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Volumn 11, Issue 11, 2012, Pages 5167-5185

Comparative secretome analyses using a hollow fiber culture system with label-free quantitative proteomics indicates the influence of PARK7 on cell proliferation and migration/invasion in lung adenocarcinoma

Author keywords

cancer metastasis; hollow fiber culture system; label free quantitative proteomics; PARK7

Indexed keywords

DJ 1 PROTEIN; PROTEOME; SECRETOME; UNCLASSIFIED DRUG;

EID: 84868314556     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300362g     Document Type: Article
Times cited : (18)

References (95)
  • 1
    • 68149106772 scopus 로고    scopus 로고
    • World Health Organization. Fact Sheet No. 310; Geneva: Switzerland
    • World Health Organization. the Top Ten Causes of Death; Fact Sheet No. 310; Geneva: Switzerland, 2008.
    • (2008) The Top Ten Causes of Death
  • 3
    • 0003964363 scopus 로고    scopus 로고
    • American Cancer Society. American Cancer Society: Atlanta, GA
    • American Cancer Society. Cancer Facts & Figures 2009; American Cancer Society: Atlanta, GA, 2009.
    • (2009) Cancer Facts & Figures 2009
  • 5
    • 67649421096 scopus 로고    scopus 로고
    • Molecular principles of cancer invasion and metastasis (review)
    • Leber, M. F.; Efferth, T. Molecular principles of cancer invasion and metastasis (review) Int. J. Oncol. 2009, 34 (4) 881-895
    • (2009) Int. J. Oncol. , vol.34 , Issue.4 , pp. 881-895
    • Leber, M.F.1    Efferth, T.2
  • 6
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H.; Bolhuis, A.; Jongbloed, J. D.; Bron, S.; van Dijl, J. M. Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome Microbiol. Mol. Biol. Rev 2000, 64, 515-547
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    Van Dijl, J.M.5
  • 8
    • 70349972788 scopus 로고    scopus 로고
    • Discovery of retinoblastoma-associated binding protein 46 as a novel prognostic marker for distant metastasis in nonsmall cell lung cancer by combined analysis of cancer cell secretome and pleural effusion proteome
    • Wang, C. L.; Wang, C. I.; Liao, P. C.; Chen, C. D.; Liang, Y.; Chuang, W. Y.; Tsai, Y. H.; Chen, H. C.; Chang, Y. S.; Yu, J. S.; Wu, C. C.; Yu, C. J. Discovery of retinoblastoma-associated binding protein 46 as a novel prognostic marker for distant metastasis in nonsmall cell lung cancer by combined analysis of cancer cell secretome and pleural effusion proteome J. Proteome Res. 2009, 8 (10) 4428-4440
    • (2009) J. Proteome Res. , vol.8 , Issue.10 , pp. 4428-4440
    • Wang, C.L.1    Wang, C.I.2    Liao, P.C.3    Chen, C.D.4    Liang, Y.5    Chuang, W.Y.6    Tsai, Y.H.7    Chen, H.C.8    Chang, Y.S.9    Yu, J.S.10    Wu, C.C.11    Yu, C.J.12
  • 9
    • 84865763229 scopus 로고    scopus 로고
    • Differential secretome analysis reveals CST6 as a suppressor of breast cancer bone metastasis
    • Jin, L.; Zhang, Y.; Li, H.; Yao, L.; Fu, D.; Yao, X.; Xu, L. X.; Hu, X.; Hu, G. Differential secretome analysis reveals CST6 as a suppressor of breast cancer bone metastasis Cell Res. 2012, 22, 1356-1373
    • (2012) Cell Res. , vol.22 , pp. 1356-1373
    • Jin, L.1    Zhang, Y.2    Li, H.3    Yao, L.4    Fu, D.5    Yao, X.6    Xu, L.X.7    Hu, X.8    Hu, G.9
  • 11
    • 84863932570 scopus 로고    scopus 로고
    • Proteomic signatures of the desmoplastic invasion front reveal collagen type XII as a marker of myofibroblastic differentiation during colorectal cancer metastasis
    • Karagiannis, G. S.; Petraki, C.; Prassas, I.; Saraon, P.; Musrap, N.; Dimitromanolakis, A.; Diamandis, E. P. Proteomic signatures of the desmoplastic invasion front reveal collagen type XII as a marker of myofibroblastic differentiation during colorectal cancer metastasis Oncotarget 2012, 3 (3) 267-285
