated osteopontin peptides suppress crystallization by inhibiting the growth of calcium oxalate crystals. Kidney Int. 2001, 60:77-82.
    • (2001) Kidney Int. , vol.60 , pp. 77-82
    • Hoyer, J.R.1    Asplin, J.R.2    Otvos, L.3
  • 18
    • 77953946508 scopus 로고    scopus 로고
    • A large-scale study of differential gene expression in monocyte-derived macrophages infected with several strains of Mycobacterium avium subspecies paratuberculosis
    • Kabara E., Kloss C.C., Wilson M., Tempelman R.J., Sreevatsan S., Janagama H., Coussens P.M. A large-scale study of differential gene expression in monocyte-derived macrophages infected with several strains of Mycobacterium avium subspecies paratuberculosis. Brief. Funct. Genomics 2010, 9:220-237.
    • (2010) Brief. Funct. Genomics , vol.9 , pp. 220-237
    • Kabara, E.1    Kloss, C.C.2    Wilson, M.3    Tempelman, R.J.4    Sreevatsan, S.5    Janagama, H.6    Coussens, P.M.7
  • 19
    • 35648934023 scopus 로고    scopus 로고
    • Control of osteopontin signaling and function by post-translational phosphorylation and protein folding
    • Kazanecki C.C., Uzwiak D.J., Denhardt D.T. Control of osteopontin signaling and function by post-translational phosphorylation and protein folding. J. Cell. Biochem. 2007, 102:912-924.
    • (2007) J. Cell. Biochem. , vol.102 , pp. 912-924
    • Kazanecki, C.C.1    Uzwiak, D.J.2    Denhardt, D.T.3
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 70349902884 scopus 로고    scopus 로고
    • Overexpression of human osteopontin increases cell proliferation and migration in human embryo kidney-293 cells
    • Liu Y.J., Zhang D.Q., Sui X.M., Tian W. Overexpression of human osteopontin increases cell proliferation and migration in human embryo kidney-293 cells. Cell. Mol. Biol. Lett. 2009, 14:670-678.
    • (2009) Cell. Mol. Biol. Lett. , vol.14 , pp. 670-678
    • Liu, Y.J.1    Zhang, D.Q.2    Sui, X.M.3    Tian, W.4
  • 27
    • 0030029816 scopus 로고    scopus 로고
    • Secretion of osteopontin by macrophages and its accumulation at tissue surfaces during wound healing in mineralized tissues: A potential requirement for macrophage adhesion and phagocytosis
    • McKee M.D., Nanci A. Secretion of osteopontin by macrophages and its accumulation at tissue surfaces during wound healing in mineralized tissues: A potential requirement for macrophage adhesion and phagocytosis. Anat. Rec. 1996, 245:394-409.
    • (1996) Anat. Rec. , vol.245 , pp. 394-409
    • McKee, M.D.1    Nanci, A.2
  • 29
    • 4644222082 scopus 로고    scopus 로고
    • Microarray analysis of human milk cells: Persistent high expression of osteopontin during the lactation period
    • Nagatomo T., Ohga S., Takada H., Nomura A., Hikino S., Imura M., Ohshima K., Hara T. Microarray analysis of human milk cells: Persistent high expression of osteopontin during the lactation period. Clin. Exp. Immunol. 2004, 138:47-53.
    • (2004) Clin. Exp. Immunol. , vol.138 , pp. 47-53
    • Nagatomo, T.1    Ohga, S.2    Takada, H.3    Nomura, A.4    Hikino, S.5    Imura, M.6    Ohshima, K.7    Hara, T.8
  • 31
    • 40349103655 scopus 로고    scopus 로고
    • Development of fragment-specific osteopontin antibodies and ELISA for quantification in human metastatic breast cancer
    • Plumer A., Duan H., Subramaniam S., Lucas F.L., Miesfeldt S., Ng A.K., Liaw L. Development of fragment-specific osteopontin antibodies and ELISA for quantification in human metastatic breast cancer. BMC Cancer 2008, 8:38.
    • (2008) BMC Cancer , vol.8 , pp. 38
    • Plumer, A.1    Duan, H.2    Subramaniam, S.3    Lucas, F.L.4    Miesfeldt, S.5    Ng, A.K.6    Liaw, L.7
  • 32
    • 78049264738 scopus 로고    scopus 로고
    • Interface between hemostasis and adaptive immunity
    • Qu Z., Chaikof E.L. Interface between hemostasis and adaptive immunity. Curr. Opin. Immunol. 2010, 22:634-642.
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 634-642
    • Qu, Z.1    Chaikof, E.L.2
  • 33
    • 8844258021 scopus 로고    scopus 로고
    • Differential effect of bicycling exercise intensity on activity and phosphorylation of atypical protein kinase C and extracellular signal-regulated protein kinase in skeletal muscle
    • Richter E.A., Vistisen B., Maarbjerg S.J., Sajan M., Farese R.V., Kiens B. Differential effect of bicycling exercise intensity on activity and phosphorylation of atypical protein kinase C and extracellular signal-regulated protein kinase in skeletal muscle. J. Physiol. 2004, 560:909-918.
    • (2004) J. Physiol. , vol.560 , pp. 909-918
    • Richter, E.A.1    Vistisen, B.2    Maarbjerg, S.J.3    Sajan, M.4    Farese, R.V.5    Kiens, B.6
  • 34
    • 0024278757 scopus 로고
    • Hydrophobicity of the peptide C=O...H-N hydrogen-bonded group
    • Roseman M.A. Hydrophobicity of the peptide C=O...H-N hydrogen-bonded group. J. Mol. Biol. 1988, 201:621-623.
