메뉴 건너뛰기




Volumn 24, Issue 4, 2013, Pages 595-603

C2-streptavidin mediates the delivery of biotin-conjugated tumor suppressor protein P53 into tumor cells

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; CELLS; CONFOCAL MICROSCOPY; DISEASES; LANTHANUM COMPOUNDS; MAMMALS; MOLECULAR BIOLOGY; MOLECULES; RECOMBINANT PROTEINS; SURFACE PLASMON RESONANCE; TUMORS;

EID: 84876474969     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc300563c     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 41549129885 scopus 로고    scopus 로고
    • Binary actin-ADP-ribosylating toxins and their use as molecular Trojan horses for drug delivery into eukaryotic cells
    • Barth, H. and Stiles, B. G. (2008) Binary actin-ADP-ribosylating toxins and their use as molecular Trojan horses for drug delivery into eukaryotic cells Curr. Med. Chem. 15, 459-69
    • (2008) Curr. Med. Chem. , vol.15 , pp. 459-469
    • Barth, H.1    Stiles, B.G.2
  • 3
    • 0034723205 scopus 로고    scopus 로고
    • Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates
    • Eckhardt, M., Barth, H., Blocker, D., and Aktories, K. (2000) Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates J. Biol. Chem. 275, 2328-34
    • (2000) J. Biol. Chem. , vol.275 , pp. 2328-2334
    • Eckhardt, M.1    Barth, H.2    Blocker, D.3    Aktories, K.4
  • 5
    • 78449295494 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin is internalized by clathrin-and Rho-dependent mechanisms
    • Pust, S., Barth, H., and Sandvig, K. (2010) Clostridium botulinum C2 toxin is internalized by clathrin-and Rho-dependent mechanisms Cell Microbiol. 12, 1809-20
    • (2010) Cell Microbiol. , vol.12 , pp. 1809-1820
    • Pust, S.1    Barth, H.2    Sandvig, K.3
  • 6
    • 0041856090 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol
    • Haug, G., Leemhuis, J., Tiemann, D., Meyer, D. K., Aktories, K., and Barth, H. (2003) The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol J. Biol. Chem. 278, 32266-74
    • (2003) J. Biol. Chem. , vol.278 , pp. 32266-32274
    • Haug, G.1    Leemhuis, J.2    Tiemann, D.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 7
    • 64049084122 scopus 로고    scopus 로고
    • Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells
    • Kaiser, E., Pust, S., Kroll, C., and Barth, H. (2009) Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells Cell Microbiol. 11, 780-95
    • (2009) Cell Microbiol. , vol.11 , pp. 780-795
    • Kaiser, E.1    Pust, S.2    Kroll, C.3    Barth, H.4
  • 8
    • 84863992806 scopus 로고    scopus 로고
    • FK506-binding protein 51 interacts with Clostridium botulinum C2 toxin and FK506 inhibits membrane translocation of the toxin in mammalian cells
    • Kaiser, E., Bohm, N., Ernst, K., Langer, S., Schwan, C., Aktories, K., Popoff, M., Fischer, G., and Barth, H. (2012) FK506-binding protein 51 interacts with Clostridium botulinum C2 toxin and FK506 inhibits membrane translocation of the toxin in mammalian cells Cell Microbiol. 14, 1193-205
    • (2012) Cell Microbiol. , vol.14 , pp. 1193-1205
    • Kaiser, E.1    Bohm, N.2    Ernst, K.3    Langer, S.4    Schwan, C.5    Aktories, K.6    Popoff, M.7    Fischer, G.8    Barth, H.9
  • 9
    • 0023708116 scopus 로고
    • ADP-ribosylated actin caps the barbed ends of actin filaments
