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Volumn 15, Issue 1-2, 2011, Pages 83-90

Characterization of phosphoproteins in gastric cancer secretome

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; HYPOCALCIN; LIPOCORTIN 2; PHOSPHOPROTEIN; STANNIOCALCIN 2; UNCLASSIFIED DRUG;

EID: 79551536439     PISSN: 15362310     EISSN: None     Source Type: Journal    
DOI: 10.1089/omi.2010.0056     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 50049110046 scopus 로고    scopus 로고
    • Characterization of the human cerebrospinal fluid phosphoproteome by titanium dioxide affinity chromatography and mass spectrometry
    • Bahl, J.M.C., Jensen, S.S., Larsen, M.R., and Heegaard, N.H.H. (2008). Characterization of the human cerebrospinal fluid phosphoproteome by titanium dioxide affinity chromatography and mass spectrometry. Anal Chem 80, 6308-6316.
    • (2008) Anal. Chem. , vol.80 , pp. 6308-6316
    • Bahl, J.M.C.1    Jensen, S.S.2    Larsen, M.R.3    Heegaard, N.H.H.4
  • 5
    • 70349973075 scopus 로고    scopus 로고
    • Quantitative mitochondrial phosphoproteomics using iTRAQ on an LTQ-orbitrap with high energy collision dissociation
    • Boja, E.S., Phillips, D., French, S.A., Harris, R.A., and Balaban, R.S. (2009). Quantitative mitochondrial phosphoproteomics using iTRAQ on an LTQ-orbitrap with high energy collision dissociation. J Proteome Res 8, 4665-4675.
    • (2009) J. Proteome. Res. , vol.8 , pp. 4665-4675
    • Boja, E.S.1    Phillips, D.2    French, S.A.3    Harris, R.A.4    Balaban, R.S.5
  • 6
    • 34047150710 scopus 로고    scopus 로고
    • Modifications of the fibroblast growth factor-2 gene led to a marked enhancement in secretion and stability of the recombinant fibroblast growth factor-2 protein
    • Chen, S.T., Gysin, R., Kapur, S., Baylink, D.J., and Lau, K.H.W. (2007). Modifications of the fibroblast growth factor-2 gene led to a marked enhancement in secretion and stability of the recombinant fibroblast growth factor-2 protein. J Cell Biochem 100, 1493-1508.
    • (2007) J. Cell. Biochem. , vol.100 , pp. 1493-1508
    • Chen, S.T.1    Gysin, R.2    Kapur, S.3    Baylink, D.J.4    Lau, K.H.W.5
  • 7
    • 34250303532 scopus 로고    scopus 로고
    • Toward a better analysis of secreted proteins: The example of the myeloid cells secretome
    • Chevallet, M., Diemer, H., Van Dorssealer, A., Villiers, C., and Rabilloud, T. (2007). Toward a better analysis of secreted proteins: the example of the myeloid cells secretome. Proteomics 7, 1757-1770.
    • (2007) Proteomics , vol.7 , pp. 1757-1770
    • Chevallet, M.1    Diemer, H.2    Van Dorssealer, A.3    Villiers, C.4    Rabilloud, T.5
  • 8
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular-matrix and for a novel secretory mechanism
    • Cooper, D.N.W., and Barondes, S.H. (1990). Evidence for export of a muscle lectin from cytosol to extracellular-matrix and for a novel secretory mechanism. J Cell Biol 110, 1681-1691.
    • (1990) J. Cell. Biol. , vol.110 , pp. 1681-1691
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 9
    • 0347481133 scopus 로고    scopus 로고
    • Nonclassical secretion of annexin A2 to the lumenal side of the enterocyte brush border membrane
    • Danielsen, E.M., van Deurs, B., and Hansen, G.H. (2003). "Nonclassical" secretion of annexin A2 to the lumenal side of the enterocyte brush border membrane. Biochemistry 42, 14670-14676.
    • (2003) Biochemistry , vol.42 , pp. 14670-14676
    • Danielsen, E.M.1    Van Deurs, B.2    Hansen, G.H.3
  • 10
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11 dependent translocation of annexin 2 to the cell surface
    • Deora, A.B., Kreitzer, G., Jacovina, A.T., and Hajjar, K.A. (2004). An annexin 2 phosphorylation switch mediates p11- dependent translocation of annexin 2 to the cell surface. J Biol Chem 279, 43411-43418.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 11
    • 44949241428 scopus 로고    scopus 로고
    • PCSK9 is phosphorylated by a golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans
    • Dewpura, T., Raymond, A., Hamelin, J., Seidah, N.G., Mbikay, M., Chretien, M., et al2008). PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans. FEBS J 275, 3480-3493.
