Cell surface adherence and endocytosis of protein transduction domains

Molecular Therapy

Volumn 8, Issue 1, 2003, Pages 143-150

  Lundberg, Mathias ^a   Wikström, Sara ^a   Johansson, Magnus ^a  

^a KAROLINSKA UNIVERSITY HOSPITAL   (Sweden)

Author keywords

Biological therapy; Drug carrier; Endocytosis; Gene therapy; Membrane translocation; Protein transport

Indexed keywords

DRUG CARRIER; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; POLYARGININE; POLYLYSINE; TRANSACTIVATOR PROTEIN; VIRUS PROTEIN; VIRUS VECTOR;

ANIMAL CELL; ARTICLE; CELL ADHESION; CELL INTERACTION; CELL MEMBRANE; CELL NUCLEUS; CELL SURFACE; CHO CELL; CONTROLLED STUDY; CYTOSOL; ENDOCYTOSIS; ENDOSOME; GENE THERAPY; GENETIC TRANSDUCTION; HERPES SIMPLEX VIRUS; MACROMOLECULE; MAMMAL CELL; NONHUMAN; NUCLEAR IMPORT; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN TRANSPORT; VIRAL GENE DELIVERY SYSTEM;

ANIMALIA; MAMMALIA; SIMPLEXVIRUS;

EID: 0042199010     PISSN: 15250016     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1525-0016(03)00135-7     Document Type: Article

References (49)

