메뉴 건너뛰기




Volumn 191, Issue 7, 2000, Pages 1177-1185

Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages

Author keywords

Antigen presentation; Antigen presenting cell; Cysteine protease; Protease inhibitor; Proteolysis

Indexed keywords

CATHEPSIN; CATHEPSIN F; CATHEPSIN S; CATHEPSIN Z; CELL MEMBRANE PROTEIN; CLASS II ASSOCIATED INVARIANT CHAIN PEPTIDE; CYSTEINE PROTEINASE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 0034599498     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.191.7.1177     Document Type: Article
Times cited : (209)

References (42)
  • 1
    • 0028313992 scopus 로고
    • Assembly, transport, and function of MHC class II molecules
    • Cresswell, P. 1994. Assembly, transport, and function of MHC class II molecules. Annu. Rev. Immunol. 12:259-293.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 259-293
    • Cresswell, P.1
  • 2
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain, R.N. 1994. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell. 76:287-299.
    • (1994) Cell. , vol.76 , pp. 287-299
    • Germain, R.N.1
  • 3
    • 0029615496 scopus 로고
    • How MHC class II molecules acquire peptide cargo: Biosynthesis and trafficking through the endocytic pathway
    • Wolf, P.R., and H.L. Ploegh. 1995. How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. Annu. Rev. Cell. Dev. Biol. 11:267-306.
    • (1995) Annu. Rev. Cell. Dev. Biol. , vol.11 , pp. 267-306
    • Wolf, P.R.1    Ploegh, H.L.2
  • 4
    • 0030937833 scopus 로고    scopus 로고
    • Capture and processing of exogenous antigens for presentation on MHC molecules
    • Watts, C. 1997. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 15:821-850.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 821-850
    • Watts, C.1
  • 6
    • 0029084023 scopus 로고
    • DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide
    • Sherman, M.A., D.A. Weber, and P.E. Jenson. 1995. DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide. Immunity. 3:197-205.
    • (1995) Immunity , vol.3 , pp. 197-205
    • Sherman, M.A.1    Weber, D.A.2    Jenson, P.E.3
  • 9
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • Ghosh, P., M. Amaya, E. Mellins, and D.C. Wiley. 1995. The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature. 378:457-462.
    • (1995) Nature , vol.378 , pp. 457-462
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 10
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R.J., P.R. Wolf, D. Bromme, L.R. Natkin, J.A. Villadangos, H.L. Ploegh, and H.A. Chapman. 1996. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity. 4:357-366.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 15
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • Pierre, P., and I. Mellman. 1998. Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell. 93:1135-1145.
    • (1998) Cell. , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 16
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer, J.T., D. Rasnick, J.L. Klaus, and D. Bromme. 1995. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem. 38:3193-3196.
    • (1995) J. Med. Chem. , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Bromme, D.4
  • 17
    • 0029744988 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors
    • Meara, J.P., and D.H. Rich. 1996. Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors. J. Med. Chem. 39:3357-3366.
    • (1996) J. Med. Chem. , vol.39 , pp. 3357-3366
    • Meara, J.P.1    Rich, D.H.2
  • 18
    • 0029996205 scopus 로고    scopus 로고
    • High level expression and crystallization of recombinant human cathepsin S
    • Bromme, D., and M.E. McGrath. 1996. High level expression and crystallization of recombinant human cathepsin S. Protein. Sci. 5:789-791.
    • (1996) Protein. Sci. , vol.5 , pp. 789-791
    • Bromme, D.1    McGrath, M.E.2
  • 19
    • 0033610817 scopus 로고    scopus 로고
    • Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization
