Conjugation of antisense oligonucleotides to PEGylated carbon Nanotubes enables efficient knockdown of PTPN22 in T lymphocytes

Bioconjugate Chemistry

Volumn 20, Issue 3, 2009, Pages 427-431

  Delogu, Lucia G ^a   Magrini, Andrea ^b   Bergamaschi, Antonio ^c   Rosato, Nicola ^b   Dawson, Marcia I ^d   Bottini, Nunzio ^a,e   Bottini, Massimo ^b,d,e  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

^c CATHOLIC UNIVERSITY   (Italy)

^d BURNHAM INSTITUTE   (United States)

^e Institute for Medical Research   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; BIOCOMPATIBILITY; COVALENT BONDS; ELECTROPHORESIS; GENES; OLIGONUCLEOTIDES; POLYMERASE CHAIN REACTION; PROTEINS; SULFUR COMPOUNDS; T-CELLS; YARN;

ANTISENSE OLIGONUCLEOTIDES; AUTOIMMUNE DISEASE; DISULPHIDE BONDS; IN-VIVO; NANOCARRIERS; PEGYLATED; PROTEIN-TYROSINE PHOSPHATASE; T LYMPHOCYTES; TARGET GENES; TYPE 1 DIABETES;

CARBON NANOTUBES;

ANTISENSE OLIGONUCLEOTIDE; CARBON NANOTUBE; DITHIOTHREITOL; MACROGOL; NANOCARRIER; PEGYLATED CARBON NANOTUBE PROTEIN TYROSINE PHOSPHATASE N22 ANTISENSE OLIGONUCLEOTIDE CONJUGATE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE N22; UNCLASSIFIED DRUG; MACROGOL DERIVATIVE; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 22; PTPN22 PROTEIN, HUMAN;

AGAR GEL ELECTROPHORESIS; ARTICLE; ATOMIC FORCE MICROSCOPY; BIOCOMPATIBILITY; CONTROLLED STUDY; CYTOTOXICITY; DISULFIDE BOND; GENE TARGETING; HUMAN; HUMAN CELL; LYMPHOCYTE CULTURE; PROTEIN EXPRESSION; REAL TIME POLYMERASE CHAIN REACTION; SPECTROSCOPY; T LYMPHOCYTE; WESTERN BLOTTING; CHEMISTRY; GENE SILENCING; GENETICS; JURKAT CELL LINE; METABOLISM;

GENE KNOCKDOWN TECHNIQUES; HUMANS; JURKAT CELLS; NANOTUBES, CARBON; OLIGONUCLEOTIDES, ANTISENSE; POLYETHYLENE GLYCOLS; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 22; T-LYMPHOCYTES;

EID: 63749120634     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc800540j     Document Type: Article

References (35)

