The roles of γ1 heavy chain membrane expression and cytoplasmic tail in IgG1 responses

Science

Volumn 276, Issue 5311, 1997, Pages 412-415

  Kaisho, Tsuneyasu ^a,b   Schwenk, Frieder ^a   Rajewsky, Klaus ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b HYOGO COLLEGE OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE ANTIGEN; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN HEAVY CHAIN; LYMPHOCYTE ANTIGEN RECEPTOR;

ANIMAL CELL; ANIMAL EXPERIMENT; ANTIBODY RESPONSE; ANTIGEN PRESENTATION; ARTICLE; B LYMPHOCYTE; CELL SURFACE; CONTROLLED STUDY; CYTOPLASM; IMMUNIZATION; IMMUNOGLOBULIN PRODUCTION; INTERNALIZATION; MEMORY CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANIMALIA;

EID: 0030994044     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.276.5311.412     Document Type: Article

References (31)

1. M. Reth, Annu. Rev. Immunol. 10, 97 (1992).
2. C. Esser and A. Radbruch, ibid. 8, 717 (1990).
3. Δtail/Δtail mice confirmed that the stop codon had been introduced and revealed no unexpected mutations in any of the exons encoding the IgG1 constant region.
4. Δtail/Δtail mice confirmed that the stop codon had been introduced and revealed no unexpected mutations in any of the exons encoding the IgG1 constant region.
5. Δtail/Δtail mice confirmed that the stop codon had been introduced and revealed no unexpected mutations in any of the exons encoding the IgG1 constant region.
6. Δtail/Δtail mice confirmed that the stop codon had been introduced and revealed no unexpected mutations in any of the exons encoding the IgG1 constant region.
7. Δtail/Δtail mice confirmed that the stop codon had been introduced and revealed no unexpected mutations in any of the exons encoding the IgG1 constant region.
8. H. Gu, Y. Zou, K. Rajewsky, Cell 73, 1155 (1993).
9. F. Schwenk, U. Baron, K. Rajewsky, Nucleic Acids Res. 23, 5080 (1995).
10. J. E. Layton, E. S. Vitteta, J. W. Uhr, P. H. Krammer, J. Exp. Med. 160, 1850 (1984).
11. T. Kaisho, F. Schwenk, K. Rajewsky, data not shown.
12. K. Okumura, M. H. Julius, T. Tsu, L. A. Herzenberg, L. A. Herzenberg, Eur. J. Immunol. 6, 467 (1976); H. Shan, M. Schlomchik, M. Weigert, J. Exp. Med. 172, 531 (1990).
13. K. Okumura, M. H. Julius, T. Tsu, L. A. Herzenberg, L. A. Herzenberg, Eur. J. Immunol. 6, 467 (1976); H. Shan, M. Schlomchik, M. Weigert, J. Exp. Med. 172, 531 (1990).
14. 14-bovine serum albumin (5 μg/ml). Cells were washed and incubated with fluorescein isothiocyanate (FITC)-conjugated sheep anti-digoxigenin Fab fragments (Boehringer, Mannheim), the phycoerythrin-conjugated mAb R33-24-12 to IgM [R. Grützman, thesis, University of Cologne, Germany (1981 )], the phycoerythrin-conjugated mAb 1.3-5 to IgD [J. Roes, W. Müller, K. Rajewsky, J. Immunol. Methods 183, 231 (1995)], and the allophycocyanin-conjugated mAb S43 to NP [M. Reth, G. J. Hämmerling, K. Rajewsky, Eur. J. Immunol. 8, 393 (1978)]. Cells were analyzed on a FAC-Star (Becton Dickinson, San Jose, CA). Dead cells were excluded by propidium iodide staining.
15. 14-bovine serum albumin (5 μg/ml). Cells were washed and incubated with fluorescein isothiocyanate (FITC)-conjugated sheep anti-digoxigenin Fab fragments (Boehringer, Mannheim), the phycoerythrin-conjugated mAb R33-24-12 to IgM [R. Grützman, thesis, University of Cologne, Germany (1981 )], the phycoerythrin-conjugated mAb 1.3-5 to IgD [J. Roes, W. Müller, K. Rajewsky, J. Immunol. Methods 183, 231 (1995)], and the allophycocyanin-conjugated mAb S43 to NP [M. Reth, G. J. Hämmerling, K. Rajewsky, Eur. J. Immunol. 8, 393 (1978)]. Cells were analyzed on a FAC-Star (Becton Dickinson, San Jose, CA). Dead cells were excluded by propidium iodide staining.
