Double-cleavage production of the CTL epitope by proteasomes and PA28: Role of the flanking region

Genes to Cells

Volumn 2, Issue 12, 1997, Pages 785-800

  Shimbara, Naoki ^a,b   Nakajima, Hiroto ^a,b   Tanahashi, Nobuyuki ^b,c   Ogawa, Kiyoko ^a,b   Niwa, Shin Ichiro ^a,b   Uenaka, Akiko ^d   Nakayama, Eiichi ^d   Tanaka, Keiji ^b,c  

^a SUMITOMO ELECTRIC INDUSTRIES LTD   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

^d OKAYAMA UNIVERSITY MEDICAL SCHOOL   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; EPITOPE; MULTIENZYME COMPLEX; PEPTIDE; PROTEASOME; PROTEIN; PSME1 PROTEIN, RAT; PSME2 PROTEIN, RAT; TUMOR ANTIGEN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CYTOTOXIC T LYMPHOCYTE; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IMMUNOLOGY; ISOLATION AND PURIFICATION; MAJOR HISTOCOMPATIBILITY COMPLEX; METABOLISM; MOLECULAR GENETICS; RAT;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, NEOPLASM; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYSTEINE ENDOPEPTIDASES; EPITOPES, T-LYMPHOCYTE; IMMUNODOMINANT EPITOPES; MAJOR HISTOCOMPATIBILITY COMPLEX; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; PEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEINS; RATS; T-LYMPHOCYTES, CYTOTOXIC;

EID: 0031306693     PISSN: 13569597     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2443.1997.1610359.x     Document Type: Article

References (10)

1. Ahn, J.Y., Tanahashi, N., Akiyama, K., et al. (1995) Primary structures of two homologous subunits of PA28, a γ-interferon-inducible protein activator of the 20S proteasome. FEBS Lett. 366, 37-42.
2. Androlewicz, M.J. & Cresswell, P. (1996) How selective is the transporter associated with antigen processing? Immunity 5, 1-5.
3. Baumeister, W. & Lupas, A. (1997) The proteasome. Curr. Opin. Struct. Biol. 7, 273-278.
4. Boes, B., Hengel, H., Ruppert, T., Multhaup, G., Koszinowski, U.H. & Kloetzel, P.-M. (1994) Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J. Exp. Med. 179, 901-909.
5. Chimini, G., Pala, P., Sire, J., Jordan, B.R. & Maryanski, J.L. (1989) Recognition of oligonucleotide-encoded T cell epitopes introduced into a gene unrelated to the original antigen. J. Exp. Med. 169, 297-302.
6. Coux, O., Tanaka, K. & Goldberg, A.L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
7. Del Val, M., Schlicht, H.-J., Ruppert, T., Reddehase, M.J. & Koszinowski, U.H. (1991) Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends on its neighboring residues in the protein. Cell 66, 1145-1153.
8. Dick, L.R., Aldrich, C., Jameson, S.C., et al. (1994) Proteolytic processing of ovalbumin and β-galactosidase by the proteasome to yield antigenic peptides. J. Immunol. 152, 3884-3894.
9. Dick, T.P., Ruppert, T., Groettrup, M., et al. (1996) Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands. Cell 86, 253-262.
10. Dubiel, W., Pratt, G., Ferrell, K. & Rechsteiner, M. (1992) Purification of an 11 S regulator of the multicatalytic protease. J. Biol. Chem. 267, 22369-22377.