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Volumn 1, Issue 5, 2000, Pages 413-418

Two new proteases in the MHC class I processing pathway

Author keywords

[No Author keywords available]

Indexed keywords

ALANYL ALANYL PHENYLALANINE CHLOROMETHYL KETONE; ALANYL-ALANYL-PHENYLALANINE CHLOROMETHYL KETONE; AMINOPEPTIDASE; BLEOMYCIN HYDROLASE; CYSTEINE PROTEINASE; ENKEPHALIN DEGRADING ENZYME; EPITOPE; HLA ANTIGEN CLASS 1; LIGAND; MULTIENZYME COMPLEX; NUCLEOCAPSID PROTEIN; PEPTIDE CHLOROMETHYL KETONE; PROTEASOME; PROTEINASE; VIRUS ANTIGEN;

EID: 5944236047     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/80852     Document Type: Article
Times cited : (220)

References (32)
  • 1
    • 0031032422 scopus 로고    scopus 로고
    • The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells
    • Cerundolo, V. et al. The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells. Eur. J. Immunol. 27, 336-341 (1997).
    • (1997) Eur. J. Immunol. , vol.27 , pp. 336-341
    • Cerundolo, V.1
  • 2
    • 0025155682 scopus 로고
    • Cellular peptide composition governed by major histocompatibility complex class I molecules
    • Falk, K., Rotzschke, O. & Rammensee, H. -G. Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature 348, 243-251 (1990).
    • (1990) Nature , vol.348 , pp. 243-251
    • Falk, K.1    Rotzschke, O.2    Rammensee, H.-G.3
  • 3
    • 0028096715 scopus 로고
    • Trimming of antigenic peptides in an early secretory compartment
    • Snyder, H. L., Yewdell, J. W. & Bennink, J. R. Trimming of antigenic peptides in an early secretory compartment. J. Exp. Med. 180, 2389-2394 (1994).
    • (1994) J. Exp. Med. , vol.180 , pp. 2389-2394
    • Snyder, H.L.1    Yewdell, J.W.2    Bennink, J.R.3
  • 4
    • 0028925556 scopus 로고
    • Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum
    • Elliott, T., Willis, A., Cerundolo, V. & Townsend, A. Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum. J. Exp. Med. 181, 1481-1491 (1995).
    • (1995) J. Exp. Med. , vol.181 , pp. 1481-1491
    • Elliott, T.1    Willis, A.2    Cerundolo, V.3    Townsend, A.4
  • 5
    • 0034073861 scopus 로고    scopus 로고
    • Proteolytic processing of peptides in the lumen of the endoplasmic reticulum for antigen presentation by major histocompatibility class I
    • Lobigs, M., Chelvanayagam, G. & Mullbacher, A. Proteolytic processing of peptides in the lumen of the endoplasmic reticulum for antigen presentation by major histocompatibility class I. Eur. J. Immunol. 30, 1496-1506 (2000).
    • (2000) Eur. J. Immunol. , vol.30 , pp. 1496-1506
    • Lobigs, M.1    Chelvanayagam, G.2    Mullbacher, A.3
  • 6
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga, J., Rock, K. L. & Goldberg, A. L. Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273, 18734-18742 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 7
    • 0033548055 scopus 로고    scopus 로고
    • A giant protease with potential to substitute for some functions of the proteasome
    • Geier, E. et al. A giant protease with potential to substitute for some functions of the proteasome. Science 283, 978-981 (1999).
    • (1999) Science , vol.283 , pp. 978-981
    • Geier, E.1
  • 8
    • 0031771008 scopus 로고
    • Generation of the vesicular stomatitis virus nucleoprotein cytotoxic T lymphocyte epitope requires proteasome-dependent and -independent proteolytic activities
    • Stoltze, L. et al. Generation of the vesicular stomatitis virus nucleoprotein cytotoxic T lymphocyte epitope requires proteasome-dependent and -independent proteolytic activities. Eur. J. Immunol. 28, 4029-4036 (1993).
    • (1993) Eur. J. Immunol. , vol.28 , pp. 4029-4036
    • Stoltze, L.1
  • 9
    • 0033179885 scopus 로고    scopus 로고
    • Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER
    • Paz, P., Brouwenstijn, N., Perry, R. & Shastri, N. Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER. Immunity 11, 241-251 (1999).
    • (1999) Immunity , vol.11 , pp. 241-251
    • Paz, P.1    Brouwenstijn, N.2    Perry, R.3    Shastri, N.4
  • 10
    • 0034647551 scopus 로고    scopus 로고
    • The human 26S and 20S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate
    • submitted
    • Emmerich, N. P. et al. The human 26S and 20S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate. J. Biol. Chem. (submitted, 2000).