    • Wegner, A. and Aktories, K. (1988) ADP-ribosylated actin caps the barbed ends of actin filaments J. Biol. Chem. 263, 13739-42
    • (1988) J. Biol. Chem. , vol.263 , pp. 13739-13742
    • Wegner, A.1    Aktories, K.2
  • 10
    • 53649083009 scopus 로고    scopus 로고
    • ADP-ribosylation of actin by the Clostridium botulinum C2 toxin in mammalian cells results in delayed caspase-dependent apoptotic cell death
    • Heine, K., Pust, S., Enzenmuller, S., and Barth, H. (2008) ADP-ribosylation of actin by the Clostridium botulinum C2 toxin in mammalian cells results in delayed caspase-dependent apoptotic cell death Infect. Immun. 76, 4600-8
    • (2008) Infect. Immun. , vol.76 , pp. 4600-4608
    • Heine, K.1    Pust, S.2    Enzenmuller, S.3    Barth, H.4
  • 11
    • 0032036388 scopus 로고    scopus 로고
    • The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin
    • Barth, H., Hofmann, F., Olenik, C., Just, I., and Aktories, K. (1998) The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin Infect. Immun. 66, 1364-9
    • (1998) Infect. Immun. , vol.66 , pp. 1364-1369
    • Barth, H.1    Hofmann, F.2    Olenik, C.3    Just, I.4    Aktories, K.5
  • 12
    • 74949085139 scopus 로고    scopus 로고
    • Genetically engineered clostridial C2 toxin as a novel delivery system for living mammalian cells
    • Fahrer, J., Plunien, R., Binder, U., Langer, T., Seliger, H., and Barth, H. (2010) Genetically engineered clostridial C2 toxin as a novel delivery system for living mammalian cells Bioconjugate Chem. 21, 130-9
    • (2010) Bioconjugate Chem. , vol.21 , pp. 130-139
    • Fahrer, J.1    Plunien, R.2    Binder, U.3    Langer, T.4    Seliger, H.5    Barth, H.6
  • 15
    • 78649377141 scopus 로고    scopus 로고
    • The C2-streptavidin delivery system promotes the uptake of biotinylated molecules in macrophages and T-leukemia cells
    • Fahrer, J., Rieger, J., van Zandbergen, G., and Barth, H. (2010) The C2-streptavidin delivery system promotes the uptake of biotinylated molecules in macrophages and T-leukemia cells Biol. Chem. 391, 1315-25
    • (2010) Biol. Chem. , vol.391 , pp. 1315-1325
    • Fahrer, J.1    Rieger, J.2    Van Zandbergen, G.3    Barth, H.4
  • 17
    • 33847271089 scopus 로고    scopus 로고
    • Coping with stress: Multiple ways to activate p53
    • Horn, H. F. and Vousden, K. H. (2007) Coping with stress: multiple ways to activate p53 Oncogene 26, 1306-16
    • (2007) Oncogene , vol.26 , pp. 1306-1316
    • Horn, H.F.1    Vousden, K.H.2
  • 18
    • 33845270990 scopus 로고    scopus 로고
    • Regulating the p53 pathway: In vitro hypotheses, in vivo veritas
    • Toledo, F. and Wahl, G. M. (2006) Regulating the p53 pathway: in vitro hypotheses, in vivo veritas Nat. Rev. Cancer 6, 909-23
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 909-923
    • Toledo, F.1    Wahl, G.M.2
  • 19
    • 77955363995 scopus 로고    scopus 로고
    • TP53 mutations in human cancers: Origins, consequences, and clinical use
    • Olivier, M., Hollstein, M., and Hainaut, P. (2010) TP53 mutations in human cancers: origins, consequences, and clinical use Cold Spring Harbor Perspect. Biol. 2, a001008
    • (2010) Cold Spring Harbor Perspect. Biol. , vol.2 , pp. 001008
    • Olivier, M.1    Hollstein, M.2    Hainaut, P.3
  • 20
    • 77951093704 scopus 로고    scopus 로고
