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Volumn 7, Issue 10, 2012, Pages

Efficiency of Immunotoxin Cytotoxicity Is Modulated by the Intracellular Itinerary

Author keywords

[No Author keywords available]

Indexed keywords

CXCL11 CHEMOKINE; FURIN; INTERLEUKIN 2 RECEPTOR ALPHA; MEMBRANE PROTEIN; PROTEIN TGN38; PSEUDOMONAS EXOTOXIN; PSEUDOMONAS EXOTOXIN LMB 2; UNCLASSIFIED DRUG;

EID: 84867295577     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047320     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0027572639 scopus 로고
    • Single-chain immunotoxin fusions between anti-Tac and Pseudomonas exotoxin: relative importance of the two toxin disulfide bonds
    • Kreitman RJ, Batra JK, Seetharam S, Chaudhary VK, FitzGerald DJ, et al. (1993) Single-chain immunotoxin fusions between anti-Tac and Pseudomonas exotoxin: relative importance of the two toxin disulfide bonds. Bioconjug Chem 4: 112-120.
    • (1993) Bioconjug Chem , vol.4 , pp. 112-120
    • Kreitman, R.J.1    Batra, J.K.2    Seetharam, S.3    Chaudhary, V.K.4    FitzGerald, D.J.5
  • 2
    • 0038290547 scopus 로고    scopus 로고
    • Immunotoxins containing Pseudomonas exotoxin A: a short history
    • Pastan I, (2003) Immunotoxins containing Pseudomonas exotoxin A: a short history. Cancer Immunol Immunother 52: 338-341.
    • (2003) Cancer Immunol Immunother , vol.52 , pp. 338-341
    • Pastan, I.1
  • 3
    • 33748643264 scopus 로고    scopus 로고
    • The role of interleukin-2 receptor alpha in cancer
    • Kuhn DJ, Dou QP, (2005) The role of interleukin-2 receptor alpha in cancer. Front Biosci 10: 1462-1474.
    • (2005) Front Biosci , vol.10 , pp. 1462-1474
    • Kuhn, D.J.1    Dou, Q.P.2
  • 4
    • 0028057249 scopus 로고
    • Recombinant immunotoxins containing anti-Tac(Fv) and derivatives of Pseudomonas exotoxin produce complete regression in mice of an interleukin-2 receptor-expressing human carcinoma
    • Kreitman RJ, Bailon P, Chaudhary VK, FitzGerald DJ, Pastan I, (1994) Recombinant immunotoxins containing anti-Tac(Fv) and derivatives of Pseudomonas exotoxin produce complete regression in mice of an interleukin-2 receptor-expressing human carcinoma. Blood 83: 426-434.
    • (1994) Blood , vol.83 , pp. 426-434
    • Kreitman, R.J.1    Bailon, P.2    Chaudhary, V.K.3    FitzGerald, D.J.4    Pastan, I.5
  • 5
    • 64349108724 scopus 로고    scopus 로고
    • Recombinant immunotoxins containing truncated bacterial toxins for the treatment of hematologic malignancies
    • Kreitman RJ, (2009) Recombinant immunotoxins containing truncated bacterial toxins for the treatment of hematologic malignancies. BioDrugs 23: 1-13.
    • (2009) BioDrugs , vol.23 , pp. 1-13
    • Kreitman, R.J.1
  • 6
    • 0026690341 scopus 로고
    • The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A
    • Kounnas MZ, Morris RE, Thompson MR, FitzGerald DJ, Strickland DK, et al. (1992) The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J Biol Chem. 267: 12420-12423.
    • (1992) J Biol Chem , vol.267 , pp. 12420-12423
    • Kounnas, M.Z.1    Morris, R.E.2    Thompson, M.R.3    FitzGerald, D.J.4    Strickland, D.K.5
  • 7
    • 33644871336 scopus 로고    scopus 로고
    • Internalized Pseudomonas exotoxin A can exploit multiple pathways to reach the endoplasmic reticulum
    • Smith DC, Spooner RA, Watson PD, Murray JL, Hodge TW, et al. (2006) Internalized Pseudomonas exotoxin A can exploit multiple pathways to reach the endoplasmic reticulum. Traffic 7: 379-393.
    • (2006) Traffic , vol.7 , pp. 379-393
    • Smith, D.C.1    Spooner, R.A.2    Watson, P.D.3    Murray, J.L.4    Hodge, T.W.5
  • 8
    • 60849116672 scopus 로고    scopus 로고
    • Pseudomonas exotoxin A: from virulence factor to anti-cancer agent
    • Wolf P, Elsasser-Beile U, (2009) Pseudomonas exotoxin A: from virulence factor to anti-cancer agent. Int J Med Microbiol 299: 161-176.
    • (2009) Int J Med Microbiol , vol.299 , pp. 161-176
