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Volumn 36, Issue 4, 2005, Pages 527-534

Expression, purification, refolding, and characterization of recombinant human soluble-Fas ligand from Escherichia coli

Author keywords

Apoptosis; Fas ligand; Refolding

Indexed keywords

CELLS; CHEMOTHERAPY; ESCHERICHIA COLI; NICKEL; OLIGOMERS; TUMORS;

EID: 13244281956     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2004.11.013     Document Type: Article
Times cited : (3)

References (39)
  • 1
    • 0027145632 scopus 로고
    • Molecular cloning and expression of the Fas ligand: A novel member of the tumor necrosis factor family
    • T. Suda, T. Takahashi, P. Golstein, and S. Nagata Molecular cloning and expression of the Fas ligand: a novel member of the tumor necrosis factor family Cell 75 1993 1169 1178
    • (1993) Cell , vol.75 , pp. 1169-1178
    • Suda, T.1    Takahashi, T.2    Golstein, P.3    Nagata, S.4
  • 4
    • 10544232277 scopus 로고    scopus 로고
    • Melanoma cell expression of Fas (APO-1/CD95) ligand: Implications for tumor immune escape
    • M. Hahne, D. Rimoldi, M. Schroter, P. Romero, P.M. Schreier, and L.E. French Melanoma cell expression of Fas (APO-1/CD95) ligand: implications for tumor immune escape Science 274 1996 1363 1366
    • (1996) Science , vol.274 , pp. 1363-1366
    • Hahne, M.1    Rimoldi, D.2    Schroter, M.3    Romero, P.4    Schreier, P.M.5    French, L.E.6
  • 5
    • 0030842535 scopus 로고    scopus 로고
    • Fas ligand expression in islets of Langerhans does not confer immune privilege and instead targets them for rapid destruction
    • S.M. Kang, D.B. Schneider, Z. Lin, D. Hanahan, D.A. Dichek, and P.G. Stock Fas ligand expression in islets of Langerhans does not confer immune privilege and instead targets them for rapid destruction Nat Med 3 1997 738 743
    • (1997) Nat Med , vol.3 , pp. 738-743
    • Kang, S.M.1    Schneider, D.B.2    Lin, Z.3    Hanahan, D.4    Dichek, D.A.5    Stock, P.G.6
  • 7
    • 0032573581 scopus 로고    scopus 로고
    • Regulation of the pro-inflammatory effects of Fas ligand (CD95L)
    • J.J. Chen, Y. Sun, and G.J. Nabel Regulation of the pro-inflammatory effects of Fas ligand (CD95L) Science 282 1998 1714 1717
    • (1998) Science , vol.282 , pp. 1714-1717
    • Chen, J.J.1    Sun, Y.2    Nabel, G.J.3
  • 8
    • 0028893078 scopus 로고
    • Fas (CD95)/FasL interactions required for programmed cell death after T-cell activation
    • S.T. Ju, D.J. Panka, H. Cui, R. Ettinger, M. el-Khatib, and D.H. Sherr Fas (CD95)/FasL interactions required for programmed cell death after T-cell activation Nature 373 1995 444 448
    • (1995) Nature , vol.373 , pp. 444-448
    • Ju, S.T.1    Panka, D.J.2    Cui, H.3    Ettinger, R.4    El-Khatib, M.5    Sherr, D.H.6
  • 9
    • 85012514730 scopus 로고    scopus 로고
    • Role of Fas-FasL in inflammatory diseases
    • J. O'Connell Role of Fas-FasL in inflammatory diseases Exp Rev Mol Med 10 2001 1 18
    • (2001) Exp Rev Mol Med , vol.10 , pp. 1-18
    • O'Connell, J.1
  • 10
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor induced cell death
    • M.P. Boldin, T.M. Goncharov, Y.V. Goltsev, and D. Wallach Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor induced cell death Cell 86 1996 803 815
    • (1996) Cell , vol.86 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 11
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • A.M. Chinnaiyan, K. O'Rourke, M. Tewari, and V.M. Dixit FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis Cell 81 1995 505 512
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 12
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
    • M. Enari, R.V. Talanian, W.W. Wong, and S. Nagata Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis Nature 380 1996 723 726
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 13
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1(Fas/CD95)-associated proteins from a death-inducing signaling complex (DISC) with the receptor
    • F.C. Kischkel, S. Hellbardt, I. Behrmann, M. Germer, M. Pawlita, and P.H. Krammer Cytotoxicity-dependent APO-1(Fas/CD95)-associated proteins from a death-inducing signaling complex (DISC) with the receptor EMBO J 14 1995 5579 5588