    • Biotinylated transferrin/avidin/biotinylated disulfide containing PEI bioconjugates mediated p53 gene delivery system for tumor targeted transfection
    • Zeng, X., Sun, Y. X., Qu, W., Zhang, X. Z., and Zhuo, R. X. (2010) Biotinylated transferrin/avidin/biotinylated disulfide containing PEI bioconjugates mediated p53 gene delivery system for tumor targeted transfection Biomaterials 31, 4771-80
    • (2010) Biomaterials , vol.31 , pp. 4771-4780
    • Zeng, X.1    Sun, Y.X.2    Qu, W.3    Zhang, X.Z.4    Zhuo, R.X.5
  • 21
    • 84870159045 scopus 로고    scopus 로고
    • Alginate/CaCO3 Hybrid Nanoparticles for Efficient Co-delivery of Anti-tumor Gene and Drug
    • Zhao, D., Liu, C., Zhuo, R. X., and Cheng, S. X. (2012) Alginate/CaCO3 Hybrid Nanoparticles for Efficient Co-delivery of Anti-tumor Gene and Drug Mol. Pharmaceutics 9, 2887
    • (2012) Mol. Pharmaceutics , vol.9 , pp. 2887
    • Zhao, D.1    Liu, C.2    Zhuo, R.X.3    Cheng, S.X.4
  • 22
    • 0037680428 scopus 로고    scopus 로고
    • Development of p53 protein transduction therapy using membrane-permeable peptides and the application to oral cancer cells
    • Takenobu, T., Tomizawa, K., Matsushita, M., Li, S. T., Moriwaki, A., Lu, Y. F., and Matsui, H. (2002) Development of p53 protein transduction therapy using membrane-permeable peptides and the application to oral cancer cells Mol. Cancer Ther. 1, 1043-9
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 1043-1049
    • Takenobu, T.1    Tomizawa, K.2    Matsushita, M.3    Li, S.T.4    Moriwaki, A.5    Lu, Y.F.6    Matsui, H.7
  • 23
    • 49849100270 scopus 로고    scopus 로고
    • Recombinant, refolded tetrameric p53 and gonadotropin-releasing hormone-p53 slow proliferation and induce apoptosis in p53-deficient cancer cells
    • Lafevre-Bernt, M., Wu, S., and Lin, X. (2008) Recombinant, refolded tetrameric p53 and gonadotropin-releasing hormone-p53 slow proliferation and induce apoptosis in p53-deficient cancer cells Mol. Cancer Ther. 7, 1420-9
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1420-1429
    • Lafevre-Bernt, M.1    Wu, S.2    Lin, X.3
  • 24
    • 37549022999 scopus 로고    scopus 로고
    • Quantitative analysis of the binding affinity of poly(ADP-ribose) to specific binding proteins as a function of chain length
    • Fahrer, J., Kranaster, R., Altmeyer, M., Marx, A., and Burkle, A. (2007) Quantitative analysis of the binding affinity of poly(ADP-ribose) to specific binding proteins as a function of chain length Nucleic Acids Res. 35, e143
    • (2007) Nucleic Acids Res. , vol.35 , pp. 143
    • Fahrer, J.1    Kranaster, R.2    Altmeyer, M.3    Marx, A.4    Burkle, A.5
  • 25
    • 66149185435 scopus 로고    scopus 로고
    • Biotinylated glyco-functionalized quantum dots: Synthesis, characterization, and cytotoxicity studies
    • Jiang, X., Ahmed, M., Deng, Z., and Narain, R. (2009) Biotinylated glyco-functionalized quantum dots: synthesis, characterization, and cytotoxicity studies Bioconjugate Chem. 20, 994-1001
    • (2009) Bioconjugate Chem. , vol.20 , pp. 994-1001
    • Jiang, X.1    Ahmed, M.2    Deng, Z.3    Narain, R.4
  • 26
    • 2142749540 scopus 로고    scopus 로고
    • Purification of recombinant p53 from Sf9 insect cells
    • Sun, X. Z., Nguyen, J., and Momand, J. (2003) Purification of recombinant p53 from Sf9 insect cells Methods Mol. Biol. 234, 17-28