    • Wolf, P.1    Elsasser-Beile, U.2
  • 9
    • 0028304478 scopus 로고
    • Cleavage of Pseudomonas exotoxin and diphtheria toxin by a furin-like enzyme prepared from beef liver
    • Chiron MF, Fryling CM, FitzGerald DJ, (1994) Cleavage of Pseudomonas exotoxin and diphtheria toxin by a furin-like enzyme prepared from beef liver. J Biol Chem 269: 18167-18176.
    • (1994) J Biol Chem , vol.269 , pp. 18167-18176
    • Chiron, M.F.1    Fryling, C.M.2    FitzGerald, D.J.3
  • 10
    • 0028091725 scopus 로고
    • Furin activates Pseudomonas exotoxin A by specific cleavage in vivo and in vitro
    • Inocencio NM, Moehring JM, Moehring TJ, (1994) Furin activates Pseudomonas exotoxin A by specific cleavage in vivo and in vitro. J Biol Chem 269: 31831-31835.
    • (1994) J Biol Chem , vol.269 , pp. 31831-31835
    • Inocencio, N.M.1    Moehring, J.M.2    Moehring, T.J.3
  • 11
    • 0033554871 scopus 로고    scopus 로고
    • Reduction of furin-nicked Pseudomonas exotoxin A: an unfolding story
    • McKee ML, FitzGerald DJ, (1999) Reduction of furin-nicked Pseudomonas exotoxin A: an unfolding story. Biochemistry 38: 16507-16513.
    • (1999) Biochemistry , vol.38 , pp. 16507-16513
    • McKee, M.L.1    FitzGerald, D.J.2
  • 12
    • 0032394928 scopus 로고    scopus 로고
    • Role of caspases in immunotoxin-induced apoptosis of cancer cells
    • Keppler-Hafkemeyer A, Brinkmann U, Pastan I, (1998) Role of caspases in immunotoxin-induced apoptosis of cancer cells. Biochemistry 37: 16934-16942.
    • (1998) Biochemistry , vol.37 , pp. 16934-16942
    • Keppler-Hafkemeyer, A.1    Brinkmann, U.2    Pastan, I.3
  • 13
    • 0034119870 scopus 로고    scopus 로고
    • Apoptosis induced by immunotoxins used in the treatment of hematologic malignancies
    • Keppler-Hafkemeyer A, Kreitman RJ, Pastan I, (2000) Apoptosis induced by immunotoxins used in the treatment of hematologic malignancies. Int J Cancer 87: 86-94.
    • (2000) Int J Cancer , vol.87 , pp. 86-94
    • Keppler-Hafkemeyer, A.1    Kreitman, R.J.2    Pastan, I.3
  • 14
    • 0027990837 scopus 로고
    • The cytoplasmic domain mediates localization of furin to the trans-Golgi network en route to the endosomal/lysosomal system
    • Bosshart H, Humphrey J, Deignan E, Davidson J, Drazba J, et al. (1994) The cytoplasmic domain mediates localization of furin to the trans-Golgi network en route to the endosomal/lysosomal system. J Cell Biol 126: 1157-1172.
    • (1994) J Cell Biol , vol.126 , pp. 1157-1172
    • Bosshart, H.1    Humphrey, J.2    Deignan, E.3    Davidson, J.4    Drazba, J.5
  • 15
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface
    • Molloy SS, Thomas L, VanSlyke JK, Stenberg PE, Thomas G, (1994) Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface. Embo J 13: 18-33.
    • (1994) Embo J , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 16
    • 0029071584 scopus 로고
    • Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin
    • Schafer W, Stroh A, Berghofer S, Seiler J, Vey M, et al. (1995) Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin. Embo J 14: 2424-2435.
    • (1995) Embo J , vol.14 , pp. 2424-2435
    • Schafer, W.1    Stroh, A.2    Berghofer, S.3    Seiler, J.4    Vey, M.5
  • 17
    • 0028875689 scopus 로고
    • Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain
    • Takahashi S, Nakagawa T, Banno T, Watanabe T, Murakami K, et al. (1995) Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain. J Biol Chem 270: 28397-28401.
    • (1995) J Biol Chem , vol.270 , pp. 28397-28401
    • Takahashi, S.1    Nakagawa, T.2    Banno, T.3    Watanabe, T.4    Murakami, K.5
  • 18
    • 0027159260 scopus 로고
    • TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain
    • Bos K, Wraight C, Stanley KK, (1993) TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain. Embo J 12: 2219-2228.
    • (1993) Embo J , vol.12 , pp. 2219-2228
    • Bos, K.1    Wraight, C.2    Stanley, K.K.3
  • 19
    • 0027240379 scopus 로고
