Generation of mouse macrophages expressing membrane-bound TNF variants with selectivity for TNFR1 or TNFR2

Cytokine

Volumn 50, Issue 1, 2010, Pages 75-83

  Shibata, Hiroko ^a,b   Abe, Yasuhiro ^a   Yoshioka, Yasuo ^a,c   Nomura, Tetsuya ^a,c   Sato, Masaki ^a   Kayamuro, Hiroyuki ^a,c   Kawara, Tomoyuki ^a,c   Arita, Shuhei ^a,c   Furuya, Tsuyoshi ^a,c   Nagano, Kazuya ^a   Yoshikawa, Tomoaki ^a,c   Kamada, Haruhiko ^a,c   Tsunoda, Shin ichi ^a,c   Tsutsumi, Yasuo ^a,c  

^a NATIONAL INSTITUTE OF BIOMEDICAL INNOVATION   (Japan)

^b NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

^c OSAKA UNIVERSITY   (Japan)

Author keywords

Lentiviral vector; Mutant TNF; TNFR1; TNFR2; Transmembrane TNF

Indexed keywords

TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL SPECIFICITY; CONTROLLED STUDY; MACROPHAGE; MEMBRANE BINDING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; RECEPTOR BINDING; SIGNAL TRANSDUCTION; WILD TYPE;

AMINO ACID SEQUENCE; ANIMALS; CELL DEATH; CELL MEMBRANE; GENETIC VECTORS; HUMANS; KINETICS; LENTIVIRUS; MACROPHAGES; MICE; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PROTEIN BINDING; RECEPTORS, TUMOR NECROSIS FACTOR, TYPE I; RECEPTORS, TUMOR NECROSIS FACTOR, TYPE II; SOLUBILITY; TUMOR NECROSIS FACTOR-ALPHA;

EID: 77049104259     PISSN: 10434666     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cyto.2009.11.022     Document Type: Article

References (24)

1. Aggarwal B.B. Signalling pathways of the TNF superfamily: a double-edged sword. Nat Rev Immunol 3 (2003) 745-756
2. Beutler B. Autoimmunity and apoptosis: the Crohn's connection. Immunity 15 (2001) 5-14
3. Feldmann M., and Maini R.N. Anti-TNF alpha therapy of rheumatoid arthritis: what have we learned?. Annu Rev Immunol 19 (2001) 163-196
4. Feldmann M. Development of anti-TNF therapy for rheumatoid arthritis. Nat Rev Immunol 2 (2002) 364-371
5. Kriegler M., Perez C., DeFay K., Albert I., and Lu S.D. A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell 53 (1988) 45-53
6. Tang P., Hung M.C., and Klostergaard J. Human pro-tumor necrosis factor is a homotrimer. Biochemistry 35 (1996) 8216-8225
7. Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L., Wolfson M.F., et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385 (1997) 729-733
8. Ruuls S.R., Hoek R.M., Ngo V.N., McNeil T., Lucian L.A., Janatpour M.J., et al. Membrane-bound TNF supports secondary lymphoid organ structure but is subservient to secreted TNF in driving autoimmune inflammation. Immunity 15 (2001) 533-543
9. Mueller C., Corazza N., Trachsel-Loseth S., Eugster H.P., Buhler-Jungo M., Brunner T., et al. Noncleavable transmembrane mouse tumor necrosis factor-alpha (TNFalpha) mediates effects distinct from those of wild-type TNFalpha in vitro and in vivo. J Biol Chem 274 (1999) 38112-38118
10. Olleros M.L., Guler R., Vesin D., Parapanov R., Marchal G., Martinez-Soria E., et al. Contribution of transmembrane tumor necrosis factor to host defense against Mycobacterium bovis bacillus Calmette-guerin and Mycobacterium tuberculosis infections. Am J Pathol 166 (2005) 1109-1120
11. Saunders B.M., Tran S., Ruuls S., Sedgwick J.D., Briscoe H., and Britton W.J. Transmembrane TNF is sufficient to initiate cell migration and granuloma formation and provide acute, but not long-term, control of Mycobacterium tuberculosis infection. J Immunol 174 (2005) 4852-4859
12. Torres D., Janot L., Quesniaux V.F., Grivennikov S.I., Maillet I., and Sedgwick J.D. Membrane tumor necrosis factor confers partial protection to Listeria infection. Am J Pathol 167 (2005) 1677-1687
13. Aggarwal B.B., Eessalu T.E., and Hass P.E. Characterization of receptors for human tumour necrosis factor and their regulation by gamma-interferon. Nature 318 (1985) 665-667
14. Micheau O., and Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114 (2003) 181-190
15. Perez C., Albert I., DeFay K., Zachariades N., Gooding L., and Kriegler M. A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact. Cell 63 (1990) 251-258
16. Bryde S., Grunwald I., Hammer A., Krippner-Heidenreich A., Schiestel T., Brunner H., et al. Tumor necrosis factor (TNF)-functionalized nanostructured particles for the stimulation of membrane TNF-specific cell responses. Bioconjug Chem 16 (2005) 1459-1467
17. Shibata H., Yoshioka Y., Ohkawa A., Minowa K., Mukai Y., Abe Y., et al. Creation and X-ray structure analysis of the tumor necrosis factor receptor-1-selective mutant of a tumor necrosis factor-alpha antagonist. J Biol Chem 283 (2008) 998-1007
18. Mukai Y., Shibata H., Nakamura T., Yoshioka Y., Abe Y., Nomura T., et al. Structure-function relationship of tumor necrosis factor (TNF) and its receptor interaction based on 3D structural analysis of a fully active TNFR1-selective TNF mutant. J Mol Biol 385 (2009) 1221-1229
19. Abe Y., Yoshikawa T., Kamada H., Shibata H., Nomura T., Minowa K., et al. Simple and highly sensitive assay system for TNFR2-mediated soluble- and transmembrane-TNF activity. J Immunol Methods 335 (2008) 71-78
20. Katayama K., Wada K., Miyoshi H., Ohashi K., Tachibana M., Furuki R., et al. RNA interfering approach for clarifying the PPARgamma pathway using lentiviral vector expressing short hairpin RNA. FEBS Lett 560 (2004) 178-182
21. Miyoshi H., Smith K.A., Mosier D.E., Verma I.M., and Torbett B.E. Transduction of human CD34+ cells that mediate long-term engraftment of NOD/SCID mice by HIV vectors. Science 283 (1999) 682-686
22. Decoster E., Vanhaesebroeck B., Vandenabeele P., Grooten J., and Fiers W. Generation and biological characterization of membrane-bound, uncleavable murine tumor necrosis factor. J Biol Chem 270 (1995) 18473-18478
23. Grell M., Douni E., Wajant H., Lohden M., Clauss M., Maxeiner B., et al. The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor. Cell 83 (1995) 793-802
24. Krippner-Heidenreich A., Tubing F., Bryde S., Willi S., Zimmermann G., and Scheurich P. Control of receptor-induced signaling complex formation by the kinetics of ligand/receptor interaction. J Biol Chem 277 (2002) 44155-44163