    • (2008) FEBS J. , vol.275 , pp. 3480-3493
    • Dewpura, T.1    Raymond, A.2    Hamelin, J.3    Seidah, N.G.4    Mbikay, M.5    Chretien, M.6
  • 13
    • 31644434206 scopus 로고    scopus 로고
    • Biomarker discovery from pancreatic cancer secretome using a differential proteomic approach
    • Gronborg, M., Kristiansen, T.Z., Iwahori, A., Chang, R., Reddy, R., Sato, N., et al2006). Biomarker discovery from pancreatic cancer secretome using a differential proteomic approach. Mol Cell Proteomics 5, 157-171.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 157-171
    • Gronborg, M.1    Kristiansen, T.Z.2    Iwahori, A.3    Chang, R.4    Reddy, R.5    Sato, N.6
  • 14
    • 34247133868 scopus 로고    scopus 로고
    • Approaches to the study of the cell secretome
    • Hathout, Y. (2007). Approaches to the study of the cell secretome. Expert Rev Proteomics 4, 239-248.
    • (2007) Expert Rev. Proteomics , vol.4 , pp. 239-248
    • Hathout, Y.1
  • 15
    • 0034283394 scopus 로고    scopus 로고
    • Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells
    • Jellinek, D.A., Chang, A.C., Larsen, M.R., Wang, X., Robinson, P.J., and Reddel, R.R. (2000). Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells. Biochem J 350, 453-461.
    • (2000) Biochem. J. , vol.350 , pp. 453-461
    • Jellinek, D.A.1    Chang, A.C.2    Larsen, M.R.3    Wang, X.4    Robinson, P.J.5    Reddel, R.R.6
  • 16
    • 23944453389 scopus 로고    scopus 로고
    • Global phosphoproteome of HT-29 human colon adenocarcinoma cells
    • Kim, J.E., Tannenbaum, S.R., and White, F.M. (2005). Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res 4, 1339-1346.
    • (2005) J. Proteome. Res. , vol.4 , pp. 1339-1346
    • Kim, J.E.1    Tannenbaum, S.R.2    White, F.M.3
  • 17
    • 0036491539 scopus 로고    scopus 로고
    • A proteomic approach for identification of secreted proteins during the differentiation of 3T3-L1 preadipocytes to adipocytes
    • Kratchmarova, I., Kalume, D.E., Blagoev, B., Scherer, P.E., Podtelejnikov, A.V., Molina, H., et al2002). A proteomic approach for identification of secreted proteins during the differentiation of 3T3-L1 preadipocytes to adipocytes. Mol Cell Proteomics 1, 213-222.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 213-222
    • Kratchmarova, I.1    Kalume, D.E.2    Blagoev, B.3    Scherer, P.E.4    Podtelejnikov, A.V.5    Molina, H.6
  • 18
    • 34247325212 scopus 로고    scopus 로고
    • The serine threonine tyrosine phosphoproteome of the model bacterium bacillus subtilis
    • Macek, B., Mijakovic, I., Olsen, J.V., Gnad, F., Kumar, C., Jensen, P.R., et al2007). The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 6, 697-707.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 697-707
    • Macek, B.1    Mijakovic, I.2    Olsen, J.V.3    Gnad, F.4    Kumar, C.5    Jensen, P.R.6
  • 20
    • 70349974263 scopus 로고    scopus 로고
    • Quantitative analysis of the human spindle phosphoproteome at distinct mitotic stages
    • Malik, R., Lenobel, R., Santamaria, A., Ries, A., Nigg, E.A., and Korner, R. (2009). Quantitative analysis of the human spindle phosphoproteome at distinct mitotic stages. J Proteome Res 8, 4553-4563.
    • (2009) J. Proteome. Res. , vol.8 , pp. 4553-4563
    • Malik, R.1    Lenobel, R.2    Santamaria, A.3    Ries, A.4    Nigg, E.A.5    Korner, R.6
  • 21
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • Mambula, S.S., and Calderwood, S.K. (2006). Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J Immunol 177, 7849-7857.