    • A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network
    • Jones SM, Crosby JR, Salamero J, Howell KE, (1993) A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. J Cell Biol 122: 775-788.
    • (1993) J Cell Biol , vol.122 , pp. 775-788
    • Jones, S.M.1    Crosby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 20
    • 0027447921 scopus 로고
    • TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN
    • Reaves B, Horn M, Banting G, (1993) TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN. Mol Biol Cell 4: 93-105.
    • (1993) Mol Biol Cell , vol.4 , pp. 93-105
    • Reaves, B.1    Horn, M.2    Banting, G.3
  • 21
    • 0023834942 scopus 로고
    • Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus
    • Duncan JR, Kornfeld S, (1988) Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus. J Cell Biol 106: 617-628.
    • (1988) J Cell Biol , vol.106 , pp. 617-628
    • Duncan, J.R.1    Kornfeld, S.2
  • 22
    • 0032563568 scopus 로고    scopus 로고
    • An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells
    • Ghosh RN, Mallet WG, Soe TT, McGraw TE, Maxfield FR, (1998) An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells. J Cell Biol 142: 923-936.
    • (1998) J Cell Biol , vol.142 , pp. 923-936
    • Ghosh, R.N.1    Mallet, W.G.2    Soe, T.T.3    McGraw, T.E.4    Maxfield, F.R.5
  • 23
    • 0742288050 scopus 로고    scopus 로고
    • Endocytosed cation-independent mannose 6-phosphate receptor traffics via the endocytic recycling compartment en route to the trans-Golgi network and a subpopulation of late endosomes
    • Lin SX, Mallet WG, Huang AY, Maxfield FR, (2004) Endocytosed cation-independent mannose 6-phosphate receptor traffics via the endocytic recycling compartment en route to the trans-Golgi network and a subpopulation of late endosomes. Mol Biol Cell 15: 721-733.
    • (2004) Mol Biol Cell , vol.15 , pp. 721-733
    • Lin, S.X.1    Mallet, W.G.2    Huang, A.Y.3    Maxfield, F.R.4
  • 24
    • 0033606772 scopus 로고    scopus 로고
    • Chimeric forms of furin and TGN38 are transported with the plasma membrane in the trans-Golgi network via distinct endosomal pathways
    • Mallet WG, Maxfield FR, (1999) Chimeric forms of furin and TGN38 are transported with the plasma membrane in the trans-Golgi network via distinct endosomal pathways. J Cell Biol 146: 345-359.
    • (1999) J Cell Biol , vol.146 , pp. 345-359
    • Mallet, W.G.1    Maxfield, F.R.2
  • 25
    • 2542466750 scopus 로고    scopus 로고
    • Role of cytoplasmic domain serines in intracellular trafficking of furin
    • Schapiro FB, Soe TT, Mallet WG, Maxfield FR, (2004) Role of cytoplasmic domain serines in intracellular trafficking of furin. Mol Biol Cell 15: 2884-2894.
    • (2004) Mol Biol Cell , vol.15 , pp. 2884-2894
    • Schapiro, F.B.1    Soe, T.T.2    Mallet, W.G.3    Maxfield, F.R.4
  • 28
    • 0032534995 scopus 로고    scopus 로고
    • Modeling of the Time-Dependency of in Vitro Drug Cytotoxicity and Resistance
    • Laurence M. Levasseur HKS, Youcef M Rustum, William R Greco, (1998) Modeling of the Time-Dependency of in Vitro Drug Cytotoxicity and Resistance. Cancer Research 58: 5749-5761.
    • (1998) Cancer Research , vol.58 , pp. 5749-5761
    • Laurence, M.1    Levasseur, H.K.S.2    Youcef, M.3    Rustum4    William, R.G.5
  • 29
    • 33244458202 scopus 로고    scopus 로고
    • Automated microscopy screening for compounds that partially revert cholesterol accumulation in Niemann-Pick C cells
    • Pipalia NH, Huang A, Ralph H, Rujoi M, Maxfield FR, (2006) Automated microscopy screening for compounds that partially revert cholesterol accumulation in Niemann-Pick C cells. J Lipid Res 47: 284-301.
    • (2006) J Lipid Res , vol.47 , pp. 284-301
    • Pipalia, N.H.1    Huang, A.2    Ralph, H.3    Rujoi, M.4    Maxfield, F.R.5
  • 30
    • 0032837077 scopus 로고    scopus 로고
    • Hepatotoxicity in cancer patients receiving erb-38, a recombinant immunotoxin that targets the erbB2 receptor
