메뉴 건너뛰기




Volumn 6, Issue 6, 2007, Pages 2105-2112

Comparing SILAC and two-dimensional gel electrophoresis image analysis for profiling urokinase plasminogen activator signaling in ovarian cancer cells

Author keywords

Image analysis; MALDI TOF TOF; Metabolic labeling; Protein quantitation; SILAC; Two dimensional gel electrophoresis; Urokinase plasminogen activator

Indexed keywords

UROKINASE;

EID: 34250804871     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr060638v     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 0025733509 scopus 로고
    • Quantitation of human leukocyte proteins after silver staining: A study with two-dimensional electrophoresis
    • Giometti, C. S.; Gemmell, M. A.; Tollaksen, S. L.; Taylor, J. Quantitation of human leukocyte proteins after silver staining: a study with two-dimensional electrophoresis. Electrophoresis 1991, 12, 536-543.
    • (1991) Electrophoresis , vol.12 , pp. 536-543
    • Giometti, C.S.1    Gemmell, M.A.2    Tollaksen, S.L.3    Taylor, J.4
  • 2
    • 0142151385 scopus 로고    scopus 로고
    • Overcoming technical variation and biological variation in quantitative proteomics
    • Molloy, M. P.; Brzezinski, E. E.; Hang, J.; McDowell, M. T.; VanBogelen, R. A. Overcoming technical variation and biological variation in quantitative proteomics. Proteomics 2003, 3, 1912-1919.
    • (2003) Proteomics , vol.3 , pp. 1912-1919
    • Molloy, M.P.1    Brzezinski, E.E.2    Hang, J.3    McDowell, M.T.4    VanBogelen, R.A.5
  • 3
    • 0023656216 scopus 로고
    • Detection of heritable mutations as quantitative changes in protein expression Protein changes occurring during storage of platelet concentrates. A two-dimensional gel electrophoretic analysis. Action of interferons in hairy cell leukemia
    • Giometti, C. S.; Gemmell, M. A.; Nance, S. L.; Tollaksen, S. L.; Taylor, J.; et al. Detection of heritable mutations as quantitative changes in protein expression Protein changes occurring during storage of platelet concentrates. A two-dimensional gel electrophoretic analysis. Action of interferons in hairy cell leukemia. J. Biol. Chem. 1987, 262, 12764-12767.
    • (1987) J. Biol. Chem , vol.262 , pp. 12764-12767
    • Giometti, C.S.1    Gemmell, M.A.2    Nance, S.L.3    Tollaksen, S.L.4    Taylor, J.5
  • 4
    • 30444435729 scopus 로고    scopus 로고
    • Protein expression profiling identifies maspin and stathmin as potential biomarkers of adenoid cystic carcinoma of the salivary glands
    • Nakashima, D.; Uzawa, K.; Kasamatsu, A.; Koike, H.; Endo, Y.; et al. Protein expression profiling identifies maspin and stathmin as potential biomarkers of adenoid cystic carcinoma of the salivary glands. Int. J. Cancer 2006, 118, 704-713.
    • (2006) Int. J. Cancer , vol.118 , pp. 704-713
    • Nakashima, D.1    Uzawa, K.2    Kasamatsu, A.3    Koike, H.4    Endo, Y.5
  • 5
    • 33646250180 scopus 로고    scopus 로고
    • Biomarker discovery in breast cancer serum using 2-D differential gel electrophoresis/ MALDI-TOF/TOF and data validation by routine clinical assays
    • Huang, H. L.; Stasyk, T.; Morandell, S.; Dieplinger, H.; Falkensammer, G.; et al. Biomarker discovery in breast cancer serum using 2-D differential gel electrophoresis/ MALDI-TOF/TOF and data validation by routine clinical assays. Electrophoresis 2006, 27, 1641-1650.
    • (2006) Electrophoresis , vol.27 , pp. 1641-1650
    • Huang, H.L.1    Stasyk, T.2    Morandell, S.3    Dieplinger, H.4    Falkensammer, G.5
  • 6
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M.; Morgan, M. E.; Minden, J. S. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 7
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 2002, 1, 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5
  • 8
    • 26844511378 scopus 로고    scopus 로고
    • Expression clustering reveals detailed co-expression patterns of functionally related proteins during B cell differentiation: A proteomic study using a combination of one-dimensional gel electrophoresis, LC-MS/MS, and stable isotope labeling by amino acids in cell culture (SILAC)
    • Romijn, E. P.; Christis, C.; Wieffer, M.; Gouw, J. W.; Fullaondo, A.; et al. Expression clustering reveals detailed co-expression patterns of functionally related proteins during B cell differentiation: a proteomic study using a combination of one-dimensional gel electrophoresis, LC-MS/MS, and stable isotope labeling by amino acids in cell culture (SILAC). Mol. Cell. Proteomics 2005, 4, 1297-1310.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1297-1310
    • Romijn, E.P.1    Christis, C.2    Wieffer, M.3    Gouw, J.W.4    Fullaondo, A.5
  • 9
    • 4043141477 scopus 로고    scopus 로고
