메뉴 건너뛰기




Volumn 23, Issue , 2014, Pages 8-15

Endo-lysosomal proteases in antigen presentation

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN; ENDO LYSOSOMAL PROTEASE; PROTEINASE; TOLL LIKE RECEPTOR 9; UNCLASSIFIED DRUG; PEPTIDE HYDROLASE;

EID: 84908086156     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2014.08.011     Document Type: Review
Times cited : (34)

References (69)
  • 8
    • 82755167524 scopus 로고    scopus 로고
    • Cathepsins and their involvement in immune responses
    • Conus S., Simon H.U. Cathepsins and their involvement in immune responses. Swiss Med Wkly 2010, 140:13042.
    • (2010) Swiss Med Wkly , vol.140 , pp. 13042
    • Conus, S.1    Simon, H.U.2
  • 13
    • 82755189571 scopus 로고    scopus 로고
    • The endosome-lysosome pathway and information generation in the immune system
    • Watts C. The endosome-lysosome pathway and information generation in the immune system. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2012, 1824:14-21.
    • (2012) Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics , vol.1824 , pp. 14-21
    • Watts, C.1
  • 14
    • 84885978134 scopus 로고    scopus 로고
    • Proteases: essential actors in processing antigens and intracellular toll-like receptors
    • Manoury B. Proteases: essential actors in processing antigens and intracellular toll-like receptors. Frontiers Immunol 2013, 4:299.
    • (2013) Frontiers Immunol , vol.4 , pp. 299
    • Manoury, B.1
  • 16
    • 84897632293 scopus 로고    scopus 로고
    • Structural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stage
    • Zhao L., Hua T., Crowley C., Ru H., Ni X., Shaw N., Jiao L., Ding W., Qu L., Hung L.-W., Huang W., et al. Structural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stage. Cell Res 2014, 24:344-358.
    • (2014) Cell Res , vol.24 , pp. 344-358
    • Zhao, L.1    Hua, T.2    Crowley, C.3    Ru, H.4    Ni, X.5    Shaw, N.6    Jiao, L.7    Ding, W.8    Qu, L.9    Hung, L.-W.10    Huang, W.11
  • 17
    • 36348941660 scopus 로고    scopus 로고
    • Glycosaminoglycans facilitate procathepsin b activation through disruption of propeptide-mature enzyme interactions
    • Caglič D., Pungerčar J.R., Pejler G., Turk V., Turk B. Glycosaminoglycans facilitate procathepsin b activation through disruption of propeptide-mature enzyme interactions. J Biol Chem 2007, 282:33076-33085.
    • (2007) J Biol Chem , vol.282 , pp. 33076-33085
    • Caglič, D.1    Pungerčar, J.R.2    Pejler, G.3    Turk, V.4    Turk, B.5
  • 18
    • 71949093178 scopus 로고    scopus 로고
    • Activation of cathepsin d by glycosaminoglycans
    • Beckman M., Freeman C., Parish C.R., Small D.H. Activation of cathepsin d by glycosaminoglycans. FEBS J 2009, 276:7343-7352.
    • (2009) FEBS J , vol.276 , pp. 7343-7352
    • Beckman, M.1    Freeman, C.2    Parish, C.R.3    Small, D.H.4
  • 19
    • 0041876230 scopus 로고    scopus 로고
    • Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice
    • Shirahama-Noda K., Yamamoto A., Sugihara K., Hashimoto N., Asano M., Nishimura M., Hara-Nishimura I. Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice. J Biol Chem 2003, 278:33194-33199.
    • (2003) J Biol Chem , vol.278 , pp. 33194-33199
    • Shirahama-Noda, K.1    Yamamoto, A.2    Sugihara, K.3    Hashimoto, N.4    Asano, M.5    Nishimura, M.6    Hara-Nishimura, I.7
  • 20
    • 14844340568 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    • Delamarre L., Pack M., Chang H., Mellman I., Trombetta E.S. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science 2005, 307:1630-1634.
    • (2005) Science , vol.307 , pp. 1630-1634
    • Delamarre, L.1    Pack, M.2    Chang, H.3    Mellman, I.4    Trombetta, E.S.5
  • 21
    • 64449088219 scopus 로고    scopus 로고
    • The small gtpase rac2 controls phagosomal alkalinization and antigen crosspresentation selectively in cd8(+) dendritic cells
    • Savina A., Peres A., Cebrian I., Carmo N., Moita C., Hacohen N., Moita L.F., Amigorena S. The small gtpase rac2 controls phagosomal alkalinization and antigen crosspresentation selectively in cd8(+) dendritic cells. Immunity 2009, 30:544-555.