    • Pai-Scherf LH, Villa J, Pearson D, Watson T, Liu E, et al. (1999) Hepatotoxicity in cancer patients receiving erb-38, a recombinant immunotoxin that targets the erbB2 receptor. Clin Cancer Res 5: 2311-2315.
    • (1999) Clin Cancer Res , vol.5 , pp. 2311-2315
    • Pai-Scherf, L.H.1    Villa, J.2    Pearson, D.3    Watson, T.4    Liu, E.5
  • 31
    • 0031438704 scopus 로고    scopus 로고
    • Furin-mediated cleavage of Pseudomonas exotoxin-derived chimeric toxins
    • Chiron MF, Fryling CM, FitzGerald D, (1997) Furin-mediated cleavage of Pseudomonas exotoxin-derived chimeric toxins. J Biol Chem 272: 31707-31711.
    • (1997) J Biol Chem , vol.272 , pp. 31707-31711
    • Chiron, M.F.1    Fryling, C.M.2    FitzGerald, D.3
  • 32
    • 0026786444 scopus 로고
    • A recombinant form of Pseudomonas exotoxin directed at the epidermal growth factor receptor that is cytotoxic without requiring proteolytic processing
    • Theuer CP, FitzGerald D, Pastan I, (1992) A recombinant form of Pseudomonas exotoxin directed at the epidermal growth factor receptor that is cytotoxic without requiring proteolytic processing. J Biol Chem 267: 16872-16877.
    • (1992) J Biol Chem , vol.267 , pp. 16872-16877
    • Theuer, C.P.1    FitzGerald, D.2    Pastan, I.3
  • 33
    • 65549146468 scopus 로고    scopus 로고
    • A protease-resistant immunotoxin against CD22 with greatly increased activity against CLL and diminished animal toxicity
    • Weldon JE, Xiang L, Chertov O, Margulies I, Kreitman RJ, et al. (2009) A protease-resistant immunotoxin against CD22 with greatly increased activity against CLL and diminished animal toxicity. Blood 113: 3792-3800.
    • (2009) Blood , vol.113 , pp. 3792-3800
    • Weldon, J.E.1    Xiang, L.2    Chertov, O.3    Margulies, I.4    Kreitman, R.J.5
  • 34
    • 0028913166 scopus 로고
    • Endocytosis of interleukin 2 receptors in human T lymphocytes: distinct intracellular localization and fate of the receptor alpha, beta, and gamma chains
    • Hemar A, Subtil A, Lieb M, Morelon E, Hellio R, et al. (1995) Endocytosis of interleukin 2 receptors in human T lymphocytes: distinct intracellular localization and fate of the receptor alpha, beta, and gamma chains. J Cell Biol 129: 55-64.
    • (1995) J Cell Biol , vol.129 , pp. 55-64
    • Hemar, A.1    Subtil, A.2    Lieb, M.3    Morelon, E.4    Hellio, R.5
  • 35
    • 0025301499 scopus 로고
    • Isolation of high-affinity murine interleukin 2 receptors as detergent-resistant membrane complexes
    • Hoessli DC, Poincelet M, Rungger-Brandle E, (1990) Isolation of high-affinity murine interleukin 2 receptors as detergent-resistant membrane complexes. Eur J Immunol 20: 1497-1503.
    • (1990) Eur J Immunol , vol.20 , pp. 1497-1503
    • Hoessli, D.C.1    Poincelet, M.2    Rungger-Brandle, E.3
  • 36
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway
    • Lamaze C, Dujeancourt A, Baba T, Lo CG, Benmerah A, et al. (2001) Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol Cell 7: 661-671.
    • (2001) Mol Cell , vol.7 , pp. 661-671
    • Lamaze, C.1    Dujeancourt, A.2    Baba, T.3    Lo, C.G.4    Benmerah, A.5
  • 37
    • 0026713066 scopus 로고
    • Mik-beta 1(Fv)-PE40, a recombinant immunotoxin cytotoxic toward cells bearing the beta-chain of the IL-2 receptor
    • Kreitman RJ, Schneider WP, Queen C, Tsudo M, Fitzgerald DJ, et al. (1992) Mik-beta 1(Fv)-PE40, a recombinant immunotoxin cytotoxic toward cells bearing the beta-chain of the IL-2 receptor. J Immunol 149: 2810-2815.
    • (1992) J Immunol , vol.149 , pp. 2810-2815
    • Kreitman, R.J.1    Schneider, W.P.2    Queen, C.3    Tsudo, M.4    Fitzgerald, D.J.5
  • 38
    • 84878374080 scopus 로고    scopus 로고
    • NIH Website, Accessed 2012 September 16
    • NIH Website: http://assay.nih.gov/assay/index.php/Section3:Determination_of_EC50-IC50.Accessed 2012 September 16.


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