    • (2012) Oncotarget , vol.3 , Issue.3 , pp. 267-285
    • Karagiannis, G.S.1    Petraki, C.2    Prassas, I.3    Saraon, P.4    Musrap, N.5    Dimitromanolakis, A.6    Diamandis, E.P.7
  • 12
    • 79952382501 scopus 로고    scopus 로고
    • Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling
    • Chiu, K. H.; Chang, Y. H.; Wu, Y. S.; Lee, S. H.; Liao, P. C. Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling J. Proteome Res. 2011, 10 (3) 1110-1125
    • (2011) J. Proteome Res. , vol.10 , Issue.3 , pp. 1110-1125
    • Chiu, K.H.1    Chang, Y.H.2    Wu, Y.S.3    Lee, S.H.4    Liao, P.C.5
  • 13
    • 73649116726 scopus 로고    scopus 로고
    • Identification of serum biomarkers for colorectal cancer metastasis using a differential secretome approach
    • Xue, H.; Lü, B.; Zhang, J.; Wu, M.; Huang, Q.; Wu, Q.; Sheng, H.; Wu, D.; Hu, J.; Lai, M. Identification of serum biomarkers for colorectal cancer metastasis using a differential secretome approach J. Proteome Res. 2010, 9 (1) 545-555
    • (2010) J. Proteome Res. , vol.9 , Issue.1 , pp. 545-555
    • Xue, H.1    Lü, B.2    Zhang, J.3    Wu, M.4    Huang, Q.5    Wu, Q.6    Sheng, H.7    Wu, D.8    Hu, J.9    Lai, M.10
  • 15
    • 77953142134 scopus 로고    scopus 로고
    • Hypoxic tumor cell modulates its microenvironment to enhance angiogenic and metastatic potential by secretion of proteins and exosomes
    • Park, J. E.; Tan, H. S.; Datta, A.; Lai, R. C.; Zhang, H.; Meng, W.; Lim, S. K.; Sze, S. K. Hypoxic tumor cell modulates its microenvironment to enhance angiogenic and metastatic potential by secretion of proteins and exosomes Mol. Cell. Proteomics 2010, 9 (6) 1085-1099
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.6 , pp. 1085-1099
    • Park, J.E.1    Tan, H.S.2    Datta, A.3    Lai, R.C.4    Zhang, H.5    Meng, W.6    Lim, S.K.7    Sze, S.K.8
  • 17
    • 0034042621 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 and the epidermal growth factor signal pathway in operable non-small cell lung cancer
    • Cox, G.; Jones, J.; O'Byrne, K. Matrix metalloproteinase 9 and the epidermal growth factor signal pathway in operable non-small cell lung cancer Clin. Cancer Res. 2000, 6, 2349-2355
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2349-2355
    • Cox, G.1    Jones, J.2    O'Byrne, K.3
  • 18
    • 0034954054 scopus 로고    scopus 로고
    • Fibronectin activates matrix metalloproteinase-9 secretion via the MEK1-MAPK and the PI3K-Akt pathways in ovarian cancer cells
    • Thant, A. A.; Nawa, A.; Kikkawa, F.; Ichigotani, Y.; Zhang, Y.; Sein, T. T.; Amin, A. R.; Hamaguchi, M. Fibronectin activates matrix metalloproteinase-9 secretion via the MEK1-MAPK and the PI3K-Akt pathways in ovarian cancer cells Clin. Exp. Metastasis 2000, 18 (5) 423-428
    • (2000) Clin. Exp. Metastasis , vol.18 , Issue.5 , pp. 423-428
    • Thant, A.A.1    Nawa, A.2    Kikkawa, F.3    Ichigotani, Y.4    Zhang, Y.5    Sein, T.T.6    Amin, A.R.7    Hamaguchi, M.8
  • 19
    • 0036088478 scopus 로고    scopus 로고
    • Mechanisms of normal and tumor-derived angiogenesis
    • Papetti, M.; Herman, I. M. Mechanisms of normal and tumor-derived angiogenesis Am. J. Physiol.: Cell Physiol. 2002, 282 (5) C947-970
    • (2002) Am. J. Physiol.: Cell Physiol. , vol.282 , Issue.5 , pp. 947-970
    • Papetti, M.1    Herman, I.M.2
  • 21
    • 60849139466 scopus 로고    scopus 로고
    • Proteomics analysis of nasopharyngeal carcinoma cell secretome using a hollow fiber culture system and mass spectrometry