    • (1988) J. Mol. Biol. , vol.201 , pp. 621-623
    • Roseman, M.A.1
  • 35
    • 78751690182 scopus 로고    scopus 로고
    • Osteopontin: Correlation with phagocytosis by brain macrophages in a rat model of stroke
    • Shin Y.J., Lim Kim H., Choi J.S., Choi J.Y., Cha J.H., Lee M.Y. Osteopontin: Correlation with phagocytosis by brain macrophages in a rat model of stroke. Glia 2010, 59:413-423.
    • (2010) Glia , vol.59 , pp. 413-423
    • Shin, Y.J.1    Lim Kim, H.2    Choi, J.S.3    Choi, J.Y.4    Cha, J.H.5    Lee, M.Y.6
  • 36
    • 44449131554 scopus 로고    scopus 로고
    • Alternative translation of osteopontin generates intracellular and secreted isoforms that mediate distinct biological activities in dendritic cells
    • Shinohara M.L., Kim H.J., Kim J.H., Garcia V.A., Cantor H. Alternative translation of osteopontin generates intracellular and secreted isoforms that mediate distinct biological activities in dendritic cells. Proc. Natl. Acad. Sci. USA 2008, 105:7235-7239.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7235-7239
    • Shinohara, M.L.1    Kim, H.J.2    Kim, J.H.3    Garcia, V.A.4    Cantor, H.5
  • 37
    • 0028875692 scopus 로고
    • Posttranslational modifications of bovine osteopontin: Identification of twenty-eight phosphorylation and three O-glycosylation sites
    • Sørensen E.S., Hojrup P., Petersen T.E. Posttranslational modifications of bovine osteopontin: Identification of twenty-eight phosphorylation and three O-glycosylation sites. Protein Sci. 1995, 4:2040-2049.
    • (1995) Protein Sci. , vol.4 , pp. 2040-2049
    • Sørensen, E.S.1    Hojrup, P.2    Petersen, T.E.3
  • 38
    • 0027688018 scopus 로고
    • Phosphorylation, glycosylation and amino acid sequence of component PP3 from the proteose peptone fraction of bovine milk
    • Sørensen E.S., Petersen T.E. Phosphorylation, glycosylation and amino acid sequence of component PP3 from the proteose peptone fraction of bovine milk. J. Dairy Res. 1993, 60:535-542.
    • (1993) J. Dairy Res. , vol.60 , pp. 535-542
    • Sørensen, E.S.1    Petersen, T.E.2
  • 39
    • 0011175654 scopus 로고
    • Purification and characterization of three proteins isolated from the proteose peptone fraction of bovine milk
    • Sørensen E.S., Petersen T.E. Purification and characterization of three proteins isolated from the proteose peptone fraction of bovine milk. J. Dairy Res. 1993, 60:189-197.
    • (1993) J. Dairy Res. , vol.60 , pp. 189-197
    • Sørensen, E.S.1    Petersen, T.E.2
  • 41
    • 34547885530 scopus 로고    scopus 로고
    • An osteopontin fragment is essential for tumor cell invasion in hepatocellular carcinoma
    • Takafuji V., Forgues M., Unsworth E., Goldsmith P., Wang X.W. An osteopontin fragment is essential for tumor cell invasion in hepatocellular carcinoma. Oncogene 2007, 26:6361-6371.
    • (2007) Oncogene , vol.26 , pp. 6361-6371
    • Takafuji, V.1    Forgues, M.2    Unsworth, E.3    Goldsmith, P.4    Wang, X.W.5
  • 43
    • 57049166456 scopus 로고    scopus 로고
    • Osteopontin: Role in immune regulation and stress responses
    • Wang K.X., Denhardt D.T. Osteopontin: Role in immune regulation and stress responses. Cytokine Growth Factor Rev. 2008, 19:333-345.
    • (2008) Cytokine Growth Factor Rev. , vol.19 , pp. 333-345
    • Wang, K.X.1    Denhardt, D.T.2
  • 45
    • 20244386058 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation
    • Weber G.F., Zawaideh S., Hikita S., Kumar V.A., Cantor H., Ashkar S. Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation. J. Leukoc. Biol. 2002, 72:752-761.
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 752-761
    • Weber, G.F.1    Zawaideh, S.2    Hikita, S.3    Kumar, V.A.4    Cantor, H.5    Ashkar, S.6
  • 46
    • 0035688758 scopus 로고    scopus 로고
    • Synthesis and processing of bone sialoproteins during de novo bone formation in vitro
    • Zhu X.L., Ganss B., Goldberg H.A., Sodek J. Synthesis and processing of bone sialoproteins during de novo bone formation in vitro. Biochem. Cell Biol. 2001, 79:737-746.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 737-746
    • Zhu, X.L.1    Ganss, B.2    Goldberg, H.A.3    Sodek, J.4
  • 47
    • 0031013634 scopus 로고    scopus 로고
    • Single cell analysis of intracellular osteopontin in osteogenic cultures of fetal rat calvarial cells
    • Zohar R., Lee W., Arora P., Cheifetz S., McCulloch C., Sodek J. Single cell analysis of intracellular osteopontin in osteogenic cultures of fetal rat calvarial cells. J. Cell. Physiol. 1997, 170:88-100.
    • (1997) J. Cell. Physiol. , vol.170 , pp. 88-100
    • Zohar, R.1    Lee, W.2    Arora, P.3    Cheifetz, S.4    McCulloch, C.5    Sodek, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.