1. Gariépy, J., and Kawamura, K. (2001). Vectorial delivery of macromolecules into cells using peptide-based vehicles. Trends Biotechnol. 19: 21-28.
2. Schwarze, S. R., Hruska, K. A., and Dowdy, S. F. (2000). Protein transduction: Unrestricted delivery into all cells? Trends Cell Biol. 10: 290-295.
3. Frankel, A. D., and Pabo, C. O. (1988). Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55: 1189-1193.
4. Fawell, S., et al. (1994). Tat-mediated delivery of heterologous proteins into cells. Proc. Natl. Acad. Sci. USA 91: 664-668.
5. Vivès, E., Brodin, P., and Lebleu, B. (1997). A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272: 16010-16017.
6. Schwarze, S. R., Ho, A., Vocero-Akbani, A., and Dowdy, S. F. (1999). In vivo protein transduction: Delivery of a biologically active protein into the mouse. Science 285: 1569-1572.
7. Ho, A., Schwarze, S. R., Mermelstein, S. J., Waksman, G., and Dowdy, S. F. (2001). Synthetic protein transduction domains: Enhanced transduction potential in vitro and in vivo. Cancer Res. 61: 474-477.
8. Silhol, M., Tyagi, M., Giacca, M., Lebleu, B., and Vives, E. (2002). Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat. Eur. J. Biochem. 269: 494-501.
9. Mann, D. A., and Frankel, A. D. (1991). Endocytosis and targeting of exogenous HIV-1 Tat protein. EMBO J. 10: 1733-1739.
10. Becker-Hapak, M., McAllister, S. S., and Dowdy, S. F. (2001). TAT-mediated protein transduction into mammalian cells. Methods 24: 247-256.
11. Park, J., et al. (2002). Mutational analysis of a human immunodeficiency virus type 1 Tat protein transduction domain which is required for delivery of an exogenous protein into mammalian cells. J. Gen. Virol. 83: 1173-1181.
12. Mai, J. C., Shen, H., Watkins, S. C., Cheng, T., and Robbins, P. D. (2002). Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate. J. Biol. Chem. 277: 30208-30218.
13. Rusnati, M., et al. (1997). Interaction of HIV-1 Tat protein with heparin. Role of the backbone structure, sulfation, and size. J. Biol. Chem. 272: 11313-11320.
14. Tyagi, M., Rusnati, M., Presta, M., and Giacca, M. (2001). Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans. J. Biol. Chem. 276: 3254-3261.
15. Rusnati, M., et al. (2001). Pentosan polysulfate as an inhibitor of extracellular HIV-1 Tat. J. Biol. Chem. 276: 22420-22425.
16. Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L., and Rothbard, J. B. (2000). The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters. Proc. Natl. Acad. Sci. USA 97: 13003-13008.
17. Suzuki, T., Futaki, S., Niwa, M., Tanaka, S., Uedo, K., and Sugiura, Y. (2002). Possible existence of common internalization mechanisms among arginine-rich peptides. J. Biol. Chem. 277: 2437-2443.
18. Futaki, S., et al. (2001). Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276:5836-5840.
19. Lewin, M., et al. (2000). Tat peptide-derivatized magnetic nanoparticles allow in vivo tracking and recovery of progenitor cells. Nat. Biotechnol. 18: 410-414.
20. Vocero-Akbani, A. M., Heyden, N. V., Lissy, N. A., Ratner, L., and Dowdy, S. F. (1999). Killing HIV-infected cells by transduction with an HIV protease-activated caspase-3 protein. Nat. Med. 5: 29-33.
21. Nagahara, H., et al. (1998). Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration. Nat. Med. 4: 1449-1452.
22. Xia, H., Mao, Q., and Davidson, B. L. (2001). The HIV Tat protein transduction domain improves the biodistribution of beta-glucuronidase expressed from recombinant viral vectors. Nat. Biotechnol. 19: 640-644.
23. Gius, D. R., Ezhevsky, S. A., Becker-Hapak, M., Naghara, H., Wei, M. C., and Dowdy, S. F. (1999). Transduced p161NK4a peptides inhibit hypophosphorylation of the retinoblastoma protein and cell cycle progression prior to activation of Cdk2 complexes in late G1. Cancer Res. 59: 2577-2580.
24. Harada, H., Hiraoka, M., and Kizaka-Kondoh, S. (2002). Antitumor effect of TAT-oxygen-dependent degradation-caspase-3 fusion protein specifically stabilized and activated in hypoxic tumor cells. Cancer Res. 62: 2013-2018.
25. Peitz, M., Pfannkuche, K., Rajewsky, K., and Edenhofer, F. (2002). Ability of the hydrophobic FGF and basic TAT peptides to promote cellular uptake of recombinant Cre recombinase: A tool for efficient genetic engineering of mammalian genomes. Proc. Natl. Acad. Sci. USA 99: 4489-4494.
26. Derossi, D., Joliot, A. H., Chassaing, G., and Prochiantz, A. (1994). The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269: 10444-10450.
27. Derossi, D., Calvet, S., Trembleau, A., Brunissen, A., Chassaing, G., and Prochiantz, A. (1996). Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 271: 18188-18193.
28. Pietersz, G. A., Li, W., and Apostolopoulos, V. (2001). A 16-mer peptide (RQIKIWFQN-RRMKWKK) from antennapedia preferentially targets the Class I pathway. Vaccine 19: 1397-1405.
29. Elliott, G., and O'Hare, P. (1997). Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88: 223-233.
30. Brewis, N., Phelan, A., Webb, J., Drew, J., Elliott, G., and O'Hare, P. (2000). Evaluation of VP22 spread in tissue culture. J. Virol. 74: 1051-1056.
31. Aints, A., Dilber, M. S., and Smith, C. I. E. (1999). Intercellular spread of GFP-VP22. J. Gene Med. 1: 275-279.
32. Elliott, G., and O'Hare, P. (1999). Intercellular trafficking of VP22-GFP fusion proteins. Gene Ther. 6: 149-151.
33. Wybranietz, W. A., et al. (1999). Quantification of VP22-GFP spread by direct fluorescence in 15 commonly used cell lines. J. Gene Med. 1: 265-274.
34. Kueltzo, L. A., Normand, N., O'Hare, P., and Middaugh, C. R. (2000). Conformational lability of herpesvirus protein VP22. J. Biol. Chem. 275: 33213-33221.
35. Dilber, M. S., et al. (1999). Intercellular delivery of thymidine kinase prodrug activating enzyme by the herpes simplex virus protein, VP22. Gene Ther. 6: 12-21.
36. Phelan, A., Elliott, G., and O'Hare, P. (1998). Intercellular delivery of functional p53 by the herpesvirus protein VP22. Nat. Biotechnol. 16: 440-443.
37. Lundberg, M., and Johansson, M. (2001). Is VP22 nuclear homing an artifact? Nat. Biotechnol. 19: 713-714.
38. Lundberg, M., and Johansson, M. (2002). Positively charged DNA-binding proteins cause apparent cell membrane translocation. Biochem. Biophys. Res. Commun. 291: 367-371.
39. Falnes, P. O., Wesche, J., and Olsnes, S. (2001). Ability of the Tat basic domain and VP22 to mediate cell binding, but not membrane translocation of the diphtheria toxin A-fragment. Biochemistry 40: 4349-4358.
40. Leifert, J. A., Harkins, S., and Whitton, J. L. (2002). Full-length proteins attached to the HIV tat protein transduction domain are neither transduced between cells, nor exhibit enhanced immunogenicity. Gene Ther. 9: 1422-1428.
41. Jo, D., et al. (2001). Epigenetic regulation of gene structure and function with a cell-permeable Cre recombinase. Nat. Biotechnol. 19: 929-933.
42. Joshi, S. K., Hashimoto, K., and Koni, P. A. (2002). Induced DNA recombination by Cre recombinase protein transduction. Genesis 33: 48-54.
43. Bennett, R. P., Dalby, B., and Guy, P. M. (2002). Protein delivery using VP22. Nat. Biotechnol. 20: 20.
44. Conant, K., Ma, M., Nath, A., and Major, E. O. (1996). Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. J. Virol. 70:1384-1389.
45. Borgatti, P., Zauli, G., Cantley, L. C., and Capitani, S. (1998). Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. Biochem. Biophys. Res. Commun. 242: 332-337.
46. Chesnoy, S., and Huang, L. (2000). Structure and function of lipid-DNA complexes for gene delivery. Annu. Rev. Biophys. Biomol. Struct. 29: 27-47.
47. Godbey, W. T., Wu, K. K., and Mikos, A. G. (1999). Tracking the intracellular path of poly(ethylenimine)/DNA complexes for gene delivery. Proc. Natl. Acad. Sci. USA 96: 5177-5181.
48. Will, E., et al. (2002). Unmodified Cre recombinase crosses the membrane. Nucleic Acids Res. 30: e59.
49. Richard, J. P., et al. (2003). Cell-penetrating peptides: A reevaluation of the mechanism of cellular uptake. J. Biol. Chem. 278: 585-590.