    • Wu, H. Y.; Chang, Y. H.; Chang, Y. C.; Liao, P. C. Proteomics analysis of nasopharyngeal carcinoma cell secretome using a hollow fiber culture system and mass spectrometry J. Proteome Res. 2009, 8 (1) 380-389
    • (2009) J. Proteome Res. , vol.8 , Issue.1 , pp. 380-389
    • Wu, H.Y.1    Chang, Y.H.2    Chang, Y.C.3    Liao, P.C.4
  • 22
    • 71549131311 scopus 로고    scopus 로고
    • Cell secretome analysis using hollow fiber culture system leads to the discovery of CLIC1 protein as a novel plasma marker for nasopharyngeal carcinoma
    • Chang, Y. H.; Wu, C. C.; Chang, K. P.; Yu, J. S.; Chang, Y. C.; Liao, P. C. Cell secretome analysis using hollow fiber culture system leads to the discovery of CLIC1 protein as a novel plasma marker for nasopharyngeal carcinoma J. Proteome Res. 2009, 8 (12) 5465-5474
    • (2009) J. Proteome Res. , vol.8 , Issue.12 , pp. 5465-5474
    • Chang, Y.H.1    Wu, C.C.2    Chang, K.P.3    Yu, J.S.4    Chang, Y.C.5    Liao, P.C.6
  • 23
    • 78650173202 scopus 로고    scopus 로고
    • Collection of in vivo-like liver cell secretome with alternative sample enrichment method using a hollow fiber bioreactor culture system combined with tangential flow filtration for secretomics analysis
    • Wen, Y. T.; Chang, Y. C.; Lin, L. C.; Liao, P. C. Collection of in vivo-like liver cell secretome with alternative sample enrichment method using a hollow fiber bioreactor culture system combined with tangential flow filtration for secretomics analysis Anal. Chim. Acta 2011, 684 (1-2) 72-79
    • (2011) Anal. Chim. Acta , vol.684 , Issue.1-2 , pp. 72-79
    • Wen, Y.T.1    Chang, Y.C.2    Lin, L.C.3    Liao, P.C.4
  • 24
    • 0026904364 scopus 로고
    • Characterization of the mucin differentiation in human lung adenocarcinoma cell lines
    • Yang, P. C.; Luh, K. T.; Wu, R.; Wu, C. W. Characterization of the mucin differentiation in human lung adenocarcinoma cell lines Am. J. Respir. Cell Mol. Biol. 1992, 7 (2) 161-171
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.7 , Issue.2 , pp. 161-171
    • Yang, P.C.1    Luh, K.T.2    Wu, R.3    Wu, C.W.4
  • 25
    • 79952382501 scopus 로고    scopus 로고
    • Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling
    • Chiu, K. H.; Chang, Y. H.; Wu, Y. S.; Lee, S. H.; Liao, P. C. Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling J. Proteome Res. 2011, 10 (3) 1110-1125
    • (2011) J. Proteome Res. , vol.10 , Issue.3 , pp. 1110-1125
    • Chiu, K.H.1    Chang, Y.H.2    Wu, Y.S.3    Lee, S.H.4    Liao, P.C.5
  • 27
    • 76649139789 scopus 로고    scopus 로고
    • IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation
    • Tsou, C. C.; Tsai, C. F.; Tsui, Y. H.; Sudhir, P. R.; Wang, Y. T.; Chen, Y. J.; Chen, J. Y.; Sung, T. Y.; Hsu, W. L. IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation Mol. Cell. Proteomics 2010, 9 (1) 131-144
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.1 , pp. 131-144
    • Tsou, C.C.1    Tsai, C.F.2    Tsui, Y.H.3    Sudhir, P.R.4    Wang, Y.T.5    Chen, Y.J.6    Chen, J.Y.7    Sung, T.Y.8    Hsu, W.L.9
  • 29
    • 0031603460 scopus 로고    scopus 로고
    • Prediction of signal peptides and signal anchors by a hidden Markov model
    • Nielsen, H.; Krogh, A. Prediction of signal peptides and signal anchors by a hidden Markov model Proc. Int. Conf. Intell. Syst. Mol. Biol. 1998, 6, 122-130
    • (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.6 , pp. 122-130
    • Nielsen, H.1    Krogh, A.2
  • 30
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen, T. N.; Brunak, S.; von Heijne, G.; Nielsen, H. SignalP 4.0: discriminating signal peptides from transmembrane regions Nat. Methods 2011, 8 (10) 785-786