    • (2006) J. Immunol. , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 22
    • 38549099740 scopus 로고    scopus 로고
    • Phosphorylation of bone morphogenetic protein-15 and growth and differentiation factor-9 plays a critical role in determining agonistic or antagonistic functions
    • McMahon, H.E., Sharma, S., and Shimasaki, S. (2008). Phosphorylation of bone morphogenetic protein-15 and growth and differentiation factor-9 plays a critical role in determining agonistic or antagonistic functions. Endocrinology 149, 812-817.
    • (2008) Endocrinology , vol.149 , pp. 812-817
    • McMahon, H.E.1    Sharma, S.2    Shimasaki, S.3
  • 23
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman, I., and Warren, G. (2000). The road taken: past and future foundations of membrane traffic. Cell 100, 99-112.
    • (2000) Cell. , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 24
    • 39049165852 scopus 로고    scopus 로고
    • Characterization of apin a secreted protein highly expressed in tooth-associated epithelia
    • Moffatt, P., Smith, C.E., St-Arnaud, R., and Nanci, A. (2008). Characterization of Apin, a secreted protein highly expressed in tooth-associated epithelia. J Cell Biochem 103, 941-956.
    • (2008) J. Cell. Biochem. , vol.103 , pp. 941-956
    • Moffatt, P.1    Smith, C.E.2    St-Arnaud, R.3    Nanci, A.4
  • 25
    • 34347404255 scopus 로고    scopus 로고
    • Threonine phosphorylation post-translationally regulates protein secretion in pseudomonas aeruginosa
    • 797-U 121
    • Mougous, J.D., Gifford, C.A., Ramsdell, T.L., and Mekalanos, J.J. (2007). Threonine phosphorylation post-translationally regulates protein secretion in Pseudomonas aeruginosa. Nat Cell Biol 9, 797-U121.
    • (2007) Nat. Cell. Biol. , vol.9
    • Mougous, J.D.1    Gifford, C.A.2    Ramsdell, T.L.3    Mekalanos, J.J.4
  • 26
    • 62349088782 scopus 로고    scopus 로고
    • Manual validation of peptide sequence and sites of tyrosine phosphorylation from MS MS spectra
    • Nichols, A.M., and White, F.M. (2009). Manual validation of peptide sequence and sites of tyrosine phosphorylation from MS/MS spectra. Methods Mol Biol 143-160.
    • (2009) Methods Mol. Biol. , pp. 143-160
    • Nichols, A.M.1    White, F.M.2
  • 27
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion - A current view on cargo proteins and potential export routes
    • Nickel, W. (2003). The mystery of nonclassical protein secretion- a current view on cargo proteins and potential export routes. Eur J Biochem 270, 2109-2119.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 28
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J.C., Cantley, L.C., and Yaffe, M.B. (2003). Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res 31, 3635-3641.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 29
    • 66949144402 scopus 로고    scopus 로고
    • HMGB1 is phosphorylated by classical protein kinase C and is secreted by a calcium-dependent mechanism
    • Oh, Y.J., Youn, J.H., Ji, Y., Lee, S.E., Lim, K.J., Choi, J.E., et al2009). HMGB1 is phosphorylated by classical protein kinase C and is secreted by a calcium-dependent mechanism. J Immunol 182, 5800-5809.
    • (2009) J. Immunol. , vol.182 , pp. 5800-5809
    • Oh, Y.J.1    Youn, J.H.2    Ji, Y.3    Lee, S.E.4    Lim, K.J.5    Choi, J.E.6
  • 30
    • 33750456519 scopus 로고    scopus 로고
    • Global in vivo and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J.V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., et al2006). Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648.
    • (2006) Cell. , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6
  • 31
    • 55849147636 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors
    • Pan, C., Gnad, F., Olsen, J.V., and Mann, M. (2008). Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors. Proteomics 8, 4534-4546.
    • (2008) Proteomics , vol.8 , pp. 4534-4546
    • Pan, C.1    Gnad, F.2    Olsen, J.V.3    Mann, M.4
  • 32
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., et al2007). Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131, 1190-1203.
    • (2007) Cell. , vol.131 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4    Yu, J.5    Haack, H.6
  • 33
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1-beta a protein lacking a signal sequence
    • Rubartelli, A., Cozzolino, F., Talio, M., and Sitia, R. (1990). A novel secretory pathway for interleukin-1-beta, a protein lacking a signal sequence. EMBO J 9, 1503-1510.