    • Quantitative cancer proteomics: Stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research
    • Everley, P. A.; Krijgsveld, J.; Zetter, B. R.; Gygi, S. P. Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol. Cell. Proteomics 2004, 3, 729-735.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 729-735
    • Everley, P.A.1    Krijgsveld, J.2    Zetter, B.R.3    Gygi, S.P.4
  • 11
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev, B.; Ong, S. E.; Kratchmarova, I.; Mann, M. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat. Biotechnol. 2004, 22, 1139-1145.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 12
    • 0242569349 scopus 로고    scopus 로고
    • A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture
    • Ibarrola, N.; Kalume, D. E.; Gronborg, M.; Iwahori, A.; Pandey, A. A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture. Anal. Chem. 2003, 75, 6043-6049.
    • (2003) Anal. Chem , vol.75 , pp. 6043-6049
    • Ibarrola, N.1    Kalume, D.E.2    Gronborg, M.3    Iwahori, A.4    Pandey, A.5
  • 13
    • 33644836196 scopus 로고    scopus 로고
    • Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)
    • Zhang, G.; Spellman, D. S.; Skolnik, E. Y.; Neubert, T. A. Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC). J. Proteome Res. 2006, 5, 581-588.
    • (2006) J. Proteome Res , vol.5 , pp. 581-588
    • Zhang, G.1    Spellman, D.S.2    Skolnik, E.Y.3    Neubert, T.A.4
  • 14
    • 30744464873 scopus 로고    scopus 로고
    • Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC)
    • Foster, L. J.; Rudich, A.; Talior, I.; Patel, N.; Huang, X.; et al. Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC). J. Proteome Res. 2006, 5, 64-75.
    • (2006) J. Proteome Res , vol.5 , pp. 64-75
    • Foster, L.J.1    Rudich, A.2    Talior, I.3    Patel, N.4    Huang, X.5
  • 15
    • 33644670152 scopus 로고    scopus 로고
    • An integrated mass spectrometry-based proteomic approach: Quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network
    • Guerrero, C.; Tagwerker, C.; Kaiser, P.; Huang, L. An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol. Cell. Proteomics 2006, 5, 366-378.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 366-378
    • Guerrero, C.1    Tagwerker, C.2    Kaiser, P.3    Huang, L.4
  • 16
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev, B.; Kratchmarova, I.; Ong, S. E.; Nielsen, M.; Foster, L. J.; et al. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 2003, 21, 315-318.
    • (2003) Nat. Biotechnol , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5
  • 17
    • 0026063532 scopus 로고
    • Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosylphosphatidylinositol
    • Ploug, M.; Ronne, E.; Behrendt, N.; Jensen, A. L.; Blasi, F.; et al. Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosylphosphatidylinositol. J. Biol. Chem. 1991, 266, 1926-1933.
    • (1991) J. Biol. Chem , vol.266 , pp. 1926-1933
    • Ploug, M.1    Ronne, E.2    Behrendt, N.3    Jensen, A.L.4    Blasi, F.5
  • 18
    • 0033542781 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator binding to its receptor stimulates tumor cell migration by enhancing integrin-mediated signal transduction
    • Yebra, M.; Goretzki, L.; Pfeifer, M.; Mueller, B. M. Urokinase-type plasminogen activator binding to its receptor stimulates tumor cell migration by enhancing integrin-mediated signal transduction. Exp. Cell Res. 1999, 250, 231-240.
    • (1999) Exp. Cell Res , vol.250 , pp. 231-240
    • Yebra, M.1    Goretzki, L.2    Pfeifer, M.3    Mueller, B.M.4
  • 19
    • 0033549558 scopus 로고    scopus 로고
    • Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrin-selective manner
    • Nguyen, D. H.; Catling, A. D.; Webb, D. J.; Sankovic, M.; Walker, L. A.; et al. Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrin-selective manner. J. Cell Biol. 1999, 146, 149-164.
    • (1999) J. Cell Biol , vol.146 , pp. 149-164
    • Nguyen, D.H.1    Catling, A.D.2    Webb, D.J.3    Sankovic, M.4    Walker, L.A.5
  • 20
    • 0032522751 scopus 로고    scopus 로고
    • Downstream targets of urokinase-type plasminogen-activator-mediated signal transduction
    • Konakova, M.; Hucho, F.; Schleuning, W. D. Downstream targets of urokinase-type plasminogen-activator-mediated signal transduction. Eur. J. Biochem. 1998, 253, 421-429.
    • (1998) Eur. J. Biochem , vol.253 , pp. 421-429
    • Konakova, M.1    Hucho, F.2    Schleuning, W.D.3
  • 21
    • 0344875558 scopus 로고    scopus 로고
    • Soluble urokinase-type plasminogen activator receptor inhibits cancer cell growth and invasion by direct urokinase-independent effects on cell signaling