    • (2011) Nat. Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 33
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Möller, S.; Croning, M. D.; Apweiler, R. Evaluation of methods for the prediction of membrane spanning regions Bioinformatics 2001, 17, 646-653
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Möller, S.1    Croning, M.D.2    Apweiler, R.3
  • 36
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: A compendium of exosomal proteins and RNA
    • Mathivanan, S.; Simpson, R. J. ExoCarta: A compendium of exosomal proteins and RNA Proteomics 2009, 9 (21) 4997-5000
    • (2009) Proteomics , vol.9 , Issue.21 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 40
    • 76649094917 scopus 로고    scopus 로고
    • Proteomics analysis of A33 immunoaffinity-purified exosomes released from the human colon tumor cell line LIM1215 reveals a tissue-specific protein signature
    • Mathivanan, S.; Lim, J. W.; Tauro, B. J.; Ji, H.; Moritz, R. L.; Simpson, R. J. Proteomics analysis of A33 immunoaffinity-purified exosomes released from the human colon tumor cell line LIM1215 reveals a tissue-specific protein signature Mol. Cell. Proteomics 2010, 9, 197-208
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 197-208
    • Mathivanan, S.1    Lim, J.W.2    Tauro, B.J.3    Ji, H.4    Moritz, R.L.5    Simpson, R.J.6
  • 41
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • CHAPTER 3 Unit 3.22
    • Théry, C.; Amigorena, S.; Raposo, G.; Clayton, A. Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr. Protoc. Cell Biol. 2006, Chapter 3, Unit 3.22.
    • (2006) Curr. Protoc. Cell Biol.
    • Théry, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 42
    • 55749112807 scopus 로고    scopus 로고
    • Proteomic profiling of exosomes: Current perspectives
    • Simpson, R. J.; Jensen, S. S.; Lim, J. W. Proteomic profiling of exosomes: current perspectives Proteomics 2008, 8 (19) 4083-4099
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 4083-4099
    • Simpson, R.J.1    Jensen, S.S.2    Lim, J.W.3
  • 43
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins-theory and application
    • Speers, A. E.; Wu, C. C. Proteomics of integral membrane proteins-theory and application Chem. Rev. 2007, 107 (8) 3687-3714
    • (2007) Chem. Rev. , vol.107 , Issue.8 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 44
    • 70349495604 scopus 로고    scopus 로고
    • Ischaemia/reperfusion in rat renal cortex: Vesicle leakiness and Na+, K+-ATPase activity in membrane preparations
    • Coux, G.; Elías, M, M,; Trumper, L. Ischaemia/reperfusion in rat renal cortex: Vesicle leakiness and Na+, K+-ATPase activity in membrane preparations Nephrol., Dial., Transplant. 2009, 24 (10) 3020-3024
    • (2009) Nephrol., Dial., Transplant. , vol.24 , Issue.10 , pp. 3020-3024
    • Coux, G.1    Elías, M.M.2    Trumper, L.3
  • 45
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Théry, C.; Ostrowski, M.; Segura, E. Membrane vesicles as conveyors of immune responses Nat. Rev. Immunol. 2009, 9 (8) 581-593
    • (2009) Nat. Rev. Immunol. , vol.9 , Issue.8 , pp. 581-593
    • Théry, C.1    Ostrowski, M.2    Segura, E.3
  • 46
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: A compendium of exosomal proteins and RNA
    • Mathivanan, S.; Simpson, R. J. ExoCarta: A compendium of exosomal proteins and RNA Proteomics 2009, 9 (21) 4997-5000
    • (2009) Proteomics , vol.9 , Issue.21 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 47