    • Wang, B., G.-P. Shi, P.M. Yao, Z. Li, H.A. Chapman, and D. Bromme. 1998. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J. Biol. Chem. 273:32000-32008.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32000-32008
    • Wang, B.1    Shi, G.-P.2    Yao, P.M.3    Li, Z.4    Chapman, H.A.5    Bromme, D.6
  • 20
    • 0025309427 scopus 로고
    • The distinct leukocyte integrins of mouse spleen dendritic cells as identified with new hamster monoclonal antibodies
    • Metlay, J.P., M.D. Witmer-Pack, R. Agger, M.T. Crowley, D. Lawless, and R.M. Steinman. 1990. The distinct leukocyte integrins of mouse spleen dendritic cells as identified with new hamster monoclonal antibodies. J. Exp. Med. 171: 1753-1771.
    • (1990) J. Exp. Med. , vol.171 , pp. 1753-1771
    • Metlay, J.P.1    Witmer-Pack, M.D.2    Agger, R.3    Crowley, M.T.4    Lawless, D.5    Steinman, R.M.6
  • 21
    • 0017704547 scopus 로고
    • Influence of acute exposure to cigarette smoke on the alveolar macrophage system
    • Guarneri, J.J. 1977. Influence of acute exposure to cigarette smoke on the alveolar macrophage system. J. Lab. Clin. Med. 89:1215-1224.
    • (1977) J. Lab. Clin. Med. , vol.89 , pp. 1215-1224
    • Guarneri, J.J.1
  • 22
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • Shi, G.-P., J.S. Munger, J.P. Meara, D.H. Rich, and H.A. Chapman. 1992. Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J. Biol. Chem. 267:7258-7262.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7258-7262
    • Shi, G.-P.1    Munger, J.S.2    Meara, J.P.3    Rich, D.H.4    Chapman, H.A.5
  • 25
    • 0030790341 scopus 로고    scopus 로고
    • Degradation of mouse invariant chain: Roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism
    • Villadangos, J.A., R.J. Riese, C. Peters, H.A. Chapman, and H.L. Ploegh. 1997. Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism. J. Exp. Med. 186:549-560.
    • (1997) J. Exp. Med. , vol.186 , pp. 549-560
    • Villadangos, J.A.1    Riese, R.J.2    Peters, C.3    Chapman, H.A.4    Ploegh, H.L.5
  • 27
    • 0028835637 scopus 로고
    • Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2
    • Shi, G.-P., H.A. Chapman, S.M. Bhairi, C. DeLeeuw, V.Y. Reddy, and S.J. Weiss. 1995. Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2. FEBS Lett. 357:129-134.
    • (1995) FEBS Lett. , vol.357 , pp. 129-134
    • Shi, G.-P.1    Chapman, H.A.2    Bhairi, S.M.3    Deleeuw, C.4    Reddy, V.Y.5    Weiss, S.J.6
  • 28
    • 0040909177 scopus 로고    scopus 로고
    • The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide
    • Quraishi, O., D.K. Nagler, T. Fox, J. Sivaraman, M. Cygler, J.S. Mort, and A.C. Storer. 1999. The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide. Biochemistry. 38:5017-5023.
    • (1999) Biochemistry , vol.38 , pp. 5017-5023
    • Quraishi, O.1    Nagler, D.K.2    Fox, T.3    Sivaraman, J.4    Cygler, M.5    Mort, J.S.6    Storer, A.C.7
  • 29
    • 0040234054 scopus 로고    scopus 로고
    • Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions
    • Nagler, D.K., and R. Menard. 1998. Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions. FEBS Lett. 434:135-139.
    • (1998) FEBS Lett. , vol.434 , pp. 135-139
    • Nagler, D.K.1    Menard, R.2
  • 30
    • 0032479144 scopus 로고    scopus 로고
    • Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location
    • Santamaria, I., G. Velasco, A.M. Pendas, A. Fueyo, and C. Lopez-Otin. 1998. Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location. J. Biol. Chem. 273:16816-16823.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16816-16823
    • Santamaria, I.1    Velasco, G.2    Pendas, A.M.3    Fueyo, A.4    Lopez-Otin, C.5
  • 31
    • 0039642231 scopus 로고    scopus 로고
    • Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen
    • Nagler, D.K., T. Sulea, and R. Menard. 1999. Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. Biochem. Biophys. Res. Commun. 257:313-318.
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 313-318