    • (2009) Immunity , vol.30 , pp. 544-555
    • Savina, A.1    Peres, A.2    Cebrian, I.3    Carmo, N.4    Moita, C.5    Hacohen, N.6    Moita, L.F.7    Amigorena, S.8
  • 22
    • 84872474723 scopus 로고    scopus 로고
    • Reactive oxygen species production in the phagosome: impact on antigen presentation in dendritic cells
    • Kotsias F., Hoffmann E., Amigorena S., Savina A. Reactive oxygen species production in the phagosome: impact on antigen presentation in dendritic cells. Antioxidants Redox Signal 2013, 18:714-729.
    • (2013) Antioxidants Redox Signal , vol.18 , pp. 714-729
    • Kotsias, F.1    Hoffmann, E.2    Amigorena, S.3    Savina, A.4
  • 23
    • 17444370883 scopus 로고    scopus 로고
    • Specific inactivation of cysteine protease-type cathepsin by singlet oxygen generated from naphthalene endoperoxides
    • Nagaoka Y., Otsu K., Okada F., Sato K., Ohba Y., Kotani N., Fujii J. Specific inactivation of cysteine protease-type cathepsin by singlet oxygen generated from naphthalene endoperoxides. Biochem Biophys Res Commun 2005, 331:215-223.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 215-223
    • Nagaoka, Y.1    Otsu, K.2    Okada, F.3    Sato, K.4    Ohba, Y.5    Kotani, N.6    Fujii, J.7
  • 24
    • 30044444910 scopus 로고    scopus 로고
    • Endosomal proteases in antigen presentation
    • Chapman H.A. Endosomal proteases in antigen presentation. Curr Opin Immunol 2006, 18:78-84.
    • (2006) Curr Opin Immunol , vol.18 , pp. 78-84
    • Chapman, H.A.1
  • 25
    • 0006380659 scopus 로고
    • Cdna clone for the human invariant gamma chain of class II histocompatibility antigens and its implications for the protein structure
    • Claesson L., Larhammar D., Rask L., Peterson P.A. Cdna clone for the human invariant gamma chain of class II histocompatibility antigens and its implications for the protein structure. Proc Nat Acad Sci USA 1983, 80:7395-7399.
    • (1983) Proc Nat Acad Sci USA , vol.80 , pp. 7395-7399
    • Claesson, L.1    Larhammar, D.2    Rask, L.3    Peterson, P.A.4
  • 26
    • 0026440236 scopus 로고
    • Hla-dr molecules from an antigen-processing mutant-cell line are associated with invariant chain peptides
    • Riberdy J.M., Newcomb J.R., Surman M.J., Barbosa J.A., Cresswell P. Hla-dr molecules from an antigen-processing mutant-cell line are associated with invariant chain peptides. Nature 1992, 360:474-477.
    • (1992) Nature , vol.360 , pp. 474-477
    • Riberdy, J.M.1    Newcomb, J.R.2    Surman, M.J.3    Barbosa, J.A.4    Cresswell, P.5
  • 28
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class-II hla antigens
    • Blum J.S., Cresswell P. Role for intracellular proteases in the processing and transport of class-II hla antigens. Proc Natl Acad Sci USA 1988, 85:3975-3979.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3975-3979
    • Blum, J.S.1    Cresswell, P.2
  • 29
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin s in mhc class II - associated invariant chain processing and peptide loading
    • Riese R.J., Wolf P.R., Bromme D., Natkin L.R., Villadangos J.A., Ploegh H.L., Chapman H.A. Essential role for cathepsin s in mhc class II - associated invariant chain processing and peptide loading. Immunity 1996, 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
  • 30
    • 0029979452 scopus 로고    scopus 로고
    • Trafficking of major histocompatibility complex class II molecules through intracellular compartments containing hla-dm
    • Robbins N.F., Hammond C., Denzin L.K., Pan M., Cresswell P. Trafficking of major histocompatibility complex class II molecules through intracellular compartments containing hla-dm. Hum Immunol 1996, 45:13-23.
    • (1996) Hum Immunol , vol.45 , pp. 13-23
    • Robbins, N.F.1    Hammond, C.2    Denzin, L.K.3    Pan, M.4    Cresswell, P.5
  • 32
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer J.T., Rasnick D., Klaus J.L., Bromme D. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J Med Chem 1995, 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
  • 35
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin f in invariant chain processing and major histocompatibility complex class ii peptide loading by macrophages
    • Shi G.P., Bryant R.A.R., Riese R., Verhelst S., Driessen C., Li Z.Q., Bromme D., Ploegh H.L., Chapman H.A. Role for cathepsin f in invariant chain processing and major histocompatibility complex class ii peptide loading by macrophages. J Exp Med 2000, 191:1177-1185.