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y.; Hochberg, Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing J. R. Stattist. Soc. B 1995, 57, 289-300
    • (1995) J. R. Stattist. Soc. B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 48
    • 26844570608 scopus 로고    scopus 로고
    • Tumor suppressor in lung cancer 1 (TSLC1) alters tumorigenic growth properties and gene expression
    • Sussan, T. E.; Pletcher, M. T.; Murakami, Y.; Reeves, R. H. Tumor suppressor in lung cancer 1 (TSLC1) alters tumorigenic growth properties and gene expression Mol. Cancer 2005, 4, 28
    • (2005) Mol. Cancer , vol.4 , pp. 28
    • Sussan, T.E.1    Pletcher, M.T.2    Murakami, Y.3    Reeves, R.H.4
  • 49
    • 33846861339 scopus 로고    scopus 로고
    • Depsipeptide a histone deacetlyase inhibitor down regulates levels of matrix metalloproteinases 2 and 9 mRNA and protein expressions in lung cancer cells (A549)
    • Vinodhkumar, R.; Song, Y. S.; Ravikumar, V.; Ramakrishnan, G.; Devaki, T. Depsipeptide a histone deacetlyase inhibitor down regulates levels of matrix metalloproteinases 2 and 9 mRNA and protein expressions in lung cancer cells (A549) Chem.-Biol. Interact. 2007, 165 (3) 220-229
    • (2007) Chem.-Biol. Interact. , vol.165 , Issue.3 , pp. 220-229
    • Vinodhkumar, R.1    Song, Y.S.2    Ravikumar, V.3    Ramakrishnan, G.4    Devaki, T.5
  • 51
    • 82955163926 scopus 로고    scopus 로고
    • Myosin VI in PC12 cells plays important roles in cell migration and proliferation but not in catecholamine secretion
    • Majewski, A.; Sobczak, M.; Wasik, A.; Skowronek, K.; Rèdowicz, M. J. Myosin VI in PC12 cells plays important roles in cell migration and proliferation but not in catecholamine secretion J. Muscle Res. Cell Motil. 2011, 32, 291-302
    • (2011) J. Muscle Res. Cell Motil. , vol.32 , pp. 291-302
    • Majewski, A.1    Sobczak, M.2    Wasik, A.3    Skowronek, K.4    Rèdowicz, M.J.5
  • 53
    • 34548697091 scopus 로고    scopus 로고
    • Comparison of the expression of agrin, a basement membrane heparan sulfate proteoglycan, in cholangiocarcinoma and hepatocellular carcinoma
    • Batmunkh, E.; Tátrai, P.; Szabó, E.; Lódi, C.; Holczbauer, A.; Páska, C.; Kupcsulik, P.; Kiss, A.; Schaff, Z.; Kovalszky, I. Comparison of the expression of agrin, a basement membrane heparan sulfate proteoglycan, in cholangiocarcinoma and hepatocellular carcinoma Hum. Pathol. 2007, 38 (10) 1508-1515
    • (2007) Hum. Pathol. , vol.38 , Issue.10 , pp. 1508-1515
    • Batmunkh, E.1    Tátrai, P.2    Szabó, E.3    Lódi, C.4    Holczbauer, A.5    Páska, C.6    Kupcsulik, P.7    Kiss, A.8    Schaff, Z.9    Kovalszky, I.10
  • 54
    • 0032414023 scopus 로고    scopus 로고
    • Role of fibronectin-stimulated tumor cell migration in glioma invasion in vivo: Clinical significance of fibronectin and fibronectin receptor expressed in human glioma tissues
    • Ohnishi, T.; Hiraga, S.; Izumoto, S.; Matsumura, H.; Kanemura, Y.; Arita, N.; Hayakawa, T. Role of fibronectin-stimulated tumor cell migration in glioma invasion in vivo: clinical significance of fibronectin and fibronectin receptor expressed in human glioma tissues Clin. Exp. Metastasis 1998, 16 (8) 729-741
    • (1998) Clin. Exp. Metastasis , vol.16 , Issue.8 , pp. 729-741
    • Ohnishi, T.1    Hiraga, S.2    Izumoto, S.3    Matsumura, H.4    Kanemura, Y.5    Arita, N.6    Hayakawa, T.7
  • 55
    • 5044224593 scopus 로고    scopus 로고
    • Non-muscle alpha-actinin-4 interacts with plasminogen activator inhibitor type-1 (PAI-1)
    • Magdolen, U.; Schroeck, F.; Creutzburg, S.; Schmitt, M.; Magdolen, V. Non-muscle alpha-actinin-4 interacts with plasminogen activator inhibitor type-1 (PAI-1) Biol. Chem. 2004, 385 (9) 801-808