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6
  • 15
    • 0033396491 scopus 로고    scopus 로고
    • Fas ligand-induced apoptosis
    • S. Nagata Fas ligand-induced apoptosis Annu Rev Genet 33 1999 29 55
    • (1999) Annu Rev Genet , vol.33 , pp. 29-55
    • Nagata, S.1
  • 17
    • 0036695656 scopus 로고    scopus 로고
    • Death receptor Fas and autoimmune disease: From the original generation to therapeutic application of agonistic anti-Fas monoclonal antibody
    • S. Yonehara Death receptor Fas and autoimmune disease: from the original generation to therapeutic application of agonistic anti-Fas monoclonal antibody Cytokine Growth Factor Rev 13 2002 393 402
    • (2002) Cytokine Growth Factor Rev , vol.13 , pp. 393-402
    • Yonehara, S.1
  • 18
    • 0033151892 scopus 로고    scopus 로고
    • Identification of the ligand binding site in Fas (CD95) and analysis of Fas-ligand interactions
    • J. Bajorath Identification of the ligand binding site in Fas (CD95) and analysis of Fas-ligand interactions Proteins 35 1999 475 482
    • (1999) Proteins , vol.35 , pp. 475-482
    • Bajorath, J.1
  • 19
    • 0032764980 scopus 로고    scopus 로고
    • Analysis of Fas-ligand interactions using a molecular model of the receptor-ligand interface
    • J. Bajorath Analysis of Fas-ligand interactions using a molecular model of the receptor-ligand interface J Comput Aided Mol Des 13 1999 409 414
    • (1999) J Comput Aided Mol des , vol.13 , pp. 409-414
    • Bajorath, J.1
  • 22
    • 0028919473 scopus 로고
    • Expression of the functional soluble form of human Fas ligand in activated lymphocytes
    • M. Tanaka, T. Suda, T. Takahashi, and S. Nagata Expression of the functional soluble form of human Fas ligand in activated lymphocytes EMBO J 14 1995 1129 11335
    • (1995) EMBO J , vol.14 , pp. 1129-11335
    • Tanaka, M.1    Suda, T.2    Takahashi, T.3    Nagata, S.4
  • 24
    • 0034850864 scopus 로고    scopus 로고
    • The membrane-bound but not the soluble form of human Fas ligand is responsible for its inflammatory activity
    • K. Shudo, K. Kinoshita, R. Imamura, H. Fan, K. Hasumoto, and M. Tanaka The membrane-bound but not the soluble form of human Fas ligand is responsible for its inflammatory activity Eur J Immunol 31 2001 2504 2511
    • (2001) Eur J Immunol , vol.31 , pp. 2504-2511
    • Shudo, K.1    Kinoshita, K.2    Imamura, R.3    Fan, H.4    Hasumoto, K.5    Tanaka, M.6
  • 25
    • 0033777407 scopus 로고    scopus 로고
    • Recombinant expression of the Candida rugosa lip4 lipase in Escherichia coli
    • S.J. Tang, K.H. Sun, G.H. Sun, T.Y. Chang, and G.C. Lee Recombinant expression of the Candida rugosa lip4 lipase in Escherichia coli Protein Exp Purif 20 2000 308 313
    • (2000) Protein Exp Purif , vol.20 , pp. 308-313
    • Tang, S.J.1    Sun, K.H.2    Sun, G.H.3    Chang, T.Y.4    Lee, G.C.5
  • 26
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays J Immunol Methods 65 1983 55 63
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 27
    • 0028825817 scopus 로고
    • Gene fusion expression systems in Escherichia coli
    • E.R. LaVallie, and J.M. McCoy Gene fusion expression systems in Escherichia coli Curr Opin Biotechnol 6 1995 501 506
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 501-506
    • Lavallie, E.R.1    McCoy, J.M.2
  • 28
    • 0026494193 scopus 로고
    • A linkage map of mouse chromosome 1 using an inter-specific cross segregation for the gld autoimmunity mutation
    • M.L. Watson, P. D'Eustachio, B.A. Mock, A.D. Steinberg, H.C. Morse, and R.J. Oakey A linkage map of mouse chromosome 1 using an inter-specific cross segregation for the gld autoimmunity mutation Mamm Genome 2 1993 158 171
    • (1993) Mamm Genome , vol.2 , pp. 158-171
    • Watson, M.L.1    D'Eustachio, P.2    Mock, B.A.3    Steinberg, A.D.4    Morse, H.C.5    Oakey, R.J.6
  • 29
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • A.I. Derman, W.A. Prinz, D. Belin, and J. Beckwith Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli Science 262 1993 1744 1747
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 30