    • (2000) J. Biol. Chem.
    • Emmerich, N.P.1
  • 11
    • 0029965803 scopus 로고    scopus 로고
    • The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum
    • Hughes, E. A., Ortmann, B., Surman, M. & Cresswell, P. The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum. J. Exp. Med. 183, 1569-1573 (1996).
    • (1996) J. Exp. Med. , vol.183 , pp. 1569-1573
    • Hughes, E.A.1    Ortmann, B.2    Surman, M.3    Cresswell, P.4
  • 12
    • 13344281002 scopus 로고    scopus 로고
    • Characterization and inhibition of a cholecystokinin-inactivating serine peptidase
    • Rose, C. et al. Characterization and inhibition of a cholecystokinin-inactivating serine peptidase. Nature 380, 403-409 (1996).
    • (1996) Nature , vol.380 , pp. 403-409
    • Rose, C.1
  • 13
    • 0033152757 scopus 로고    scopus 로고
    • Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease
    • O'Farrell, P.A. et al. Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease. Structure Fold. Des. 7, 619-627 (1999).
    • (1999) Structure Fold. Des. , vol.7 , pp. 619-627
    • O'Farrell, P.A.1
  • 14
    • 0028843821 scopus 로고
    • Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization
    • Constam, D. B. et al. Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization. J. Biol. Chem. 270, 26931-26939 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 26931-26939
    • Constam, D.B.1
  • 15
    • 0027499191 scopus 로고
    • BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase
    • Enenkel, C. & Wolf, D. H. BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase. J. Biol. Chem. 268, 7036-7043 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 7036-7043
    • Enenkel, C.1    Wolf, D.H.2
  • 16
    • 0030886208 scopus 로고    scopus 로고
    • Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide
    • Craiu, A., Akopian, T., Goldberg, A. & Rock, K. L. Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide. Proc. Natl Acad. Sci. USA 94, 10850-10855 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10850-10855
    • Craiu, A.1    Akopian, T.2    Goldberg, A.3    Rock, K.L.4
  • 17
    • 0019498536 scopus 로고
    • Solubilization and characterization of two rat brain membrane-bound aminopeptidases active on Met-enkephalin
    • Hersh, L. B. Solubilization and characterization of two rat brain membrane-bound aminopeptidases active on Met-enkephalin. Biochemistry 20, 2345-2350 (1981).
    • (1981) Biochemistry , vol.20 , pp. 2345-2350
    • Hersh, L.B.1
  • 18
    • 0025823384 scopus 로고
    • An enkephalin degrading aminopeptidase of human brain preserved during the vertebrate phylogeny
    • de Souza, A. N., Bruno, J. A. & Carvalho, K. M. An enkephalin degrading aminopeptidase of human brain preserved during the vertebrate phylogeny. Comp. Biochem. Physiol. C 99, 363-367 (1991).
    • (1991) Comp. Biochem. Physiol. C , vol.99 , pp. 363-367
    • De Souza, A.N.1    Bruno, J.A.2    Carvalho, K.M.3
  • 19
    • 0023743331 scopus 로고
    • Studies on the tissue distribution of the puromycin-sensitive enkephalin-degrading aminopeptidases
    • McLellan, S., Dyer, S. H., Rodriguez, G. & Hersh, L. B. Studies on the tissue distribution of the puromycin-sensitive enkephalin-degrading aminopeptidases. J. Neurochem. 51, 1552-1559 (1988).
    • (1988) J. Neurochem. , vol.51 , pp. 1552-1559
    • McLellan, S.1    Dyer, S.H.2    Rodriguez, G.3    Hersh, L.B.4
  • 20
    • 0033542141 scopus 로고    scopus 로고
    • Cloning and analysis of the gene for the human puromycin-sensitive aminopeptidase
    • Thompson, M. W., Tobler, A., Fontana, A. & Hersh, L. B. Cloning and analysis of the gene for the human puromycin-sensitive aminopeptidase. Biochem. Biophys. Res. Commun. 258, 234-240 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 234-240
    • Thompson, M.W.1    Tobler, A.2    Fontana, A.3    Hersh, L.B.4
  • 21
    • 0242707686 scopus 로고    scopus 로고
    • Sequential cleavage by metallopeptidases and proteasomes is involved in processing HIV-1 ENV epitope for endogenous MHC class I antigen presentation
    • Lopez, D., Gil-Torregrosa, B. C., Bergmann, C. & Del Val, M. Sequential cleavage by metallopeptidases and proteasomes is involved in processing HIV-1 ENV epitope for endogenous MHC class I antigen presentation. J. Immunol. 164, 5070-5077 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 5070-5077