    • (2004) Biol. Chem. , vol.385 , Issue.9 , pp. 801-808
    • Magdolen, U.1    Schroeck, F.2    Creutzburg, S.3    Schmitt, M.4    Magdolen, V.5
  • 56
  • 60
    • 0036841790 scopus 로고    scopus 로고
    • Up-regulated caveolin-1 accentuates the metastasis capability of lung adenocarcinoma by inducing filopodia formation
    • Ho, C. C.; Huang, P. H.; Huang, H. Y.; Chen, Y. H.; Yang, P. C.; Hsu, S. M. Up-regulated caveolin-1 accentuates the metastasis capability of lung adenocarcinoma by inducing filopodia formation Am. J. Pathol. 2002, 161 (5) 1647-1656
    • (2002) Am. J. Pathol. , vol.161 , Issue.5 , pp. 1647-1656
    • Ho, C.C.1    Huang, P.H.2    Huang, H.Y.3    Chen, Y.H.4    Yang, P.C.5    Hsu, S.M.6
  • 62
    • 0042358985 scopus 로고    scopus 로고
    • Cell culture: Biology's new dimension
    • Abbott, A. Cell culture: Biology's new dimension Nature 2003, 424 (6951) 870-872
    • (2003) Nature , vol.424 , Issue.6951 , pp. 870-872
    • Abbott, A.1
  • 63
    • 84855573739 scopus 로고    scopus 로고
    • The roles of tumor-derived exosomes in cancer pathogenesis
    • 842849
    • Yang, C.; Robbins, P. D. The roles of tumor-derived exosomes in cancer pathogenesis Clin. Dev. Immunol. 2011, 2011 842849
    • (2011) Clin. Dev. Immunol. , vol.2011
    • Yang, C.1    Robbins, P.D.2
  • 64
    • 79957879331 scopus 로고    scopus 로고
    • Exosomes released by melanoma cells prepare sentinel lymph nodes for tumor metastasis
    • Hood, J. L.; San, R. S.; Wickline, S. A. Exosomes released by melanoma cells prepare sentinel lymph nodes for tumor metastasis Cancer Res. 2011, 71 (11) 3792-3801
    • (2011) Cancer Res. , vol.71 , Issue.11 , pp. 3792-3801
    • Hood, J.L.1    San, R.S.2    Wickline, S.A.3
  • 65
    • 68549128599 scopus 로고    scopus 로고
    • Lung cancer secreted microvesicles: Underappreciated modulators of microenvironment in expanding tumors
    • Wysoczynski, M.; Ratajczak, M. Z. Lung cancer secreted microvesicles: underappreciated modulators of microenvironment in expanding tumors Int. J. Cancer 2009, 125 (7) 1595-1603
    • (2009) Int. J. Cancer , vol.125 , Issue.7 , pp. 1595-1603
    • Wysoczynski, M.1    Ratajczak, M.Z.2
  • 66
    • 79960960417 scopus 로고    scopus 로고
    • Microvesicles released from human renal cancer stem cells stimulate angiogenesis and formation of lung premetastatic niche
    • Grange, C.; Tapparo, M.; Collino, F.; Vitillo, L.; Damasco, C.; Deregibus, M. C.; Tetta, C.; Bussolati, B.; Camussi, G. Microvesicles released from human renal cancer stem cells stimulate angiogenesis and formation of lung premetastatic niche Cancer Res. 2011, 71 (15) 5346-5356
    • (2011) Cancer Res. , vol.71 , Issue.15 , pp. 5346-5356
    • Grange, C.1    Tapparo, M.2    Collino, F.3    Vitillo, L.4    Damasco, C.5    Deregibus, M.C.6    Tetta, C.7    Bussolati, B.8    Camussi, G.9
  • 67
    • 7644224191 scopus 로고    scopus 로고
    • Extracellular proteases as targets for treatment of cancer metastases
    • Lee, M.; Fridman, R.; Mobashery, S. Extracellular proteases as targets for treatment of cancer metastases Chem. Soc. Rev. 2004, 33, 401-409
    • (2004) Chem. Soc. Rev. , vol.33 , pp. 401-409
    • Lee, M.1    Fridman, R.2    Mobashery, S.3
  • 68
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood, J. D.; Cheresh, D. A. Role of integrins in cell invasion and migration Nat. Rev. Cancer 2002, 2 (2) 91-100
    • (2002) Nat. Rev. Cancer , vol.2 , Issue.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 69
    • 10344262906 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton: An oncogenic function for CDK inhibitors?