    • Jo, M.; Thomas, K. S.; Wu, L.; Gonias, S. L. Soluble urokinase-type plasminogen activator receptor inhibits cancer cell growth and invasion by direct urokinase-independent effects on cell signaling. J. Biol. Chem. 2003, 278, 46692-46698.
    • (2003) J. Biol. Chem , vol.278 , pp. 46692-46698
    • Jo, M.1    Thomas, K.S.2    Wu, L.3    Gonias, S.L.4
  • 22
    • 0031463337 scopus 로고    scopus 로고
    • A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity
    • Fazioli, F.; Resnati, M.; Sidenius, N.; Higashimoto, Y.; Appella, E.; et al. A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity. EMBO J. 1997, 16, 7279-7286.
    • (1997) EMBO J , vol.16 , pp. 7279-7286
    • Fazioli, F.1    Resnati, M.2    Sidenius, N.3    Higashimoto, Y.4    Appella, E.5
  • 23
    • 0033566354 scopus 로고    scopus 로고
    • Src-dependence and pertussis-toxin sensitivity of urokinase receptor-dependent chemotaxis and cytoskeleton reorganization in rat smooth muscle cells
    • Degryse, B.; Resnati, M.; Rabbani, S. A.; Villa, A.; Fazioli, F.; et al. Src-dependence and pertussis-toxin sensitivity of urokinase receptor-dependent chemotaxis and cytoskeleton reorganization in rat smooth muscle cells. Blood 1999, 94, 649-662.
    • (1999) Blood , vol.94 , pp. 649-662
    • Degryse, B.1    Resnati, M.2    Rabbani, S.A.3    Villa, A.4    Fazioli, F.5
  • 24
    • 0038364216 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system in cancer: Recent advances and implication for prognosis and therapy
    • Sidenius, N.; Blasi, F. The urokinase plasminogen activator system in cancer: recent advances and implication for prognosis and therapy. Cancer Metastasis Rev. 2003, 22, 205-222.
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 205-222
    • Sidenius, N.1    Blasi, F.2
  • 25
    • 0037379794 scopus 로고    scopus 로고
    • ERK(MAPK) activity as a determinant of tumor growth and dormancy; regulation by p38(SAPK)
    • Aguirre-Ghiso, J. A.; Estrada, Y.; Liu, D.; Ossowski, L. ERK(MAPK) activity as a determinant of tumor growth and dormancy; regulation by p38(SAPK). Cancer Res. 2003, 63, 1684-1695.
    • (2003) Cancer Res , vol.63 , pp. 1684-1695
    • Aguirre-Ghiso, J.A.1    Estrada, Y.2    Liu, D.3    Ossowski, L.4
  • 26
    • 0034705424 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator stimulates the Ras/Extracellular signal-regulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, Src, and Shc. Rapid dissociation of GRB2/Sps-Shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells
    • Nguyen, D. H.; Webb, D. J.; Catling, A. D.; Song, Q.; Dhakephalkar, A.; et al. Urokinase-type plasminogen activator stimulates the Ras/Extracellular signal-regulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, Src, and Shc. Rapid dissociation of GRB2/Sps-Shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells. J. Biol. Chem. 2000, 275, 19382-19388.
    • (2000) J. Biol. Chem , vol.275 , pp. 19382-19388
    • Nguyen, D.H.1    Webb, D.J.2    Catling, A.D.3    Song, Q.4    Dhakephalkar, A.5
  • 27
    • 0036007394 scopus 로고    scopus 로고
    • Association between alphavbeta6 integrin expression, elevated p42/44 kDa MAPK, and plasminogen-dependent matrix degradation in ovarian cancer
    • Ahmed, N.; Pansino, F.; Baker, M.; Rice, G.; Quinn, M. Association between alphavbeta6 integrin expression, elevated p42/44 kDa MAPK, and plasminogen-dependent matrix degradation in ovarian cancer. J. Cell. Biochem. 2002, 84, 675-686.
    • (2002) J. Cell. Biochem , vol.84 , pp. 675-686
    • Ahmed, N.1    Pansino, F.2    Baker, M.3    Rice, G.4    Quinn, M.5
  • 28
    • 32144464247 scopus 로고    scopus 로고
    • Quantitative proteome analysis of CD95 (Fas/Apo-1)-induced apoptosis by stable isotope labeling with amino acids in cell culture, 2-DE and MALDI-MS
    • Thiede, B.; Kretschmer, A.; Rudel, T. Quantitative proteome analysis of CD95 (Fas/Apo-1)-induced apoptosis by stable isotope labeling with amino acids in cell culture, 2-DE and MALDI-MS. Proteomics 2006, 6, 614-622.
    • (2006) Proteomics , vol.6 , pp. 614-622
    • Thiede, B.1    Kretschmer, A.2    Rudel, T.3
  • 29
    • 3142671580 scopus 로고    scopus 로고
    • Quantitative proteomics of the human malaria parasite Plasmodium falciparum and its application to studies of development and inhibition
    • Nirmalan, N.; Sims, P. F.; Hyde, J. E. Quantitative proteomics of the human malaria parasite Plasmodium falciparum and its application to studies of development and inhibition. Mol. Microbiol. 2004, 52, 1187-1199.
    • (2004) Mol. Microbiol , vol.52 , pp. 1187-1199
    • Nirmalan, N.1    Sims, P.F.2    Hyde, J.E.3
  • 30


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.