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Volumn 255, Issue 1-2, 2009, Pages 41-45

Cathepsin G is differentially expressed in primary human antigen-presenting cells

Author keywords

B cells; Cathepsin; Cathepsin G; Myeloid DC; Plasmacytoid DC

Indexed keywords

ASPARTIC PROTEINASE; CATHEPSIN G; CYSTEINE; MYELIN BASIC PROTEIN;

EID: 59349120953     PISSN: 00088749     EISSN: 10902163     Source Type: Journal    
DOI: 10.1016/j.cellimm.2008.10.001     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau J., and Steinman R.M. Dendritic cells and the control of immunity. Nature 392 (1998) 245-252
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 2
    • 33845898737 scopus 로고    scopus 로고
    • Steady-state and inflammatory dendritic-cell development
    • Shortman K., and Naik S.H. Steady-state and inflammatory dendritic-cell development. Nat. Rev. Immunol. 7 (2007) 19-30
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 19-30
    • Shortman, K.1    Naik, S.H.2
  • 3
    • 26844581978 scopus 로고    scopus 로고
    • Gene family clustering identifies functionally associated subsets of human in vivo blood and tonsillar dendritic cells
    • Lindstedt M., Lundberg K., and Borrebaeck C.A. Gene family clustering identifies functionally associated subsets of human in vivo blood and tonsillar dendritic cells. J. Immunol. 175 (2005) 4839-4846
    • (2005) J. Immunol. , vol.175 , pp. 4839-4846
    • Lindstedt, M.1    Lundberg, K.2    Borrebaeck, C.A.3
  • 4
    • 33646513917 scopus 로고    scopus 로고
    • Cysteine cathepsins in the immune response
    • Zavasnik-Bergant T., and Turk B. Cysteine cathepsins in the immune response. Tissue Antigens 67 (2006) 349-355
    • (2006) Tissue Antigens , vol.67 , pp. 349-355
    • Zavasnik-Bergant, T.1    Turk, B.2
  • 5
    • 0033966413 scopus 로고    scopus 로고
    • Cathepsins and compartmentalization in antigen presentation
    • Riese R.J., and Chapman H.A. Cathepsins and compartmentalization in antigen presentation. Curr. Opin. Immunol. 12 (2000) 107-113
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 107-113
    • Riese, R.J.1    Chapman, H.A.2
  • 7
    • 26244458694 scopus 로고    scopus 로고
    • Asparaginyl endopeptidase: case history of a class II MHC compartment protease
    • Watts C., Matthews S.P., Mazzeo D., Manoury B., and Moss C.X. Asparaginyl endopeptidase: case history of a class II MHC compartment protease. Immunol. Rev. 207 (2005) 218-228
    • (2005) Immunol. Rev. , vol.207 , pp. 218-228
    • Watts, C.1    Matthews, S.P.2    Mazzeo, D.3    Manoury, B.4    Moss, C.X.5
  • 8
    • 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., Riese R.J., Peters C., Chapman H.A., and Ploegh H.L. Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism. J. Exp. Med. 186 (1997) 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
  • 11
    • 30044444910 scopus 로고    scopus 로고
    • Endosomal proteases in antigen presentation
    • Chapman H.A. Endosomal proteases in antigen presentation. Curr. Opin. Immunol. 18 (2006) 78-84
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 78-84
    • Chapman, H.A.1
  • 13
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • Yasuda Y., Li Z., Greenbaum D., Bogyo M., Weber E., and Bromme D. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279 (2004) 36761-36770
    • (2004) J. Biol. Chem. , vol.279 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Bromme, D.6
  • 15
    • 49149123424 scopus 로고    scopus 로고
    • Lysosomal cysteine and aspartic proteases are heterogeneously expressed and act redundantly to initiate human invariant chain degradation
    • Costantino C.M., Hang H.C., Kent S.C., Hafler D.A., and Ploegh H.L. Lysosomal cysteine and aspartic proteases are heterogeneously expressed and act redundantly to initiate human invariant chain degradation. J. Immunol. 180 (2008) 2876-2885
    • (2008) J. Immunol. , vol.180 , pp. 2876-2885
    • Costantino, C.M.1    Hang, H.C.2    Kent, S.C.3    Hafler, D.A.4    Ploegh, H.L.5
  • 16
