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Volumn 111, Issue 3, 2004, Pages 252-261

Hydrolysis of the tumor-associated antigen epitope gp100280-288 by membrane-associated and soluble enzymes expressed by immature and mature dendritic cells

Author keywords

Dendritic cells; Human; Maturation; Peptides; Tumor immunity; Vaccination

Indexed keywords

EPITOPE; GLYCOPROTEIN GP 100; HLA A2 ANTIGEN; TUMOR ANTIGEN;

EID: 2942534491     PISSN: 15216616     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clim.2004.02.006     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0033039278 scopus 로고    scopus 로고
    • Responses of CD8(+) T cells to intracellular bacteria
    • Harty J.T., Bevan M.J. Responses of CD8(+) T cells to intracellular bacteria. Curr. Opin. Immunol. 11:1999;89-93
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 89-93
    • Harty, J.T.1    Bevan, M.J.2
  • 2
    • 0032519410 scopus 로고    scopus 로고
    • Antigen presentation by dendritic cells focuses T cell response against immunodominant peptides: Studies in the hen egg white lysozyme (HEL) model
    • Gapin L., Bravo de Alba Y., Casrouge A., Cabaniols J.P., Kourilsky P., Kanellopuolos J. Antigen presentation by dendritic cells focuses T cell response against immunodominant peptides: studies in the hen egg white lysozyme (HEL) model. J. Immunol. 160:1998;1555-1564
    • (1998) J. Immunol. , vol.160 , pp. 1555-1564
    • Gapin, L.1    Bravo De Alba, Y.2    Casrouge, A.3    Cabaniols, J.P.4    Kourilsky, P.5    Kanellopuolos, J.6
  • 3
    • 0033559238 scopus 로고    scopus 로고
    • Modulation of proteosomal activity required for the generation of a cytotoxic T lymphocyte-defined peptide derived from the tumor antigen MAGE-3
    • Valmori D., Gileadi U., Servis C., Dunbar P.R., Cerottini J.C., Romero P., Cerundolo V., Levy F. Modulation of proteosomal activity required for the generation of a cytotoxic T lymphocyte-defined peptide derived from the tumor antigen MAGE-3. J. Exp. Med. 189:1999;895-906
    • (1999) J. Exp. Med. , vol.189 , pp. 895-906
    • Valmori, D.1    Gileadi, U.2    Servis, C.3    Dunbar, P.R.4    Cerottini, J.C.5    Romero, P.6    Cerundolo, V.7    Levy, F.8
  • 6
    • 0028298224 scopus 로고
    • Cancer antigens: Immune recognition of self and altered self
    • Houghton A.N. Cancer antigens: immune recognition of self and altered self. J. Exp. Med. 180:1994;1-4
    • (1994) J. Exp. Med. , vol.180 , pp. 1-4
    • Houghton, A.N.1
  • 7
    • 0036202012 scopus 로고    scopus 로고
    • Rapid induction of cytotoxic T-lymphocytes against melanoma associated antigens by a recombinant vaccinia virus vector expressing immunodominant epitopes and costimulatory molecules in vivo
    • Oertli D., Marti W.R., Zajac P., Noppen C., Kocher T., Padovan E., Adamina M., Schumacher R., Harder F., Heberer M., Spagnoli G.C. Rapid induction of cytotoxic T-lymphocytes against melanoma associated antigens by a recombinant vaccinia virus vector expressing immunodominant epitopes and costimulatory molecules in vivo. Hum. Gene Ther. 13:2002;569-575
    • (2002) Hum. Gene Ther. , vol.13 , pp. 569-575
    • Oertli, D.1    Marti, W.R.2    Zajac, P.3    Noppen, C.4    Kocher, T.5    Padovan, E.6    Adamina, M.7    Schumacher, R.8    Harder, F.9    Heberer, M.10    Spagnoli, G.C.11
  • 9
    • 0030977720 scopus 로고    scopus 로고
    • DNA vaccines - A modern gimmick or a boon to vaccinology?
    • Manickan E., Karem K.L., Rouse B.T. DNA vaccines - A modern gimmick or a boon to vaccinology? Crit. Rev. Immunol. 17:1997;139-154
    • (1997) Crit. Rev. Immunol. , vol.17 , pp. 139-154
    • Manickan, E.1    Karem, K.L.2    Rouse, B.T.3
  • 10
    • 0025609606 scopus 로고
    • The role of beta2-microglobulin in peptide binding by class I molecules
    • Vitiello A., Potter T.A., Sherman L.A. The role of beta2-microglobulin in peptide binding by class I molecules. Science. 250:1990;1423-1426
    • (1990) Science , vol.250 , pp. 1423-1426
    • Vitiello, A.1    Potter, T.A.2    Sherman, L.A.3
  • 11
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/monocyte colony-stimulating factor plus interleukin 4 and down regulated by tumor necrosis factor alpha
