Phenotype-dependent differences in proteasome subunit composition and cleavage specificity in B cell lines

Journal of Immunology

Volumn 160, Issue 7, 1998, Pages 3281-3289

  Frisan, Teresa ^a,c   Levitsky, Victor ^a   Polack, Axel ^b   Masucci, Maria G ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b Gesell F Strahlung U   (Germany)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA INTERFERON; PROTEASOME;

ARTICLE; B LYMPHOCYTE ACTIVATION; B LYMPHOCYTE DIFFERENTIATION; BURKITT LYMPHOMA; DOWN REGULATION; ENZYME INDUCTION; ENZYME SPECIFICITY; ENZYME SUBUNIT; GROWTH REGULATION; HUMAN; HUMAN CELL; IMMUNOGENICITY; IMMUNOREGULATION; LYMPHOCYTE TRANSFORMATION; PRIORITY JOURNAL; PROTEIN EXPRESSION;

B-LYMPHOCYTE SUBSETS; BURKITT LYMPHOMA; CELL LINE, TRANSFORMED; CYSTEINE ENDOPEPTIDASES; ENZYME ACTIVATION; EPITOPES; EPSTEIN-BARR VIRUS NUCLEAR ANTIGENS; HERPESVIRUS 4, HUMAN; HUMANS; HYDROLYSIS; INTERFERON TYPE II; MULTIENZYME COMPLEXES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BIOSYNTHESIS; TUMOR CELLS, CULTURED; VIRAL MATRIX PROTEINS;

EID: 0032055569     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (63)