    • 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., Riese R., Verhelst S., Driessen C., Li Z., Bromme D., Ploegh H.L., and Chapman H.A. Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med. 191 (2000) 1177-1186
    • (2000) J. Exp. Med. , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Bromme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 18
  • 22
    • 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., and Watts C. Destructive potential of the aspartyl protease cathepsin D in MHC class II-restricted antigen processing. Eur. J. Immunol. 35 (2005) 3442-3451
    • (2005) Eur. J. Immunol. , vol.35 , pp. 3442-3451
    • Moss, C.X.1    Villadangos, J.A.2    Watts, C.3
  • 23
    • 0026587182 scopus 로고
    • Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E
    • Bennett K., Levine T., Ellis J.S., Peanasky R.J., Samloff I.M., Kay J., and Chain B.M. Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E. Eur. J. Immunol. 22 (1992) 1519-1524
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1519-1524
    • Bennett, K.1    Levine, T.2    Ellis, J.S.3    Peanasky, R.J.4    Samloff, I.M.5    Kay, J.6    Chain, B.M.7
  • 24
  • 27
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum D., Medzihradszky K.F., Burlingame A., and Bogyo M. Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem. Biol. 7 (2000) 569-581
    • (2000) Chem. Biol. , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 28
    • 0025979246 scopus 로고
    • Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters
    • Oleksyszyn J., and Powers J.C. Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters. Biochemistry 30 (1991) 485-493
    • (1991) Biochemistry , vol.30 , pp. 485-493
    • Oleksyszyn, J.1    Powers, J.C.2
  • 30
    • 34247617743 scopus 로고    scopus 로고
    • Human CD4+ T cells displaying viral epitopes elicit a functional virus-specific memory CD8+ T cell response
    • Adamopoulou E., Diekmann J., Tolosa E., Kuntz G., Einsele H., Rammensee H.G., and Topp M.S. Human CD4+ T cells displaying viral epitopes elicit a functional virus-specific memory CD8+ T cell response. J. Immunol. 178 (2007) 5465-5472
    • (2007) J. Immunol. , vol.178 , pp. 5465-5472
    • Adamopoulou, E.1    Diekmann, J.2    Tolosa, E.3    Kuntz, G.4    Einsele, H.5    Rammensee, H.G.6    Topp, M.S.7
  • 33
    • 0035896750 scopus 로고    scopus 로고
    • Cytokines regulate proteolysis in major histocompatibility complex class II-dependent antigen presentation by dendritic cells
    • Fiebiger E., Meraner P., Weber E., Fang I.F., Stingl G., Ploegh H., and Maurer D. Cytokines regulate proteolysis in major histocompatibility complex class II-dependent antigen presentation by dendritic cells. J. Exp. Med. 193 (2001) 881-892
    • (2001) J. Exp. Med. , vol.193 , pp. 881-892
    • Fiebiger, E.1    Meraner, P.2    Weber, E.3    Fang, I.F.4    Stingl, G.5    Ploegh, H.6    Maurer, D.7
  • 35
    • 0141755165 scopus 로고    scopus 로고
    • Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo
    • Li D.N., Matthews S.P., Antoniou A.N., Mazzeo D., and Watts C. Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo. J. Biol. Chem. 278 (2003) 38980-38990
    • (2003) J. Biol. Chem. , vol.278 , pp. 38980-38990
    • Li, D.N.1    Matthews, S.P.2    Antoniou, A.N.3    Mazzeo, D.4    Watts, C.5
  • 36
    • 33947686680 scopus 로고    scopus 로고
    • Endocytosis targets exogenous material selectively to cathepsin S in live human dendritic cells, while cell-penetrating peptides mediate nonselective transport to cysteine cathepsins
    • Reich M., van Swieten P.F., Sommandas V., Kraus M., Fischer R., Weber E., Kalbacher H., Overkleeft H.S., and Driessen C. Endocytosis targets exogenous material selectively to cathepsin S in live human dendritic cells, while cell-penetrating peptides mediate nonselective transport to cysteine cathepsins. J. Leukoc. Biol. 81 (2007) 990-1001
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 990-1001
    • Reich, M.1    van Swieten, P.F.2    Sommandas, V.3    Kraus, M.4    Fischer, R.5    Weber, E.6    Kalbacher, H.7    Overkleeft, H.S.8    Driessen, C.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.