    • (2003) Methods Mol. Biol. , vol.234 , pp. 17-28
    • Sun, X.Z.1    Nguyen, J.2    Momand, J.3
  • 27
    • 44949253112 scopus 로고    scopus 로고
    • Phosphorylation of fibroblast growth factor (FGF) receptor 1 at Ser777 by p38 mitogen-activated protein kinase regulates translocation of exogenous FGF1 to the cytosol and nucleus
    • Sorensen, V., Zhen, Y., Zakrzewska, M., Haugsten, E. M., Walchli, S., Nilsen, T., Olsnes, S., and Wiedlocha, A. (2008) Phosphorylation of fibroblast growth factor (FGF) receptor 1 at Ser777 by p38 mitogen-activated protein kinase regulates translocation of exogenous FGF1 to the cytosol and nucleus Mol. Cell. Biol. 28, 4129-41
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4129-4141
    • Sorensen, V.1    Zhen, Y.2    Zakrzewska, M.3    Haugsten, E.M.4    Walchli, S.5    Nilsen, T.6    Olsnes, S.7    Wiedlocha, A.8
  • 28
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci, C., Parton, R. G., Mather, I. H., Stunnenberg, H., Simons, K., Hoflack, B., and Zerial, M. (1992) The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway Cell 70, 715-28
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, I.H.3    Stunnenberg, H.4    Simons, K.5    Hoflack, B.6    Zerial, M.7
  • 29
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M., Vierstra, R. D., and Howley, P. M. (1993) The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53 Cell 75, 495-505
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 30
    • 84934444622 scopus 로고    scopus 로고
    • Characterizing peptide-mediated DNA internalization in human cancer cells
    • Wittrup, A. and Belting, M. (2009) Characterizing peptide-mediated DNA internalization in human cancer cells Methods Mol. Biol. 480, 101-12
    • (2009) Methods Mol. Biol. , vol.480 , pp. 101-112
    • Wittrup, A.1    Belting, M.2
  • 31
    • 0034142388 scopus 로고    scopus 로고
    • Development of a binding assay for p53/HDM2 by using homogeneous time-resolved fluorescence
    • Kane, S. A., Fleener, C. A., Zhang, Y. S., Davis, L. J., Musselman, A. L., and Huang, P. S. (2000) Development of a binding assay for p53/HDM2 by using homogeneous time-resolved fluorescence Anal. Biochem. 278, 29-38
    • (2000) Anal. Biochem. , vol.278 , pp. 29-38
    • Kane, S.A.1    Fleener, C.A.2    Zhang, Y.S.3    Davis, L.J.4    Musselman, A.L.5    Huang, P.S.6
  • 32
    • 0030973204 scopus 로고    scopus 로고
    • Engineering subunit association of multisubunit proteins: A dimeric streptavidin
    • Sano, T., Vajda, S., Smith, C. L., and Cantor, C. R. (1997) Engineering subunit association of multisubunit proteins: a dimeric streptavidin Proc. Natl. Acad. Sci. U. S. A. 94, 6153-8
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6153-6158
    • Sano, T.1    Vajda, S.2    Smith, C.L.3    Cantor, C.R.4
  • 33
    • 21344432793 scopus 로고    scopus 로고
    • Biotinidase: Its role in biotinidase deficiency and biotin metabolism
    • Wolf, B. (2005) Biotinidase: its role in biotinidase deficiency and biotin metabolism J. Nutr. Biochem. 16, 441-5
    • (2005) J. Nutr. Biochem. , vol.16 , pp. 441-445
    • Wolf, B.1
  • 36
    • 0032755396 scopus 로고    scopus 로고
    • A bipartite nuclear localization signal is required for p53 nuclear import regulated by a carboxyl-terminal domain
