메뉴 건너뛰기




Volumn 37, Issue 4, 2007, Pages 896-904

No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes

Author keywords

Antigen processing; Cytotoxic T cells; Proteasome

Indexed keywords

AMINO ACID; AMINOPEPTIDASE; EPITOPE; LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; OVALBUMIN; PEPTIDE; PROTEASOME; TRIPEPTIDYL PEPTIDASE II; UNCLASSIFIED DRUG; HLA ANTIGEN CLASS 1; NUCLEOPROTEIN; NUCLEOPROTEIN PEPTIDE 118 126, LYMPHOCYTIC CHORIOMENINGITIS VIRUS; NUCLEOPROTEIN PEPTIDE 118-126, LYMPHOCYTIC CHORIOMENINGITIS VIRUS; PEPTIDE FRAGMENT; SERINE PROTEINASE;

EID: 34249658582     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200636372     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev, A. F., Akopian, T. N. and Goldberg, A. L., Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biel. Chem. 1998. 273: 1982-1989.
    • (1998) J. Biel. Chem , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 2
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga, J., Rock, K. L. and Goldberg, A. L., Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 1998. 273: 18734-18742.
    • (1998) J. Biol. Chem , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 4
    • 0035965357 scopus 로고    scopus 로고
    • Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase
    • Saric, T., Beninga, J., Graef, C. L, Akopian, T. N., Rock, K. L. and Goldberg, A. L., Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase. J. Biol. Chem. 2001. 276: 36474-36481.
    • (2001) J. Biol. Chem , vol.276 , pp. 36474-36481
    • Saric, T.1    Beninga, J.2    Graef, C.L.3    Akopian, T.N.4    Rock, K.L.5    Goldberg, A.L.6
  • 5
    • 0037341473 scopus 로고    scopus 로고
    • The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation
    • York, I. A., Mo, A. X. Y., Lemerise, K., Zeng, W. Y., Shen, Y. L., Abraham, C. R., Saric, T. et al., The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation. Immunity 2003. 18: 429-440.
    • (2003) Immunity , vol.18 , pp. 429-440
    • York, I.A.1    Mo, A.X.Y.2    Lemerise, K.3    Zeng, W.Y.4    Shen, Y.L.5    Abraham, C.R.6    Saric, T.7
  • 8
    • 1842785206 scopus 로고    scopus 로고
    • A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
    • Reits, E., Neijssen, J., Herberts, C., Benckhuijsen, W., Janssen, L., Drijffhout, J. W. and Neefjes, J., A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation. Immunity 2004. 20: 495-506.
    • (2004) Immunity , vol.20 , pp. 495-506
    • Reits, E.1    Neijssen, J.2    Herberts, C.3    Benckhuijsen, W.4    Janssen, L.5    Drijffhout, J.W.6    Neefjes, J.7
  • 9
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York, I. A., Chang, S. C., Saric, T., Keys, J. A., Favreau, J. M., Goldberg, A. L. and Rock, K. L., The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat. Immunol. 2002. 3: 1177-1184.
    • (2002) Nat. Immunol , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5    Goldberg, A.L.6    Rock, K.L.7
  • 10
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides
    • Saric, T., Chang, S. C., Hattori, A., York, I. A., Markant, S., Rock, K. L., Tsujimoto, M. et al., An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat. Immunol. 2002. 3: 1169-1176.
    • (2002) Nat. Immunol , vol.3 , pp. 1169-1176
    • Saric, T.1    Chang, S.C.2    Hattori, A.3    York, I.A.4    Markant, S.5    Rock, K.L.6    Tsujimoto, M.7
  • 11
    • 22144442460 scopus 로고    scopus 로고
    • Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum
    • Saveanu, L., Carroll, O., Lindo, V., Del Val, M., Lopez, D., Lepefletier, Y., Greer, F. et al., Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum. Nat. Immunol. 2005. 6: 689-697.
    • (2005) Nat. Immunol , vol.6 , pp. 689-697