    • (2000) J Exp Med , vol.191 , pp. 1177-1185
    • Shi, G.P.1    Bryant, R.A.R.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.Q.6    Bromme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 36
    • 1042278900 scopus 로고    scopus 로고
    • Class ii mhc peptide loading by the professionals
    • Bryant P., Ploegh H. Class ii mhc peptide loading by the professionals. Curr Opin Immunol 2004, 16:96-102.
    • (2004) Curr Opin Immunol , vol.16 , pp. 96-102
    • Bryant, P.1    Ploegh, H.2
  • 37
    • 0037396716 scopus 로고    scopus 로고
    • Asparagine endopeptidase can initiate the removal of the mhc class ii invariant chain chaperone
    • Manoury B., Mazzeo D., Li D.T.N., Billson J., Loak K., Benaroch P., Watts C. Asparagine endopeptidase can initiate the removal of the mhc class ii invariant chain chaperone. Immunity 2003, 18:489-498.
    • (2003) Immunity , vol.18 , pp. 489-498
    • Manoury, B.1    Mazzeo, D.2    Li, D.T.N.3    Billson, J.4    Loak, K.5    Benaroch, P.6    Watts, C.7
  • 43
    • 33748475526 scopus 로고    scopus 로고
    • Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis
    • Delamarre L., Couture R., Mellman I., Trombetta E.S. Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis. J Exp Med 2006, 203:2049-2055.
    • (2006) J Exp Med , vol.203 , pp. 2049-2055
    • Delamarre, L.1    Couture, R.2    Mellman, I.3    Trombetta, E.S.4
  • 44
    • 70449336081 scopus 로고    scopus 로고
    • Diverse regulatory roles for lysosomal proteases in the immune response
    • Colbert J.D., Matthews S.P., Miller G., Watts C. Diverse regulatory roles for lysosomal proteases in the immune response. Eur J Immunol 2009, 39:2955-2965.
    • (2009) Eur J Immunol , vol.39 , pp. 2955-2965
    • Colbert, J.D.1    Matthews, S.P.2    Miller, G.3    Watts, C.4
  • 45
    • 29744469796 scopus 로고    scopus 로고
    • Destructive potential of the aspartyl protease cathepsin d in mhc class ii-restricted antigen processing
    • Moss C.X., Villadangos J.A., Watts C. Destructive potential of the aspartyl protease cathepsin d in mhc class ii-restricted antigen processing. Eur J Immunol 2005, 35:3442-3451.
    • (2005) Eur J Immunol , vol.35 , pp. 3442-3451
    • Moss, C.X.1    Villadangos, J.A.2    Watts, C.3
  • 46
    • 0031573151 scopus 로고    scopus 로고
    • Natural processing sites for human cathepsin e and cathepsin d in tetanus toxin - implications for t cell epitope generation
    • Zaidi N., Burster T., Sommandas V., Herrmann T., Boehm B.O., Driessen C., Voelter W., Kallbacher H. Natural processing sites for human cathepsin e and cathepsin d in tetanus toxin - implications for t cell epitope generation. J Immunol 1997, 159:4693-4699.
    • (1997) J Immunol , vol.159 , pp. 4693-4699
    • Zaidi, N.1    Burster, T.2    Sommandas, V.3    Herrmann, T.4    Boehm, B.O.5    Driessen, C.6    Voelter, W.7    Kallbacher, H.8
  • 47
    • 35448940482 scopus 로고    scopus 로고
    • A novel cell penetrating aspartic protease inhibitor blocks processing and presentation of tetanus toxoid more efficiently than pepstatin a
    • Zaidi N., Burster T., Sommandas V., Herrmann T., Boehm B.O., Driessen C., Voelter W., Kalbacher H. A novel cell penetrating aspartic protease inhibitor blocks processing and presentation of tetanus toxoid more efficiently than pepstatin a. Biochem Biophys Res Commun 2007, 364:243-249.
    • (2007) Biochem Biophys Res Commun , vol.364 , pp. 243-249
    • Zaidi, N.1    Burster, T.2    Sommandas, V.3    Herrmann, T.4    Boehm, B.O.5    Driessen, C.6    Voelter, W.7    Kalbacher, H.8
  • 48
    • 33744801689 scopus 로고    scopus 로고
    • Mannose-pepstatin conjugates as targeted inhibitors of antigen processing
    • Free P., Hurley C.A., Kageyama T., Chain B.M., Tabor A.B. Mannose-pepstatin conjugates as targeted inhibitors of antigen processing. Org Biomol Chem 2006, 4:1817-1830.
    • (2006) Org Biomol Chem , vol.4 , pp. 1817-1830
    • Free, P.1    Hurley, C.A.2    Kageyama, T.3    Chain, B.M.4    Tabor, A.B.5
  • 50
    • 0033696962 scopus 로고    scopus 로고
    • Control of antigen presentation by a single protease cleavage site
    • Antoniou A.N., Blackwood S.L., Mazzeo D., Watts C. Control of antigen presentation by a single protease cleavage site. Immunity 2000, 12:391-398.