    • Liang, S. H. and Clarke, M. F. (1999) A bipartite nuclear localization signal is required for p53 nuclear import regulated by a carboxyl-terminal domain J. Biol. Chem. 274, 32699-703
    • (1999) J. Biol. Chem. , vol.274 , pp. 32699-32703
    • Liang, S.H.1    Clarke, M.F.2
  • 37
    • 33751070013 scopus 로고    scopus 로고
    • Structure and action of the binary C2 toxin from Clostridium botulinum
    • Schleberger, C., Hochmann, H., Barth, H., Aktories, K., and Schulz, G. E. (2006) Structure and action of the binary C2 toxin from Clostridium botulinum J. Mol. Biol. 364, 705-15
    • (2006) J. Mol. Biol. , vol.364 , pp. 705-715
    • Schleberger, C.1    Hochmann, H.2    Barth, H.3    Aktories, K.4    Schulz, G.E.5
  • 38
    • 0038208865 scopus 로고    scopus 로고
    • The C terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding
    • Blocker, D., Barth, H., Maier, E., Benz, R., Barbieri, J. T., and Aktories, K. (2000) The C terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding Infect. Immun. 68, 4566-73
    • (2000) Infect. Immun. , vol.68 , pp. 4566-4573
    • Blocker, D.1    Barth, H.2    Maier, E.3    Benz, R.4    Barbieri, J.T.5    Aktories, K.6
  • 39
    • 84863449301 scopus 로고    scopus 로고
    • Changing the receptor specificity of anthrax toxin
    • Mechaly, A., McCluskey, A. J., and Collier, R. J. (2012) Changing the receptor specificity of anthrax toxin. mBIO 3, e00088-12.
    • (2012) MBIO , vol.3 , pp. 00088-00012
    • Mechaly, A.1    McCluskey, A.J.2    Collier, R.J.3
  • 42
    • 84863563207 scopus 로고    scopus 로고
    • Somatostatin receptor-mediated tumor-targeting drug delivery using octreotide-PEG-deoxycholic acid conjugate-modified N-deoxycholic acid-O, N-hydroxyethylation chitosan micelles
    • Huo, M., Zou, A., Yao, C., Zhang, Y., Zhou, J., Wang, J., Zhu, Q., Li, J., and Zhang, Q. (2012) Somatostatin receptor-mediated tumor-targeting drug delivery using octreotide-PEG-deoxycholic acid conjugate-modified N-deoxycholic acid-O, N-hydroxyethylation chitosan micelles Biomaterials 33, 6393-407
    • (2012) Biomaterials , vol.33 , pp. 6393-6407
    • Huo, M.1    Zou, A.2    Yao, C.3    Zhang, Y.4    Zhou, J.5    Wang, J.6    Zhu, Q.7    Li, J.8    Zhang, Q.9
  • 43
    • 33644869654 scopus 로고    scopus 로고
    • Antibody pretargeting advances cancer radioimmunodetection and radioimmunotherapy
    • Goldenberg, D. M., Sharkey, R. M., Paganelli, G., Barbet, J., and Chatal, J. F. (2006) Antibody pretargeting advances cancer radioimmunodetection and radioimmunotherapy J. Clin. Oncol. 24, 823-34
    • (2006) J. Clin. Oncol. , vol.24 , pp. 823-834
    • Goldenberg, D.M.1    Sharkey, R.M.2    Paganelli, G.3    Barbet, J.4    Chatal, J.F.5
  • 45
    • 0030426639 scopus 로고    scopus 로고
    • Central nervous system pharmacologic effect in conscious rats after intravenous injection of a biotinylated vasoactive intestinal peptide analog coupled to a blood-brain barrier drug delivery system
    • Wu, D. and Pardridge, W. M. (1996) Central nervous system pharmacologic effect in conscious rats after intravenous injection of a biotinylated vasoactive intestinal peptide analog coupled to a blood-brain barrier drug delivery system J. Pharmacol. Exp. Ther. 279, 77-83
    • (1996) J. Pharmacol. Exp. Ther. , vol.279 , pp. 77-83
    • Wu, D.1    Pardridge, W.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.