    • Saveanu, L.1    Carroll, O.2    Lindo, V.3    Del Val, M.4    Lopez, D.5    Lepefletier, Y.6    Greer, F.7
  • 12
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes - Implications for understanding the degradative mechanism and antigen presentation
    • Kisselev, A. F., Akopian, T. N., Woo, K. M. and Goldberg, A. L., The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes - Implications for understanding the degradative mechanism and antigen presentation. J. Biol. Chem. 1999. 274: 3363-3371.
    • (1999) J. Biol. Chem , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 14
    • 0037108488 scopus 로고    scopus 로고
    • The final N-terminal trimming of a subaminoterminal proline-containing HLA class I-restricted antigenic peptide in the cytosol is mediated by two peptidases
    • Levy, F., Burri, L., Morel, S., Peitrequin, A. L., Levy, N., Bachi, A., Hellman, U. et al., The final N-terminal trimming of a subaminoterminal proline-containing HLA class I-restricted antigenic peptide in the cytosol is mediated by two peptidases. J. Immunol. 2002. 169: 4161-4171.
    • (2002) J. Immunol , vol.169 , pp. 4161-4171
    • Levy, F.1    Burri, L.2    Morel, S.3    Peitrequin, A.L.4    Levy, N.5    Bachi, A.6    Hellman, U.7
  • 15
    • 0035500453 scopus 로고    scopus 로고
    • Cutting Edge: Neosynthesis is required for the presentation of a T cell epitope from a long lived viral protein
    • Khan, S., de Giuli, R., Schmidtke, G., Bruns, M., Buchmeier, M., van den Brock, M. and Groettrup, M., Cutting Edge: Neosynthesis is required for the presentation of a T cell epitope from a long lived viral protein. J. Immunol. 2001. 167: 4801-4804.
    • (2001) J. Immunol , vol.167 , pp. 4801-4804
    • Khan, S.1    de Giuli, R.2    Schmidtke, G.3    Bruns, M.4    Buchmeier, M.5    van den Brock, M.6    Groettrup, M.7
  • 17
    • 0034659804 scopus 로고    scopus 로고
    • Schwarz, K., de Giuli, R., Schmidtke, G., Kostka, S., van den Broek, M., Kim, K., Crews, C. M. et al., The selective proteasome inhibitors lactacystin and expoxomicin can be used to either up- or downregulate antigen presentation at non-toxic doses. J. Immunol. 2000. 164: 6147-6157.
    • Schwarz, K., de Giuli, R., Schmidtke, G., Kostka, S., van den Broek, M., Kim, K., Crews, C. M. et al., The selective proteasome inhibitors lactacystin and expoxomicin can be used to either up- or downregulate antigen presentation at non-toxic doses. J. Immunol. 2000. 164: 6147-6157.
  • 18
    • 0031790032 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin prevents the generation of an endoplasmic reticulum leader-derived T cell epitope
    • Gallimore, A., Schwarz, K., van den Broek, M., Hengartner, H. and Groettrup, M., The proteasome inhibitor lactacystin prevents the generation of an endoplasmic reticulum leader-derived T cell epitope. Mol. Immunol. 1998. 35: 581-591.
    • (1998) Mol. Immunol , vol.35 , pp. 581-591
    • Gallimore, A.1    Schwarz, K.2    van den Broek, M.3    Hengartner, H.4    Groettrup, M.5
  • 20
    • 13944269123 scopus 로고    scopus 로고
    • Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II
    • Stavropoulou, V., Xie, J., Henriksson, M., Tomkinson, B., Imreh, S. and Masucci, M. G., Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II. Cancer Res. 2005. 65: 1361-1368.
    • (2005) Cancer Res , vol.65 , pp. 1361-1368
    • Stavropoulou, V.1    Xie, J.2    Henriksson, M.3    Tomkinson, B.4    Imreh, S.5    Masucci, M.G.6
  • 21
    • 33749512798 scopus 로고    scopus 로고
    • Processing of a class I-restricted epitope from tyrosinase requires peptide N-glycanase and the cooperative action of endoplasmic reticulunt aminopeptidase 1 and cytosolic proteases