    • (2000) Immunity , vol.12 , pp. 391-398
    • Antoniou, A.N.1    Blackwood, S.L.2    Mazzeo, D.3    Watts, C.4
  • 51
    • 0032542285 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase processes a microbial antigen for class ii mhc presentation
    • Manoury B., Hewitt E.W., Morrice N., Dando P.M., Barrett A.J., Watts C. An asparaginyl endopeptidase processes a microbial antigen for class ii mhc presentation. Nature 1998, 396:695-699.
    • (1998) Nature , vol.396 , pp. 695-699
    • Manoury, B.1    Hewitt, E.W.2    Morrice, N.3    Dando, P.M.4    Barrett, A.J.5    Watts, C.6
  • 53
  • 54
  • 56
  • 57
    • 56349114913 scopus 로고    scopus 로고
    • Proteolytic cleavage in an endolysosomal compartment is required for activation of toll-like receptor 9
    • Park B., Brinkmann M.M., Spooner E., Lee C.C., Kim Y.-M., Ploegh H.L. Proteolytic cleavage in an endolysosomal compartment is required for activation of toll-like receptor 9. Nat Immunol 2008, 9:1407-1414.
    • (2008) Nat Immunol , vol.9 , pp. 1407-1414
    • Park, B.1    Brinkmann, M.M.2    Spooner, E.3    Lee, C.C.4    Kim, Y.-M.5    Ploegh, H.L.6
  • 59
    • 79955743119 scopus 로고    scopus 로고
    • Nucleic acid recognition by toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase
    • Ewald S.E., Engel A., Lee J., Wang M., Bogyo M., Barton G.M. Nucleic acid recognition by toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase. J Exp Med 2011, 208:643-651.
    • (2011) J Exp Med , vol.208 , pp. 643-651
    • Ewald, S.E.1    Engel, A.2    Lee, J.3    Wang, M.4    Bogyo, M.5    Barton, G.M.6
  • 61
    • 84866558003 scopus 로고    scopus 로고
    • Proteolytic processing regulates toll-like receptor 3 stability and endosomal localization
    • Qi R., Singh D., Kao C.C. Proteolytic processing regulates toll-like receptor 3 stability and endosomal localization. J Biol Chem 2012, 287:32617-32629.
    • (2012) J Biol Chem , vol.287 , pp. 32617-32629
    • Qi, R.1    Singh, D.2    Kao, C.C.3
  • 64
    • 0242495719 scopus 로고    scopus 로고
    • The protease inhibitor cystatin c is differentially expressed among dendritic cell populations, but does not control antigen presentation
    • El-Sukkari D., Wilson N.S., Hakansson K., Steptoe R.J., Grubb A., Shortman K., Villadangos J.A. The protease inhibitor cystatin c is differentially expressed among dendritic cell populations, but does not control antigen presentation. J Immunol 2003, 171:5003-5011.
    • (2003) J Immunol , vol.171 , pp. 5003-5011
    • El-Sukkari, D.1    Wilson, N.S.2    Hakansson, K.3    Steptoe, R.J.4    Grubb, A.5    Shortman, K.6    Villadangos, J.A.7
  • 65
    • 0039547996 scopus 로고    scopus 로고
    • Crystal structure of mhc class ii-associated p41 ii fragment bound to cathepsin l reveals the structural basis for differentiation between cathepsins l and s
    • Guncar G., Pungercic G., Klemencic I., Turk V., Turk D. Crystal structure of mhc class ii-associated p41 ii fragment bound to cathepsin l reveals the structural basis for differentiation between cathepsins l and s. EMBO J 1999, 18:793-803.
    • (1999) EMBO J , vol.18 , pp. 793-803
    • Guncar, G.1    Pungercic, G.2    Klemencic, I.3    Turk, V.4    Turk, D.5
  • 68
    • 0035933763 scopus 로고    scopus 로고
    • Cathepsin S regulates the expression of cathepsin L and the turnover of γ-interferon inducible lysosomal thiol reductase in B-lymphocytes
    • Honey K., Duff M., Beers C., Brissette W.H., Elliot E.A., Peters C., Maric M., Cresswell P., Rudensky A. Cathepsin S regulates the expression of cathepsin L and the turnover of γ-interferon inducible lysosomal thiol reductase in B-lymphocytes. J Biol Chem 2001, 276:22573-22578.
    • (2001) J Biol Chem , vol.276 , pp. 22573-22578
    • Honey, K.1    Duff, M.2    Beers, C.3    Brissette, W.H.4    Elliot, E.A.5    Peters, C.6    Maric, M.7    Cresswell, P.8    Rudensky, A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.