    • 0029934575 scopus 로고    scopus 로고
    • Expression of biologically active mouse and human CD95/APO-1/Fas ligand in the baculovirus system
    • S.M. Mariani, B. Matiba, T. Sparna, and P.H. Krammer Expression of biologically active mouse and human CD95/APO-1/Fas ligand in the baculovirus system J Immunol Methods 193 1996 63 70
    • (1996) J Immunol Methods , vol.193 , pp. 63-70
    • Mariani, S.M.1    Matiba, B.2    Sparna, T.3    Krammer, P.H.4
  • 31
    • 0033559492 scopus 로고    scopus 로고
    • Soluble Fas ligand is chemotactic for human neutrophilic polymorphonuclear leukocytes
    • L. Ottonello, G. Tortolina, M. Amelotti, and F. Dallegri Soluble Fas ligand is chemotactic for human neutrophilic polymorphonuclear leukocytes J Immunol 162 1999 3601 3606
    • (1999) J Immunol , vol.162 , pp. 3601-3606
    • Ottonello, L.1    Tortolina, G.2    Amelotti, M.3    Dallegri, F.4
  • 32
    • 0031452639 scopus 로고    scopus 로고
    • Separate domain of human Fas ligand dictate self-association and receptor binding
    • J.R. Orlinick, K.B. Elkon, and M. Chao Separate domain of human Fas ligand dictate self-association and receptor binding J Biol Chem 272 1997 32222 32229
    • (1997) J Biol Chem , vol.272 , pp. 32222-32229
    • Orlinick, J.R.1    Elkon, K.B.2    Chao, M.3
  • 33
    • 0022393776 scopus 로고
    • Molecular cloning and expression of human tumor necrosis factor and comparison with mouse tumor necrosis factor
    • A. Marmenout, L. Fransen, J. Tavernier, J. Van der Heyden, R. Tizard, and E. Kawashima Molecular cloning and expression of human tumor necrosis factor and comparison with mouse tumor necrosis factor Eur J Biochem 152 1985 515 522
    • (1985) Eur J Biochem , vol.152 , pp. 515-522
    • Marmenout, A.1    Fransen, L.2    Tavernier, J.3    Van Der Heyden, J.4    Tizard, R.5    Kawashima, E.6
  • 35
    • 0025753831 scopus 로고
    • Efficient purification of recombinant human tumor necrosis factor beta from Escherichia coli yields biologically active protein with a trimeric structure that binds to both tumor necrosis factor receptors
    • H.J. Schoenfeld, B. Poeschl, J.R. Frey, H. Loetscher, W. Hunziker, and A. Lustig Efficient purification of recombinant human tumor necrosis factor beta from Escherichia coli yields biologically active protein with a trimeric structure that binds to both tumor necrosis factor receptors J Biol Chem 266 1991 3863 3869
    • (1991) J Biol Chem , vol.266 , pp. 3863-3869
    • Schoenfeld, H.J.1    Poeschl, B.2    Frey, J.R.3    Loetscher, H.4    Hunziker, W.5    Lustig, A.6
  • 36
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • H. Walczak, R.E. Miller, K. Ariail, B. Gliniak, T.S. Griffith, and M. Kubin Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo Nat Med 5 1999 157 163
    • (1999) Nat Med , vol.5 , pp. 157-163
    • Walczak, H.1    Miller, R.E.2    Ariail, K.3    Gliniak, B.4    Griffith, T.S.5    Kubin, M.6
  • 37
    • 0031938030 scopus 로고    scopus 로고
    • Downregulation of Fas ligand by shedding
    • M. Tanaka, T. Itia, M. Adachi, and S. Nagata Downregulation of Fas ligand by shedding Nat Med 4 1998 31 36
    • (1998) Nat Med , vol.4 , pp. 31-36
    • Tanaka, M.1    Itia, T.2    Adachi, M.3    Nagata, S.4
  • 38
    • 0034642495 scopus 로고    scopus 로고
    • Bioorganic synthesis of lipid-modified proteins for the study of signal transduction
    • B. Bader, K. Kuhn, D.J. Owen, H. Waldmann, A. Wittinghofer, and J. Kuhlmann Bioorganic synthesis of lipid-modified proteins for the study of signal transduction Nature 403 2000 223 226
    • (2000) Nature , vol.403 , pp. 223-226
    • Bader, B.1    Kuhn, K.2    Owen, D.J.3    Waldmann, H.4    Wittinghofer, A.5    Kuhlmann, J.6
  • 39
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein transfer of diacylglyceryl moiety from phosphatidylglycerol
    • K. Sankaran, and H.C. Wu Lipid modification of bacterial prolipoprotein transfer of diacylglyceryl moiety from phosphatidylglycerol J Biol Chem 296 1994 19701 19706
    • (1994) J Biol Chem , vol.296 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2


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