    • Sallusto F., Lanzavecchia A. Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/monocyte colony-stimulating factor plus interleukin 4 and down regulated by tumor necrosis factor alpha. J. Exp. Med. 179:1994;1109-1118
    • (1994) J. Exp. Med. , vol.179 , pp. 1109-1118
    • Sallusto, F.1    Lanzavecchia, A.2
  • 12
    • 0026664088 scopus 로고
    • The immunological properties of epidermal Langerhans cells as part of the dendritic cell system
    • Romani N., Schuler G. The immunological properties of epidermal Langerhans cells as part of the dendritic cell system. Springer Semin. Immunopathol. 13:1992;265-279
    • (1992) Springer Semin. Immunopathol. , vol.13 , pp. 265-279
    • Romani, N.1    Schuler, G.2
  • 13
    • 0036525950 scopus 로고    scopus 로고
    • IFN-α2a induces IP-10/CXCL10 production in monocyte-derived dendritic cells and enhances their capacity to attract and stimulate CD8+ effector cells
    • Padovan E., Spagnoli G.C., Ferrantini M., Heberer M. IFN-α2a induces IP-10/CXCL10 production in monocyte-derived dendritic cells and enhances their capacity to attract and stimulate CD8+ effector cells. J. Leukocyte Biol. 71:2002;669-676
    • (2002) J. Leukocyte Biol. , vol.71 , pp. 669-676
    • Padovan, E.1    Spagnoli, G.C.2    Ferrantini, M.3    Heberer, M.4
  • 16
    • 0031032376 scopus 로고    scopus 로고
    • Localization of aminopeptidase activity in freshly excised human skin: Direct visualization by confocal laser scanning microscopy
    • Boderke P., Merkle H.P., Cullander C., Ponec M., Bodde H. Localization of aminopeptidase activity in freshly excised human skin: direct visualization by confocal laser scanning microscopy. J. Invest. Dermatol. 108:1997;83-86
    • (1997) J. Invest. Dermatol. , vol.108 , pp. 83-86
    • Boderke, P.1    Merkle, H.P.2    Cullander, C.3    Ponec, M.4    Bodde, H.5
  • 17
    • 0023735020 scopus 로고
    • Enzymatic barriers to peptide and protein absorption
    • Lee V.H.L. Enzymatic barriers to peptide and protein absorption. CRC Crit. Rev. Ther. Drug Carrier Syst. 5:1988;69-97
    • (1988) CRC Crit. Rev. Ther. Drug Carrier Syst. , vol.5 , pp. 69-97
    • Lee, V.H.L.1
  • 18
    • 0023875638 scopus 로고
    • Substance P and vasoactive intestinal peptides degradation by mast cell tryptase and chymase
    • Caughey G.H., Leidig F., Viro N.F., Nadel J.A. Substance P and vasoactive intestinal peptides degradation by mast cell tryptase and chymase. J. Pharmacol. Exp. Ther. 244:1988;133-137
    • (1988) J. Pharmacol. Exp. Ther. , vol.244 , pp. 133-137
    • Caughey, G.H.1    Leidig, F.2    Viro, N.F.3    Nadel, J.A.4
  • 19
    • 0027170175 scopus 로고
    • Effect of stimulation on soluble proteolytic enzymes released by peripheral blood mononucleate cells
    • Bongiorno L., Marini M., Urbani A., Ausiello A.C.M., Roda L.G. Effect of stimulation on soluble proteolytic enzymes released by peripheral blood mononucleate cells. Int. J. Immunopharmacol. 15:1993;621-629
    • (1993) Int. J. Immunopharmacol. , vol.15 , pp. 621-629
    • Bongiorno, L.1    Marini, M.2    Urbani, A.3    Ausiello, A.C.M.4    Roda, L.G.5
  • 20
    • 0032532350 scopus 로고    scopus 로고
    • Rapid extracellular degradation of synthetic class I peptides by human dendritic cells
    • Amoscato A.A., Prenovitz D.A., Lotze M.T. Rapid extracellular degradation of synthetic class I peptides by human dendritic cells. J. Immunol. 161:1998;4023-4032
    • (1998) J. Immunol. , vol.161 , pp. 4023-4032
    • Amoscato, A.A.1    Prenovitz, D.A.2    Lotze, M.T.3
  • 24
    • 0035889903 scopus 로고    scopus 로고
    • A new generation of Melan-A/MART-1 peptides that fulfill both increased immunogenicity and high resistance to biodegradation: Implication for molecular anti-melanoma immunotherapy
    • Blanchet J.S., Valmori D., Dufau I., Ayyoub M., Nguyen C., Guillaume P., Monsarrat B., Cerottini J.C., Romero P., Gairin J.E. A new generation of Melan-A/MART-1 peptides that fulfill both increased immunogenicity and high resistance to biodegradation: implication for molecular anti-melanoma immunotherapy. J. Immunol. 15:2001;5852-5861
    • (2001) J. Immunol. , vol.15 , pp. 5852-5861