    • Besson, A.; Assoian, R. K.; Roberts, J. M. Regulation of the cytoskeleton: An oncogenic function for CDK inhibitors? Nat. Rev. Cancer 2004, 4 (12) 948-955
    • (2004) Nat. Rev. Cancer , vol.4 , Issue.12 , pp. 948-955
    • Besson, A.1    Assoian, R.K.2    Roberts, J.M.3
  • 70
    • 61849135453 scopus 로고    scopus 로고
    • Tumor suppressors and cell metabolism: A recipe for cancer growth
    • Jones, R. G.; Thompson, C. B. Tumor suppressors and cell metabolism: A recipe for cancer growth Genes Dev. 2009, 23 (5) 537-548
    • (2009) Genes Dev. , vol.23 , Issue.5 , pp. 537-548
    • Jones, R.G.1    Thompson, C.B.2
  • 71
    • 46749121459 scopus 로고    scopus 로고
    • Causes and consequences of increased glucose metabolism of cancers
    • Gillies, R. J.; Robey, I.; Gatenby, R. A. Causes and consequences of increased glucose metabolism of cancers J. Nucl. Med. 2008, 49 (Suppl 2) 24S-42S
    • (2008) J. Nucl. Med. , vol.49 , Issue.SUPPL. 2
    • Gillies, R.J.1    Robey, I.2    Gatenby, R.A.3
  • 72
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • Gatenby, R. A.; Gillies, R. J. Why do cancers have high aerobic glycolysis? Nat. Rev. Cancer 2004, 4 (11) 891-899
    • (2004) Nat. Rev. Cancer , vol.4 , Issue.11 , pp. 891-899
    • Gatenby, R.A.1    Gillies, R.J.2
  • 73
    • 33749478922 scopus 로고    scopus 로고
    • Cancer's molecular sweet tooth and the Warburg effect
    • Kim, J. W.; Dang, C. V. Cancer's molecular sweet tooth and the Warburg effect Cancer Res. 2006, 66 (18) 8927-8930
    • (2006) Cancer Res. , vol.66 , Issue.18 , pp. 8927-8930
    • Kim, J.W.1    Dang, C.V.2
  • 77
    • 33644653456 scopus 로고    scopus 로고
    • Culture of skin cells in 3D rather than 2D improves their ability to survive exposure to cytotoxic agents
    • Sun, T.; Jackson, S.; Haycock, J. W.; MacNeil, S. Culture of skin cells in 3D rather than 2D improves their ability to survive exposure to cytotoxic agents J. Biotechnol. 2006, 122 (3) 372-381
    • (2006) J. Biotechnol. , vol.122 , Issue.3 , pp. 372-381
    • Sun, T.1    Jackson, S.2    Haycock, J.W.3    MacNeil, S.4
  • 78
    • 0032191388 scopus 로고    scopus 로고
    • Recent advances in producing and selecting functional proteins by using cell-free translation
    • Jermutus, L.; Ryabova, L. A.; Plückthun, A. Recent advances in producing and selecting functional proteins by using cell-free translation Curr. Opin. Biotechnol. 1998, 9 (5) 534-548
    • (1998) Curr. Opin. Biotechnol. , vol.9 , Issue.5 , pp. 534-548
    • Jermutus, L.1    Ryabova, L.A.2    Plückthun, A.3
  • 81
    • 20944437573 scopus 로고    scopus 로고
    • The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis
    • Xu, J.; Zhong, N.; Wang, H.; Elias, J. E.; Kim, C. Y.; Woldman, I.; Pifl, C.; Gygi, S. P.; Geula, C.; Yankner, B. A. The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis Hum. Mol. Genet. 2005, 14, 1231-1241
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1231-1241
    • Xu, J.1    Zhong, N.2    Wang, H.3    Elias, J.E.4    Kim, C.Y.5    Woldman, I.6    Pifl, C.7    Gygi, S.P.8    Geula, C.9    Yankner, B.A.10
  • 85
    • 78751477930 scopus 로고    scopus 로고
    • DJ-1 expression in glioblastomas shows positive correlation with p53 expression and negative correlation with epidermal growth factor receptor amplification