1. Townsend, A., and J. Trowsdale. 1993. The transporters associated with antigen presentation. Semin. Cell Biol. 4:53.
2. Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A. L. Goldberg. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761.
3. Michalek, M. T., E. P. Grant, C. Gramm, A. L. Goldberg, and K. L. Rock. 1993. A role for ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Nature 363:552.
4. Lupas, A., A. J. Koster, and W. Baumeister. 1993. Structural features of 26S and 20S proteasomes. Enzyme Protein 47:252.
5. Tanaka, K., T. Tamura, T. Yoshimura, and A. Ichihara. 1992. Proteasomes: protein and gene structure. New Biol. 4:173.
6. Zwickl, P., A. Grziwa, G. Puhler, B. Dahlmann, F. Lottspeich, and W. Baumeister. 1992. Primary structure of the Thermoplasma proteasome and its implications for the structure, function and evolution of the multicatalytic proteinase. Biochemistry 31:964.
7. Seemüller, E., A. Lupas, D. Stock, J. Löwe, R. Huber, and W. Baumeister. 1995. Proteasome from Thermoplasma acidophylum: a threonine protease. Science 268: 579.
8. Glynne, R., S. Powis, S. Beck, A. Kelly, L. Kerr, and J. Trowsdale. 1991. A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC. Nature 353:357.
9. Kelly, A., S. Powis, R. Glynne, E. Radley, S. Beck, and J. Trowsdale. 1991. Second proteasome-related gene in the human MHC class II region. Nature 353: 667.
10. Monaco, J., and H. McDevitt. 1984. H-2-linked low-molecular weight polypeptide antigens assemble into an unusual macromolecular complex. Nature 309: 797.
11. Aki, M., N. Shimbara, M. Takashina, K. Akiyama, S. Kagawa, T. Tamura, N. Tanahashi, T. Yoshimura, K. Tanaka, and A. Ichihara. 1994. Interferon-γ induces different subunit organizations and functional diversity of proteasomes. J. Biochem. 115:257.
12. Groettrup, M., R. Kraft, S. Kostka, S. Standera, R. Stohwasser, and P. M. Kloetzel. 1996. A third interferon-γ-induced subunit exchange in the 20S proteasome. Eur. J. Immunol. 26:863.
13. Hisamatsu, H., N. Shimbara, Y. Saito, P. Kristensen, K. B. Hendil, T. Fujiwara, E. Takahashi, N. Tanahashi, T. Tamura, A. Ichihara, and K. Tanaka. 1996. Newly identified pair of proteasomal subunits regulated reciprocally by interferon-γ. J. Exp. Med. 183:1807.
14. Cardozo, C. 1993. Catalytic components of the bovine pituitary multicatalytic proteinase complex (proteasome). Enzyme Protein 47:296.
15. Gaczynska, M., K. L. Rock, and A. L. Goldberg. 1993. Nature 365:264.
16. Driscoll, J., M. G. Brown, D. Finley, and J. J. Monaco. 1993. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 365:262.
17. Gregory, C. D., T. Tursz, C. F. Edwards, C. Tetaud, M. Talbot, B. Caillou, A. B. Rickinson, and M. Lipinski. 1987. Identification of a subset of normal B cells with a Burkitt's lymphoma (BL)-like phenotype. J. Immunol. 139:313.
18. Rickinson, A., R. Murray, J. Brooks, H. Griffin, D. Moss, and M. Masucci. 1992. T cell recognition of Epstein-Barr virus associated lymphomas. In A New Look at Tumor Immunology, Vol. 13. A. McMichael and L. Franks, eds. CSHL Press, New York, pp. 53-80.
19. Rowe, M., D. T. Rowe, C. D. Gregory, L. S. Young, P. J. Farrell, H. Rupani, and A. B. Rickinson. 1987. Differences in B cell growth phenotype reflect novel patterns of Epstein-Barr virus latent gene expression in Burkitt's lymphoma. EMBO J. 6:2743.
20. Rooney, C. M., M. Rowe, L. E. Wallace, and A. B. Rickinson. 1985. Epstein-Barr virus-positive Burkitt's lymphoma cells not recognized by virus-specific T-cell surveillance. Nature 317:629.
21. Khanna, R., S. R. Burrows, V. Argaet, and D. J. Moss. 1994. Endoplasmic reticulum signal sequence facilitated transport of peptide epitopes restores immunogenicity of an antigen processing defective tumour cell line. Int. Immunol. 6:639.