    • Nagler, D.K.1    Sulea, T.2    Menard, R.3
  • 32
    • 0033553419 scopus 로고    scopus 로고
    • Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
    • Santamaria, I., G. Velasco, A.M. Pendas, A. Paz, and C. Lopez-Otin. 1999. Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J. Biol. Chem. 274:13800-13809.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13800-13809
    • Santamaria, I.1    Velasco, G.2    Pendas, A.M.3    Paz, A.4    Lopez-Otin, C.5
  • 33
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: A cysteine protease with unique carboxypeptidase activity
    • Nagler, D.K., R. Zhang, W. Tam, T. Sulea, E.O. Purisima, and R. Menard. 1999. Human cathepsin X: a cysteine protease with unique carboxypeptidase activity. Biochemistry. 38: 12648-12654.
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nagler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Menard, R.6
  • 35
    • 0032836869 scopus 로고    scopus 로고
    • Increased expression of the CD80 accessory molecule by alveolar macrophages in asthmatic subjects and its functional involvement in allergen presentation to autologous TH2 lymphocytes
    • Burastero, S.E., Z. Magnani, C. Confetti, L. Abbruzzese, S. Oddera, P. Balbo, G.A. Rossi, and E. Crimi. 1999. Increased expression of the CD80 accessory molecule by alveolar macrophages in asthmatic subjects and its functional involvement in allergen presentation to autologous TH2 lymphocytes. J. Allergy Clin. Immunol. 103:1136-1142.
    • (1999) J. Allergy Clin. Immunol. , vol.103 , pp. 1136-1142
    • Burastero, S.E.1    Magnani, Z.2    Confetti, C.3    Abbruzzese, L.4    Oddera, S.5    Balbo, P.6    Rossi, G.A.7    Crimi, E.8
  • 36
    • 0031877291 scopus 로고    scopus 로고
    • Antigen detection in vivo after immunization with different presentation forms of rabies virus antigen. II. Cellular, but not humoral, systemic immune responses against rabies virus immune-stimulating complexes are macrophage dependent
    • Claassen, I.J., A.D. Osterhaus, M. Poelen, N. Van Rooijen, and E. Claassen. 1998. Antigen detection in vivo after immunization with different presentation forms of rabies virus antigen. II. Cellular, but not humoral, systemic immune responses against rabies virus immune-stimulating complexes are macrophage dependent. Immunology. 94:455-460.
    • (1998) Immunology , vol.94 , pp. 455-460
    • Claassen, I.J.1    Osterhaus, A.D.2    Poelen, M.3    Van Rooijen, N.4    Claassen, E.5
  • 37
    • 0031573611 scopus 로고    scopus 로고
    • In vivo effects of T helper cell type 2 cytokines on macrophage antigen-presenting cell induction of T helper subsets
    • Cua, D.J., and S.A. Stohlman. 1997. In vivo effects of T helper cell type 2 cytokines on macrophage antigen-presenting cell induction of T helper subsets. J. Immunol. 159:5834-5840.
    • (1997) J. Immunol. , vol.159 , pp. 5834-5840
    • Cua, D.J.1    Stohlman, S.A.2
  • 38
    • 0032762333 scopus 로고    scopus 로고
    • Exercise suppresses macrophage antigen presentation
    • Ceddia, M.A., and J.A. Woods. 1999. Exercise suppresses macrophage antigen presentation. J. Appl. Physiol. 87:2253-2258.
    • (1999) J. Appl. Physiol. , vol.87 , pp. 2253-2258
    • Ceddia, M.A.1    Woods, J.A.2
  • 40
    • 0033058811 scopus 로고    scopus 로고
    • Cysteine protease inhibitors as chemotherapy for parasitic infections
    • McKerrow, J.H., J.C. Engel, and C.R. Caffrey. 1999. Cysteine protease inhibitors as chemotherapy for parasitic infections. Bioorg. Med. Chem. 7:639-644.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 639-644
    • McKerrow, J.H.1    Engel, J.C.2    Caffrey, C.R.3
  • 41
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel, J.C., P.S. Doyle, I. Hsieh, and J.H. McKerrow. 1998. Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection. J. Exp. Med. 188:725-734.
    • (1998) J. Exp. Med. , vol.188 , pp. 725-734
    • Engel, J.C.1    Doyle, P.S.2    Hsieh, I.3    McKerrow, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.