    • Altrich-VanLith, M. L., Ostankovitch, M., Polefrone, J. M., Mosse, C. A., Shabanowitz, J., Hunt, D. F. and Engelhard, V. H., Processing of a class I-restricted epitope from tyrosinase requires peptide N-glycanase and the cooperative action of endoplasmic reticulunt aminopeptidase 1 and cytosolic proteases. J. Immunol. 2006. 177: 5440-5450.
    • (2006) J. Immunol , vol.177 , pp. 5440-5450
    • Altrich-VanLith, M.L.1    Ostankovitch, M.2    Polefrone, J.M.3    Mosse, C.A.4    Shabanowitz, J.5    Hunt, D.F.6    Engelhard, V.H.7
  • 22
    • 33746215297 scopus 로고    scopus 로고
    • Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation
    • York, I. A., Bhutani, N., Zendzian, S., Goldberg, A. L. and Rock, K. L., Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation. J. Immunol. 2006. 177: 1434-1443.
    • (2006) J. Immunol , vol.177 , pp. 1434-1443
    • York, I.A.1    Bhutani, N.2    Zendzian, S.3    Goldberg, A.L.4    Rock, K.L.5
  • 23
    • 0032499199 scopus 로고    scopus 로고
    • A proteolytic system that compensates for loss of proteasome function
    • Glas, R., Bogyo, M., McMaster, J. S., Gaczynska, M. and Ploegh, H. L., A proteolytic system that compensates for loss of proteasome function. Nature 1998. 392: 618-622.
    • (1998) Nature , vol.392 , pp. 618-622
    • Glas, R.1    Bogyo, M.2    McMaster, J.S.3    Gaczynska, M.4    Ploegh, H.L.5
  • 25
    • 3242771511 scopus 로고    scopus 로고
    • Generation of major histocompatibility, complex class I antigens: Functional interplay between proteasomes and TPPII
    • Kloetzel, P. M., Generation of major histocompatibility, complex class I antigens: Functional interplay between proteasomes and TPPII. Nat. Immunol. 2004. 5: 661-669.
    • (2004) Nat. Immunol , vol.5 , pp. 661-669
    • Kloetzel, P.M.1
  • 26
    • 0023601760 scopus 로고
    • Cytolytic T lymphocyte recognition of the murine cytomegalovirus non-structural immediate-early protein pp89 expressed by recombinant vaccinia virus
    • Volkmer, H., Bertholet, C., Jonjic, S., Witter, R. and Koszinowski, U., Cytolytic T lymphocyte recognition of the murine cytomegalovirus non-structural immediate-early protein pp89 expressed by recombinant vaccinia virus. J. Exp. Med. 1987. 166: 668-677.
    • (1987) J. Exp. Med , vol.166 , pp. 668-677
    • Volkmer, H.1    Bertholet, C.2    Jonjic, S.3    Witter, R.4    Koszinowski, U.5
  • 27
    • 0030812840 scopus 로고    scopus 로고
    • DNA immunization: Ubiquitination of a viral protein enhances cytotoxic T-lymphocyte induction and antiviral protection but abrogates antibody induction
    • Rodriguez, F., Zhang, J. and Whitton, J. L., DNA immunization: Ubiquitination of a viral protein enhances cytotoxic T-lymphocyte induction and antiviral protection but abrogates antibody induction. J. Virol. 1997. 71: 8497-8503.
    • (1997) J. Virol , vol.71 , pp. 8497-8503
    • Rodriguez, F.1    Zhang, J.2    Whitton, J.L.3
  • 28
    • 0021035910 scopus 로고
    • Lymphocytic choriomeningitis virus. VI. Isolation of a glycoprotein mediating neutralization
    • Bruns, M., Cihak, J., Willer, G. and Lehmann-Grube, F., Lymphocytic choriomeningitis virus. VI. Isolation of a glycoprotein mediating neutralization. Virology 1983. 130: 247-251.
    • (1983) Virology , vol.130 , pp. 247-251
    • Bruns, M.1    Cihak, J.2    Willer, G.3    Lehmann-Grube, F.4
  • 29
    • 4644249095 scopus 로고    scopus 로고
    • Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus
    • Basler, M., Youhnovski, N., Van Den Brock, M., Przybylski, M. and Groettrup, M., Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus. J. Immunol. 2004. 173: 3925-3934.
    • (2004) J. Immunol , vol.173 , pp. 3925-3934
    • Basler, M.1    Youhnovski, N.2    Van Den Brock, M.3    Przybylski, M.4    Groettrup, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.