22. Rowe, M., R. Khanna, C. A. Jacob, V. Argaet, A. Kelly, S. Powis, M. Belich, D. Croom-Carter, S. Lee, S. R. Burrows, J. Trowsdale, D. J. Moss, and A. B. Rickinson. 1995. Restoration of endogenous antigen processing in Burkitt's lymphoma cells by Epstein-Barr virus latent membrane protein-1: coordinate up-regulation of peptide transporters and HLA-class I antigen expression. Eur. J. Immunol. 25:1374.
23. Frisan, T., Q.-J. Zhang, J. Levitskaya, M. Coram, M. G. Kurilla, and M. G. Masucci. 1996. Defective presentation of MHC class I-restricted cytotoxic T-cell epitopes in Burkitt's lymphoma cells. Int. J. Cancer 68:251.
24. Lenoir, G. M., M. Vuillaume, and C. Bonnardel. 1985. The use of lymphomatous and lymphoblastoid cell lines in the study of Burkitt's lymphoma. In Burkitt's Lymphoma: A Human Cancer Model, Vol. 60. G. M. Lenoir, G. T. O'Conor, and C. L. M. Olweny, eds. International Agency for Research on Cancer Scientific Publications, Lyon, pp. 309-318.
25. Diabata, M., R. E. Humphreys, K. Takada, and T. Sairenji. 1990. Activation of latent EBV via anti-IgG-triggered, second messenger pathways in the Burkitt's lymphoma cell line Akata. J. Immunol. 144:4788.
26. Rooney, C. M., C. D. Gregory, M. Rowe, S. Finerty, C. Edwards, H. Rupani, and A. B. Rickinson. 1986. Endemic Burkitt's lymphoma: phenotypic analysis of tumour biopsy cells and of the derived tumour cell lines. J. Natl. Cancer Inst. 77:681.
27. de Campos-Lima, P. O., V. Levitsky, J. Brooks, S. P. Lee, L. F. Hu, A. B. Rickinson, and M. G. Masucci. 1994. T cell responses and virus evolution: loss of HLA A11-restricted CTL epitopes in Epstein-Barr virus isolates from highly A11-positive populations by selective mutation of anchor residues. J. Exp. Med. 179:1297.
28. Salter, R. D., and P. Cresswell. 1986. Impaired assembly and transport of HLA-A and -B antigens in a mutant TxB cell hybrid. EMBO J. 5:943.
29. 1-regulating proteins by Epstein-Barr virus mutants conditional for EBNA2. EMBO J. 14:88.
30. Polack, A., K. Hörtnagel, A. Pajic, B. Christoph, B. Baier, M. Falk, J. Mautner, C. Geltinger, G. W. Bornkamm, and B. Kempkes. 1996. c-myc activation renders proliferation of Epstein-Barr virus (EBV)-transformed cells independent of EBV nuclear antigen 2 and latent membrane protein 1. Proc. Natl. Acad. Sci. USA 93:10411.
31. Hirs, C., and S. Timasheff. 1977. Methods of peptide synthesis. Methods Enzymol. 47:501.
32. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
33. Glynne, R., L.-A. Kerr, I. Mockridge, S. Beck, A. Kelly, and J. Trowsdale. 1993. The major histocompatibility complex-encoded proteasome component LMP7: alternate first exon and post-translational processing. Eur. J. Immunol. 23:860.
34. Mann, K. P., D. Staunton, and D. A. Thorley-Lawson. 1985. Epstein-Barr virus-encoded protein found in the plasma membranes of transformed cells. J. Virol. 55:710.
35. Hendil, K. B., P. Kristensen, and W. Uerkvitz. 1995. Human proteasomes analysed with monoclonal antibodies. Biochem. J. 305:245.
36. Blum, H., H. Beier, and H. J. Gross. 1987. Improved silver staining of plant protein, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93.
37. Lehninger, A. L., D. L. Nelson, and M. M. Cox. 1993. Principles of Biochemistry. Worth Publishers, New York.
38. Heemels, M. T., T. N. Schumacher, K. Wonigeit, and H. L. Ploegh. 1993. Peptide translocation by variants of the transporter associated with antigen processing. Science 262:2059.
39. Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368.
40. Hoffman, L., and M. Rechsteiner. 1994. Activation of the multicatalytic protease. J. Biochem. 269:16890.
41. Boes, B., H. Hengel, T. Ruppert, G. Multhaup, U. H. Koszinowski, and P.-M. Kloetzel. 1994. Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J. Exp. Med. 179:901.
42. Brown, M. G., J. Driscoll, and J. J. Monaco. 1993. MHC-linked low molecular mass polypeptide subunits define distinct subsets of proteasomes. J. Immunol. 151:1193.
43. Groettrup, M., T. Ruppert, L. Kuehn, M. Seeger, S. Standera, U. Koszinowski, and P.-M. Kloetzel. 1995. The interferon-γ-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro J. Biol. Chem. 270:23808.