    • (1990) EMBO J. , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 34
    • 4544228245 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in the regulation of cleavage secretion of angiotensinconverting enzyme
    • Santhamma, K.R., Sadhukhan, R., Kinter, M., Chattopadhyay, S., McCue, B., and Sen, I. (2004). Role of tyrosine phosphorylation in the regulation of cleavage secretion of angiotensinconverting enzyme. J Biol Chem 279, 40227-40236.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40227-40236
    • Santhamma, K.R.1    Sadhukhan, R.2    Kinter, M.3    Chattopadhyay, S.4    McCue, B.5    Sen, I.6
  • 36
    • 70249090440 scopus 로고    scopus 로고
    • Stanniocalcin 2 promotes invasion and is associated with metastatic stages in neuroblastoma
    • Volland, S., Kugler, W., Schweigerer, L., Wilting, J., and Becker, J. (2009). Stanniocalcin 2 promotes invasion and is associated with metastatic stages in neuroblastoma. Int J Cancer 125, 2049-2057.
    • (2009) Int. J. Cancer , vol.125 , pp. 2049-2057
    • Volland, S.1    Kugler, W.2    Schweigerer, L.3    Wilting, J.4    Becker, J.5
  • 37
    • 0036829132 scopus 로고    scopus 로고
    • Epstein-barr virus latent membrane protein 1 induces and causes release of fibroblast growth factor-2
    • Wakisaka, N., Murono, S., Yoshizaki, T., Furukawa, M., and Pagano, J.S. (2002). Epstein-Barr virus latent membrane protein 1 induces and causes release of fibroblast growth factor-2. Cancer Res 62, 6337-6344.
    • (2002) Cancer Res. , vol.62 , pp. 6337-6344
    • Wakisaka, N.1    Murono, S.2    Yoshizaki, T.3    Furukawa, M.4    Pagano, J.S.5
  • 38
    • 75849139266 scopus 로고    scopus 로고
    • The regulatory mechanism of Hsp90 alpha secretion and its function in tumor malignancy
    • USA
    • Wang, X.F., Song, X.M., Zhuo, W., Fu, Y., Shi, H.B., Liang, Y., et al2009). The regulatory mechanism of Hsp90 alpha secretion and its function in tumor malignancy. Proc Natl Acad Sci USA 106, 21288-21293.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 21288-21293
    • Wang, X.F.1    Song, X.M.2    Zhuo, W.3    Fu, Y.4    Shi, H.B.5    Liang, Y.6
  • 39
    • 53549091303 scopus 로고    scopus 로고
    • The cancer secretome: A reservoir of biomarkers
    • Xue, H., Lu, B., and Lai, M. (2008). The cancer secretome: a reservoir of biomarkers. J Translat Med 6.
    • (2008) J. Translat Med. , vol.6
    • Xue, H.1    Lu, B.2    Lai, M.3
  • 40
    • 33645472678 scopus 로고    scopus 로고
    • Identification of novel phosphoproteins in signaling pathways triggered by latent membrane protein 1 using functional proteomics technology
    • Yan, G.G., Li, L.L., Tao, Y.G., Liu, S.F., Liu, Y.P., Luo, W., et al2006). Identification of novel phosphoproteins in signaling pathways triggered by latent membrane protein 1 using functional proteomics technology. Proteomics 6, 1810-1821.
    • (2006) Proteomics , vol.6 , pp. 1810-1821
    • Yan, G.G.1    Li, L.L.2    Tao, Y.G.3    Liu, S.F.4    Liu, Y.P.5    Luo, W.6
  • 41
    • 0037423377 scopus 로고    scopus 로고
    • Secretion of annexin II via activation of insulin receptor and insulin-like growth factor receptor
    • Zhao, W.Q., Chen, G.H., Chen, H., Pascale, A., Ravindranath, L., Quon, M.J., et al2003). Secretion of annexin II via activation of insulin receptor and insulin-like growth factor receptor. J Biol Chem 278, 4205-4215
    • (2003) J. Biol. Chem. , vol.278 , pp. 4205-4215
    • Zhao, W.Q.1    Chen, G.H.2    Chen, H.3    Pascale, A.4    Ravindranath, L.5    Quon, M.J.6


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