1. Scherer, L. J., and Rossi, J. J. (2003) Approach for the sequence-specific knockdown of MRNA. Nat. Biotechnol. 21, 1457-65.
2. Crooke, S. T. (2004) Progress in antisense technology. Annu. Rev. Med. 55, 61-95.
3. Kurreck, J. (2003) Antisense technologies. Improvement through novel chemical modification. Eur. J. Biochem. 270, 1628-44.
4. Chan, J. H., Lim, S., and Wong, W. S. (2006) Andsense oligonucleotides: from design to therapeutic application. Clin. Exp. Pharmacol. Physiol. 33, 533-40.
5. Eckstein, F. (2000) Phosphorothioate oligonucleotides: What is their origin and what is unique about them? Antisense Nucleic Acids Drug Dev. 10, 117-21.
6. Lysik, M. A., and Wu-Pong, S. (2003) Innovations in oligonucleotide drug delivery. J. Pharm. Sci. 92, 1559-73.
7. Marshall, N. B., Oda, S. K., London, C. A., Moulton, H. M., Iversen, P. L., Kerkvliet, N. I., and Mourich, D. V. (2007) Arginine-rich cell-penetrating peptides facilitate delivery of antisense oligomers into murine leukocytes and alter pre-mRNA splicing. J. Immunol. Methods 325, 114-26.
8. Moghimi, S. M., Hunter, A. C., and Murray, J. C. (2005) Nanomedicine: current status and future. FASEB J. 19, 311-30.
9. Bianco, A., Kostarelos, K., Partidos, C. D., and Prato, M. (2005) Biomedical applications of functionalized carbon nanotubes. Chem. Commun. 571-7.
10. Bottini, M., Cerignoli, F., Dawson, M. I., Magrini, A., Rosato, N., and Mustelin, T. (2006) Full-length single-walled carbon nanotubes decorated with streptavidin-conjugated quantum dots as multivalent intracellular fluorescent nanoprobes. Biomacro-molecules 7, 2259-63.
11. Kam, N. W. S., Liu, Z., and Dai, H. (2005) Functionalization of carbon nanotubes via cleavable disulfide bond for efficient intracellular delivery of siRNA and potent gene silencing. J. Am. Chem. Soc. 127, 12492-3.
12. Liu, Z., Cai, W., He, L., Nakayama, N., Chen, K., Sun, X., Chen, X., and Dai, H. (2007) In vivo biodistribution and highly efficient tumor targeting of carbon nanotubes in mice. Nat. Nanotechnol. 2, 47-52.
13. Liu, Z., Davis, C., Cai, W., He, L., Chen, X., and Dai, H. (2008) Circulation and long-term fate of functionalized, biocompatible single-walled carbon nanotubes in mice probed by Raman spectroscopy. Proc. Natl. Sci. U.S.A. 105, 1410-5.
14. Schipper, M. L., Nakayama-Ratchford, N., Davis, C. R., Kam, N. W., Chu, P., Liu, Z., Sun, X., Dai, H., and Gambhir, S. S. (2008) A pilot toxicology study of single-walled carbon nanotubes in a small sample of mice. Nat. Nanotechnol. 3, 216-21.
15. Cato, M. H., D'Annibale, F., Mills, D. M., Cerignoli, F., Dawson, M. I., Bergamaschi, E., Bottini, N., Magrini, A., Bergamaschi, A., Rosato, N., Rickert, R. C., Musteln, T., and Bottini, M. (2008) Cell-type specific and cytoplasmic targeting of PEGylated carbon nanotube-based nanoassemblies. J. Nanosci. Nanotechnol. 8, 2259-69.
16. Bottini, N., Vang, T., Cucca, F, and Mustelin, T. (2006) Role of PTPN22 in type 1 diabetes and other autoimmune diseases. Semin. Immunol. 18, 207-13.
17. Gregersen, P. K., Lee, H. S., Batliwalla, E, and Begovich, A. B. (2006) PTPN22: setting thresholds for autoimmunity. Semin. Immunol. 18, 214-23.
18. Yu, X., Sun, J. P., He, Y., Guo, X., Liu, S., Zhou, B., Hudmon, A., and Zhang, Z. Y. (2007) Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases. Proc. Natl. Acad. Sci. U.S.A. 104, 19767-72.
19. Bottini, N., Musumeci, L., Alonso, A., Rahmouni, S., Nika, K., Rostamkhani, M., MacMurray, J., Meloni, G. F., Lucarelli, P., Pellecchia, M., Eisenbarth, G. S., Comings, D., and Mustehn, T. (2004) A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes. Nat. Genet. 36, 337-8.
20. Smyth, D., Cooper, J. D., Collins, J. E., Heward, J. M., Franklyn, J. A., Howson, J. M., Vella, A., Nutland, S., Ranee, H. E., Maier, L., Barratt, B. J., Guja, C., Ionescu-Tirgoviste, C., Savage, D. A., Dunger, D. B., Widmer, B., Strachan, D. P., Ring, S. M., Walker, N., Clayton, D. G, Twells, R. C., Gough, S. C., and Todd, J. A. (2004) Replication of an association between the lymphoid tyrosine phosphatase locus (LYP/PTPN22) with type 1 diabetes, and evidence for its role as a general autoimmunity locus. Diabetes 53, 3020-3.