    • Blanchet, J.S.1    Valmori, D.2    Dufau, I.3    Ayyoub, M.4    Nguyen, C.5    Guillaume, P.6    Monsarrat, B.7    Cerottini, J.C.8    Romero, P.9    Gairin, J.E.10
  • 26
    • 0026326474 scopus 로고
    • Rapid degradation of neurotensin by stimulated rat mast cells
    • Cochrane D.E., Carraway R.E., Boucher W., Feldberg R.S. Rapid degradation of neurotensin by stimulated rat mast cells. Peptides. 12:1991;1187-1194
    • (1991) Peptides , vol.12 , pp. 1187-1194
    • Cochrane, D.E.1    Carraway, R.E.2    Boucher, W.3    Feldberg, R.S.4
  • 27
    • 0025840351 scopus 로고
    • Rapid increases in the membrane of neutral endopeptidase (Cd10), aminopeptidase N (CD13), tyrosine phosphatese (CD45) and Fc gamma-RIII (CD16) upon stimulation of human peripheral leucocytes with human C5a
    • Werfel T., Sonntag G., Weber M.H., Gotze O. Rapid increases in the membrane of neutral endopeptidase (Cd10), aminopeptidase N (CD13), tyrosine phosphatese (CD45) and Fc gamma-RIII (CD16) upon stimulation of human peripheral leucocytes with human C5a. J. Immunol. 147:1991;3909-3914
    • (1991) J. Immunol. , vol.147 , pp. 3909-3914
    • Werfel, T.1    Sonntag, G.2    Weber, M.H.3    Gotze, O.4
  • 28
    • 0036681655 scopus 로고    scopus 로고
    • Native and genetically-inactivated per tussis toxins induce human dendritic cell maturation and synergize with LPS in promoting T helper type 1 responses
    • Ausiello C.M., Fedele G., Urbani F., Lande R., Di Carlo B., Cassone A. Native and genetically-inactivated per tussis toxins induce human dendritic cell maturation and synergize with LPS in promoting T helper type 1 responses. J. Infect. Dis. 186:2002;351-360
    • (2002) J. Infect. Dis. , vol.186 , pp. 351-360
    • Ausiello, C.M.1    Fedele, G.2    Urbani, F.3    Lande, R.4    Di Carlo, B.5    Cassone, A.6
  • 31
  • 32
    • 0021968677 scopus 로고
    • Binding of immunogenic peptides to Ia histocompatibility molecules
    • Babbitt B.P., Allen P.M., Matsueda G., Haber E., Unuanue E.R. Binding of immunogenic peptides to Ia histocompatibility molecules. Nature. 317:1985;359-361
    • (1985) Nature , vol.317 , pp. 359-361
    • Babbitt, B.P.1    Allen, P.M.2    Matsueda, G.3    Haber, E.4    Unuanue, E.R.5
  • 33
    • 0025889027 scopus 로고
    • Differential stability of antigenic MHC class-I restricted synthetic peptides
    • Widmann C., Maryanski J.L., Romero P., Corradin G. Differential stability of antigenic MHC class-I restricted synthetic peptides. J. Immunol. 147:1991;3745-3751
    • (1991) J. Immunol. , vol.147 , pp. 3745-3751
    • Widmann, C.1    Maryanski, J.L.2    Romero, P.3    Corradin, G.4
  • 34
    • 0027070864 scopus 로고
    • Peptide stability in drug development: A comparison of peptide reactivity in different biological media
    • Powell M.F., Grey H., Gaeta F., Sette A., Colon S. Peptide stability in drug development: a comparison of peptide reactivity in different biological media. J. Pharmacol. Sci. 81:1992;731-735
    • (1992) J. Pharmacol. Sci. , vol.81 , pp. 731-735
    • Powell, M.F.1    Grey, H.2    Gaeta, F.3    Sette, A.4    Colon, S.5
  • 35
    • 0035838981 scopus 로고    scopus 로고
    • Regulation of T cell immunity by dendritic cells
    • Lanzavecchia A., Sallusto F. Regulation of T cell immunity by dendritic cells. Cell. 106:2001;263-266
    • (2001) Cell , vol.106 , pp. 263-266
    • Lanzavecchia, A.1    Sallusto, F.2
  • 36
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: A renewed sense of self
    • Matzinger P. The danger model: a renewed sense of self. Science. 296:2002;301-305
    • (2002) Science , vol.296 , pp. 301-305
    • Matzinger, P.1
  • 37
    • 0025292591 scopus 로고
    • Hydrolysis and binding of leucine enkephalin to lymphomic and erythroleukaemic cell lines
    • Roscetti G., Bongiorno L., Urbani A., Marini M., Roda L.G. Hydrolysis and binding of leucine enkephalin to lymphomic and erythroleukaemic cell lines. Int. J. Immunopharmacol. 12:1990;391-396
    • (1990) Int. J. Immunopharmacol. , vol.12 , pp. 391-396
    • Roscetti, G.1    Bongiorno, L.2    Urbani, A.3    Marini, M.4    Roda, L.G.5


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