44. Kuckelkom, U., S. Frentzel, R. Kraft, S. Kostka, M. Groettrup, and P.-M. Kloetzel. 1995. Incorporation of major histocompatibility complex-encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon-γ. Eur. J. Immunol. 25:2605.
45. Stohwasser, R., U. Kuckelkorn, R. Kraft, S. Kostka, and P. M. Kloetzel. 1996. 20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences. FEBS Lett. 383:109.
46. Driscoll, A. D., M. Androlewicz, E. Hughes, P. Cresswell, and T. Spies. 1992. Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules. Nature 360:171.
47. Momburg, F., V. Ortiz-Navarrete, J. Neefjes, E. Goulmy, Y. van de Wal, H. Spits, S. J. Powis, G. W. Butcher, J. C. Howard, P. Walden, and G. J. Hämmerling. 1992. Proteasome subunits encoded by the major histocompatibility complex are not essential for antigen presentation. Nature 360:174.
48. d in proteasome subunit LMP2-and LMP7-deficient cells. Eur. J. Immunol. 24:1863.
49. Hendil, K. B. 1988. The 19S multicatalytic "prosome" proteinase is a constitutive enzyme in HeLa cells. Biochem. Int. 17:471.
50. Dick, P. T., T. Ruppert, M. Groettrup, P. M. Kloetzel, L. Kuehn, U. H. Koszinowski, S. Stevanovic, H. Schild, and H.-G. Rammensee. 1996. Coordinated dual cleavages induced by proteasome regulator PA28 lead to dominant MHC ligands. Cell 86:253.
51. Groettrup M., A. Soza, M. Eggers, L. Kuehn, T. P. Dick, H. Schild, H.-G. Rammensee, U. H. Koszinowski, and P. M. Kloetzel. 1996. A role for the proteasome regulator PA28. Nature 381:166.
52. Ahn, J. Y., N. Tanahashi, K. Akiyama, H. Hisamatsu, C. Noda, K. Tanaka, C. H. Chung, N. Shimbara, P. J. Willy, J. D. Mott, C. A. Slaughter, and G. N. DeMartino. 1995. Primary structures of two homologue subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome. FEBS Lett. 366:37.
53. Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726.
54. de Campos-Lima, P.-O., J. Levitskaya, T. Frisan, and M. G. Masucci. 1996. Strategies of immunoescape in Epstein-Barr virus persistence and pathogenesis. Semin. Virol. 7:75.
55. Restifo, N. P., F. Esquivel, Y. Kawakami, J. W. Yewdell, J. J. Mule, S. A. Rosenberg, and J. R. Bennink. 1993. Identification of human cancers deficient in antigen processing. J. Exp. Med. 177:265.
56. Selinger, B., A. Höhne, A. Knuth, H. Bernhard, T. Meyer, R. Tampe, F. Momburg, and C. Huber. 1995. Analysis of the major histocompatibility complex class I antigen presentation machinery in normal and malignant renal cells: evidence for deficiencies associated with transformation and progression. Cancer Res. 56:1756.
57. Miyashita, E. M., B. Yang, K. M. Lam, D. H. Crawford, and D. A. Thorley-Lawson. 1995. A novel form of Epstein-Barr virus latency in normal B cells in vivo. Cell 80:593.
58. Qu, L., and D. T. Rowe. 1992. Epstein-Barr virus latent gene expression in uncultured peripheral blood lymphocytes. J. Virol. 66:3715.
59. Chen, F., J.-Z. Zou, L. Di Renzo, G. Winberg. L.-F. Hu, E. Klein, G. Klein, and E. Ernberg. 1995. A subpopulation of normal B cells latently infected with Epstein-Barr virus resembles Burkitt lymphoma cells in expressing EBNA-1 but not EBNA-2 or LMP1. J. Virol. 69:3752.
60. Tierney, R. J., N. Steven, L. S. Young, and A. B. Rickinson. 1994. Epstein-Barr virus latency in blood mononuclear cells: analysis of viral gene transcription during primary infection and in the carrier state. J. Virol. 68:7374.
61. Levitskaya, J., M. Coram, V. Levitsky, S. Imreh, P. M. Steigerwald-Mullen, G. Klein, M. G. Kurilla, and M. G. Masucci. 1995. Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1. Nature 375:685.
62. Masucci, M. G., and I. Ernberg. 1994. Epstein-Barr virus adaptation to a life within the immune system. Trends Microbiol. 2:125.
63. Lee, S. P., W. A. Thomas, N. W. Blake, and A. B. Rickinson. 1996. Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2. Eur. J. Immunol. 26:1875.