16. 14-bovine serum albumin (5 μg/ml). Cells were washed and incubated with fluorescein isothiocyanate (FITC)-conjugated sheep anti-digoxigenin Fab fragments (Boehringer, Mannheim), the phycoerythrin-conjugated mAb R33-24-12 to IgM [R. Grützman, thesis, University of Cologne, Germany (1981 )], the phycoerythrin-conjugated mAb 1.3-5 to IgD [J. Roes, W. Müller, K. Rajewsky, J. Immunol. Methods 183, 231 (1995)], and the allophycocyanin-conjugated mAb S43 to NP [M. Reth, G. J. Hämmerling, K. Rajewsky, Eur. J. Immunol. 8, 393 (1978)]. Cells were analyzed on a FAC-Star (Becton Dickinson, San Jose, CA). Dead cells were excluded by propidium iodide staining.
17. B. Pulendran, K. G. C. Smith, G. J. V. Nossal, J. Immunol. 155, 1141 (1995).
18. K. Rajewsky, Nature 381, 751 (1996).
19. G. Achatz, L. Nitschke, M. C. Lamers, Science 276, 409 (1997).
20. P. Weiser, R. Müller, U. Braun, M. Reth, ibid., p. 407.
21. K. M. Kim, G. Alber, P. Weiser, M. Reth, Eur. J. Immunol. 23, 911 (1993).
22. Y.-J. Liu et al., Immunity 2, 239 (1995).
23. A. R. Venkitaraman et al., Nature 352, 777 (1991); P. Weiser, C. Riesterer, M. Reth, Eur. J. Immunol. 24, 665 (1994).
24. A. R. Venkitaraman et al., Nature 352, 777 (1991); P. Weiser, C. Riesterer, M. Reth, Eur. J. Immunol. 24, 665 (1994).
25. 6 cells/ml) were cultured in complete Roswell Park Memorial Institute medium supplemented with LPS (40 μg/ml) and 10% culture supernatant of an IL-4-expressing NIH 3T3 line [S. Jung, K. Rajewsky, A. Radbruch, Science 259, 984 (1993)]. After 3 days of culture, cells were harvested, incubated with the digoxigenin-conjugated rat mAb to murine IgG1 (Miltenyi Biotec, Bergisch Gladbach, Germany), and stained by FITC-conjugated sheep anti-digoxigenin Fab fragments (Boehringer, Mannheim). Intracellular staining was performed as described [M. Assenmacher, J. Schmitz, A. Radbruch, Eur. J. Immunol. 24, 1097 (1994)]. Cells were analyzed on a FACScan (Becton Dickinson, San Jose, CA).
26. 6 cells/ml) were cultured in complete Roswell Park Memorial Institute medium supplemented with LPS (40 μg/ml) and 10% culture supernatant of an IL-4-expressing NIH 3T3 line [S. Jung, K. Rajewsky, A. Radbruch, Science 259, 984 (1993)]. After 3 days of culture, cells were harvested, incubated with the digoxigenin-conjugated rat mAb to murine IgG1 (Miltenyi Biotec, Bergisch Gladbach, Germany), and stained by FITC-conjugated sheep anti-digoxigenin Fab fragments (Boehringer, Mannheim). Intracellular staining was performed as described [M. Assenmacher, J. Schmitz, A. Radbruch, Eur. J. Immunol. 24, 1097 (1994)]. Cells were analyzed on a FACScan (Becton Dickinson, San Jose, CA).
27. 4 bovine serum albumin, and the affinity of NP-specific IgG1 was calculated as described by Roes and Rajewsky.
28. 4 bovine serum albumin, and the affinity of NP-specific IgG1 was calculated as described by Roes and Rajewsky.
29. 4 bovine serum albumin, and the affinity of NP-specific IgG1 was calculated as described by Roes and Rajewsky.
30. I. Förster, P. Vieira, K. Rajewsky, Int. Immunol. 1, 321 (1989).
31. We thank R. Lamers and M. Reth for communicating results before publication. We also thank C. Uthoff-Haohenberg and C. Göttlinger for competent technical help, W. Müller for the method of detecting NP-specifc mlgG1-positive cells, R. C. Rickert and A. Tarakhovsky for critical reading of the manuscript, and U. Ringeisen for graphical work. Supported by fellowships from the Human Frontier Science Programme (HFSP) and the Alexander von Humboldt Foundation to TX. and by grants from the Deutsche Forschungsgemeinschaft through SFB 243, the HFSP, and the Land Nordrhein-Westfalen. F.S. was supported by a stipend of the Boehringer Ingelheim Fonds.