    • Hinklem, D. A.; Mullett, S. J.; Gabris, B. E.; Hamilton, R. L. DJ-1 expression in glioblastomas shows positive correlation with p53 expression and negative correlation with epidermal growth factor receptor amplification Neuropathology 2011, 31 (1) 29-37
    • (2011) Neuropathology , vol.31 , Issue.1 , pp. 29-37
    • Hinklem, D.A.1    Mullett, S.J.2    Gabris, B.E.3    Hamilton, R.L.4
  • 86
    • 79953003319 scopus 로고    scopus 로고
    • DJ-1 enhances cell survival through the binding of Cezanne, a negative regulator of NF-kappaB
    • McNally, R. S.; Davis, B. K.; Clements, C. M.; Accavitti-Loper, M. A.; Mak, T. W.; Ting, J. P. DJ-1 enhances cell survival through the binding of Cezanne, a negative regulator of NF-kappaB J. Biol. Chem. 2011, 286 (6) 4098-4106
    • (2011) J. Biol. Chem. , vol.286 , Issue.6 , pp. 4098-4106
    • McNally, R.S.1    Davis, B.K.2    Clements, C.M.3    Accavitti-Loper, M.A.4    Mak, T.W.5    Ting, J.P.6
  • 92
    • 77955475113 scopus 로고    scopus 로고
    • Protection of pancreatic beta-cells from various stress conditions is mediated by DJ-1
    • Inberg, A.; Linial, M. Protection of pancreatic beta-cells from various stress conditions is mediated by DJ-1 J. Biol. Chem. 2010, 285 (33) 25686-25698
    • (2010) J. Biol. Chem. , vol.285 , Issue.33 , pp. 25686-25698
    • Inberg, A.1    Linial, M.2
  • 93
    • 79959748950 scopus 로고    scopus 로고
    • Proteomic Analysis Identified DJ-1 as a cisplatin resistant marker in non-small cell lung cancer
    • Zeng, H. Z.; Qu, Y. Q.; Zhang, W. J.; Xiu, B.; Deng, A. M.; Liang, A. B. Proteomic Analysis Identified DJ-1 as a cisplatin resistant marker in non-small cell lung cancer Int. J. Mol. Sci. 2011, 12 (6) 3489-3499
    • (2011) Int. J. Mol. Sci. , vol.12 , Issue.6 , pp. 3489-3499
    • Zeng, H.Z.1    Qu, Y.Q.2    Zhang, W.J.3    Xiu, B.4    Deng, A.M.5    Liang, A.B.6
  • 94
    • 77954816203 scopus 로고    scopus 로고
    • Glucose-regulated protein 78 (GRP78) silencing enhances cell migration but does not influence cell proliferation in hepatocellular carcinoma
    • Chang, Y. J.; Chiu, C. C.; Wu, C. H.; An, J.; Wu, C. C.; Liu, T. Z.; Wei, P. L.; Huang, M. T. Glucose-regulated protein 78 (GRP78) silencing enhances cell migration but does not influence cell proliferation in hepatocellular carcinoma Ann. Surg. Oncol. 2010, 17 (6) 1703-1709
    • (2010) Ann. Surg. Oncol. , vol.17 , Issue.6 , pp. 1703-1709
    • Chang, Y.J.1    Chiu, C.C.2    Wu, C.H.3    An, J.4    Wu, C.C.5    Liu, T.Z.6    Wei, P.L.7    Huang, M.T.8
  • 95
    • 39049160268 scopus 로고    scopus 로고
    • Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival, and tumor angiogenesis in transgene-induced mammary tumor development
    • Dong, D.; Ni, M.; Li, J.; Xiong, S.; Ye, W.; Virrey, J. J.; Mao, C.; Ye, R.; Wang, M.; Pen, L.; Dubeau, L.; Groshen, S.; Hofman, F. M.; Lee, A. S. Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival, and tumor angiogenesis in transgene-induced mammary tumor development Cancer Res. 2008, 68 (2) 498-505
    • (2008) Cancer Res. , vol.68 , Issue.2 , pp. 498-505
    • Dong, D.1    Ni, M.2    Li, J.3    Xiong, S.4    Ye, W.5    Virrey, J.J.6    Mao, C.7    Ye, R.8    Wang, M.9    Pen, L.10    Dubeau, L.11    Groshen, S.12    Hofman, F.M.13    Lee, A.S.14


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