    • Lopez, D.1    Gil-Torregrosa, B.C.2    Bergmann, C.3    Del Val, M.4
  • 22
    • 0031453371 scopus 로고    scopus 로고
    • Gene characterization, promoter analysis, and chromosomal localization of human bleomycin hydrolase
    • Ferrando, A. A. et al. Gene characterization, promoter analysis, and chromosomal localization of human bleomycin hydrolase. J. Biol. Chem. 272, 33298-33304 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 33298-33304
    • Ferrando, A.A.1
  • 23
    • 0030008565 scopus 로고    scopus 로고
    • Human bleomycin hydrolase: Molecular cloning, sequencing, functional expression, and enzymatic characterization
    • Bromme, D., Rossi, A. B., Smeekens, S. P., Anderson, D. C. & Payan, D. G. Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization. Biochemistry 35, 6706-6714 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6706-6714
    • Bromme, D.1    Rossi, A.B.2    Smeekens, S.P.3    Anderson, D.C.4    Payan, D.G.5
  • 25
    • 0032562136 scopus 로고    scopus 로고
    • Essential binding and functional domains of human bleomycin hydrolase
    • Koldamova, R. P., Lefterov, I. M., Gadjeva, V. G. & Lazo, J. S. Essential binding and functional domains of human bleomycin hydrolase. Biochemistry 37, 2282-2290 (1998).
    • (1998) Biochemistry , vol.37 , pp. 2282-2290
    • Koldamova, R.P.1    Lefterov, I.M.2    Gadjeva, V.G.3    Lazo, J.S.4
  • 26
    • 0032524940 scopus 로고    scopus 로고
    • Dissociation of proteasomal degradation of biosynthesized viral proteins from generation of MHC class I-associated antigenic peptides
    • Anton, L. C. et al. Dissociation of proteasomal degradation of biosynthesized viral proteins from generation of MHC class I-associated antigenic peptides. J. Immunol. 160, 4859-4868 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 4859-4868
    • Anton, L.C.1
  • 27
    • 7144223429 scopus 로고    scopus 로고
    • Proteasomes can either generate or destroy MHC class I epitopes: Evidence for nonproteasomal epitope generation in the cytosol
    • Luckey, C. J. et al. Proteasomes can either generate or destroy MHC class I epitopes: evidence for nonproteasomal epitope generation in the cytosol. J. Immunol. 161, 112-121 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 112-121
    • Luckey, C.J.1
  • 28
    • 0031573620 scopus 로고    scopus 로고
    • Selective involvement of proteasomes and cysteine proteases in MHC class I antigen presentation
    • Lopez, D. & Del Val, M. Selective involvement of proteasomes and cysteine proteases in MHC class I antigen presentation. J. Immunol. 159, 5769-5772 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 5769-5772
    • Lopez, D.1    Del Val, M.2
  • 29
    • 0032409008 scopus 로고    scopus 로고
    • An evolutionarily conserved cysteine protease, human bleomycin hydrolase, binds to the human homologue of ubiquitin-conjugating enzyme 9
    • Koldamova, R. P., Lefterov, I. M., DiSabella, M. T. & Lazo, J. S. An evolutionarily conserved cysteine protease, human bleomycin hydrolase, binds to the human homologue of ubiquitin-conjugating enzyme 9. Mol. Pharmacol. 54, 954-961 (1998).
    • (1998) Mol. Pharmacol. , vol.54 , pp. 954-961
    • Koldamova, R.P.1    Lefterov, I.M.2    DiSabella, M.T.3    Lazo, J.S.4
  • 30
    • 0028519275 scopus 로고
    • Altered peptidase and viral-specific T cell response in LMP2 mutant mice
    • Van Kaer, L. et al. Altered peptidase and viral-specific T cell response in LMP2 mutant mice. Immunity 1, 533-541 (1994).
    • (1994) Immunity , vol.1 , pp. 533-541
    • Van Kaer, L.1
  • 31
    • 0027991677 scopus 로고
    • MHC class I expression in mice lacking the proteasome subunit LMP-7
    • Fehling, H. J. et al. MHC class I expression in mice lacking the proteasome subunit LMP-7. Science 265, 1234-1237 (1994).
    • (1994) Science , vol.265 , pp. 1234-1237
    • Fehling, H.J.1
  • 32
    • 0030602834 scopus 로고    scopus 로고
    • Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands
    • Dick, T. P. et al. Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands. Cell 86, 253-262 (1996).
    • (1996) Cell , vol.86 , pp. 253-262
    • Dick, T.P.1


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