21. Onengut-Gumuscu, S., Ewens, K. G, Spielman, R. S., and Concannon, P. (2004) A functional polymorphism (1858C/T) in the PTPN22 gene is linked and associated with type I diabetes in multiplex families. Genes Immun. 5, 678-80.
22. Todd, J. A., Walker, N. M., Cooper, J. D., Smyth, D. J., Downes, K., Plagnol, V., Bailey, R., Nejentsev, S., Field, S. F., Payne, E, Lowe, C. E., Szeszko, J. S., Hafier, J. P., Zeitels, L., Yang, J. H., Vella, A., Nutland, S., Stevens, H. E., Schuilenburg, H., Coleman, G, Maisuria, M., Meadows, W., Smink, L. J., Healy, B., Burren, O. S., Lam, A. A., Ovington, N. R., Allen, J., Adlem, E., Leung, H. T., Wallace, C., Howson, J. M., Guja, C., Ionescu-Tirgoviste, C., Simmonds, M. J., Heward, J. M., Gough, S. C., Dunger, D. B., Wicker, L. S., and Clayton, D. G. (2007) Robust associations of four new chromosome regions from genome-wide analyses of type 1 diabetes. Nat. Genet. 39, 857-64.
23. Begovich, A. B., Carlton, V. E., Honigberg, L. A., Schrodi, S. J., Chokkalingam, A. P., Alexander, H. C., Ardlie, K. G., Huang, Q., Smith, A. M., Spoerke, J. M., Conn, M. T., Chang, M., Chang, S. Y., Saiki, R. K., Catanese, J. J., Leong, D. U., Garcia, V. E., McAllister, L. B., Jeffery, D. A., Lee, A. T., Batliwalla, F., Remmers, E., Criswell, L. A., Seldin, M. F., Kastner, D. L., Amos, C. I., Sninsky, J. J., and Gregersen, P. K. (2004) A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis. Am. J. Hum. Genet. 75, 330-7.
24. Orozco, G, Sanchez, E., Gonzalez-Gay, M. A., Lopez-Nevot, M. A., Torres, B., Caliz, R., Ortego-Centeno, N., Jimenez-Alonso, J., Pascual-Salcedo, D., Balsa, A., de Pablo, R., Nunez-Roldan, A., Gonzalez-Escribano, M. F., and Martin, J. (2005) Association of a functional single-nucleotide polymorphism of PTPN22, encoding lymphoid protein phosphatase, with rheumatoid arthritis and systemic lupus erythematosus. Arthritis Rheum. 52, 219-24.
25. Gregersen, P. K. (2005) Gaining insight into PTPN22 and autoimmunity. Nat. Genet. 37, 1300-2.
26. Cloutier, J. F., and Veillette, A. (1999) Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase. J. Exp. Med. 189, 111-21.
27. Gjorloff-Wingren, A., Saxena, M., Williams, S., Hammi, D., and Mustelin, T. (1999) Characterization of TCR-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP. Eur. J. Immunol. 29, 3845-54.
28. Hill, R. J., Zozulya, S., Lu, Y. L., Ward, K., Gishizky, M., and Jallal, B. (2002) The lymphoid protein tyrosine phosphatase Lyp interacts with the adaptor molecule Grb2 and functions as a negative regulator of T-cell activation. Exp. Hematol. 30, 237-44.
29. Vang, T., Congia, M., Macis, M. D., Musumeci, L., Orrú, V., Zavattari, P., Nika, K., Tautz, L., Taskén, K., Cucca, F., Mustelin, T., and Bottini, N. (2005) Autoimmune-associated lymphoid tyrosine phosphatase is a gain-of-function variant. Nat. Genet. 37, 1317-9.
30. Rieck, M., Arechiga, A., Onengut-Gumuscu, S., Greenbaum, C., Concannon, P., and Buckner, J. H. (2007) Genetic variation in PTPN22 corresponds to altered function of T and B lymphocytes. J. Immunol. 179, 4704-10.
31. Sakaguchi, N., Takahashi, T., Hata, H., Nomura, T., Tagami, T., Yamazaki, S., Sakihama, T., Matsutani, T., Negishi, I., Nakatsuru, S., and Sakaguchi, S. (2003) Altered thymic T-cell selection due to a mutation of the ZAP-70 gene causes autoimmune arthritis in mice. Nature 426, 454-60.
32. Siggs, O. M., Miosge, L. A., Yates, A. L., Kucharska, E. M., Sheahan, D., Brdicka, T., Weiss, A., Liston, A., and Goodnow, C. C. (2007) Opposing functions of the T cell receptor kinase ZAP-70 in immunity and tolerance differentially titrate in response to nucleotide substitutions. Immunity 27, 912-26.
33. Northrop, J. P., Ullman, K. S., and Crabtree, G. R. (1993) Characterization of the nuclear and cytoplasmic components of the lymphoid-specific nuclear factor of activated T cells (NF-AT) complex. J. Biol. Chem. 268, 2917-23.
34. Pandey, S. K., Yu, X. X., Watts, L. M., Michael, M. D., Sloop, K. W., Rivard, A. R., Leedom, T. A., Manchem, V. P., Samadzadeh, L., McKay, R. A., Monia, B. P., and Bhanot, S. (2007) Reduction of low molecular weight protein-tyrosine phosphatase expression improves hyperglycemia and insulin sensitivity in obese mice. J Biol. Chem. 282, 14291-9.
35. Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., and Mustelin, T. (2004) Protein tyrosine phosphatases in the human genome. Cell 117, 699-711.