메뉴 건너뛰기




Volumn 168, Issue 2, 1996, Pages 248-254

Intracellular location of cysteine transport activity correlates with productive processing of antigen disulfide

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GALACTOSIDASE; GLUTATHIONE; HERMES ANTIGEN; LYSOZYME;

EID: 0029781197     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(199608)168:2<248::AID-JCP3>3.0.CO;2-P     Document Type: Article
Times cited : (39)

References (36)
  • 1
    • 0019740345 scopus 로고
    • Assay of glutathione, glutathione disulfide, and glutathione mixed disulfide in biological samples
    • Akerboom, T.P.M., and Sies, H. (1981) Assay of glutathione, glutathione disulfide, and glutathione mixed disulfide in biological samples. Methods Enzymol., 77:373-382.
    • (1981) Methods Enzymol. , vol.77 , pp. 373-382
    • Akerboom, T.P.M.1    Sies, H.2
  • 2
    • 0018347674 scopus 로고
    • Monoclonal cytolytic T cell lines
    • Baker, P.E., Gillis, S., and Smith, K.A. (1979) Monoclonal cytolytic T cell lines. J. Exp. Med., 149:273-278.
    • (1979) J. Exp. Med. , vol.149 , pp. 273-278
    • Baker, P.E.1    Gillis, S.2    Smith, K.A.3
  • 3
    • 0022638764 scopus 로고
    • Role of membrane transport in metabolism and function of glutathione in mammals
    • Bannai, S., and Tateishi, N. (1986) Role of membrane transport in metabolism and function of glutathione in mammals. J. Membr. Biol., 89:1-8.
    • (1986) J. Membr. Biol. , vol.89 , pp. 1-8
    • Bannai, S.1    Tateishi, N.2
  • 4
    • 43949161996 scopus 로고
    • How alpha beta T-cell receptors 'see' peptide/MHC complexes
    • Chien, Y.H., and Davis, M.M. (1993) How alpha beta T-cell receptors 'see' peptide/MHC complexes. Immunol. Today, 14:597-602.
    • (1993) Immunol. Today , vol.14 , pp. 597-602
    • Chien, Y.H.1    Davis, M.M.2
  • 5
    • 0026343001 scopus 로고
    • Reduction of disulfide bonds within lysosomes is a key step in antigen processing
    • Collins, D.S., Unanue, E.R., and Harding, C.V. (1991) Reduction of disulfide bonds within lysosomes is a key step in antigen processing. J. Immunol., 147:4054-4059.
    • (1991) J. Immunol. , vol.147 , pp. 4054-4059
    • Collins, D.S.1    Unanue, E.R.2    Harding, C.V.3
  • 6
    • 0642282644 scopus 로고
    • Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis
    • Cresswell, P. (1985) Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis. Proc. Natl. Acad. Sci. U.S.A., 82:8188-8192.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 8188-8192
    • Cresswell, P.1
  • 7
    • 0025281091 scopus 로고
    • Endocytosis, intracellular trafficking, and processing of membrane IgG and monovalent antigen/membrane IgG complexes in B lymphocytes
    • Davidson, H.W., West, M.A., and Collins, C. (1990) Endocytosis, intracellular trafficking, and processing of membrane IgG and monovalent antigen/membrane IgG complexes in B lymphocytes. J. Immunol., 144:4101-4109.
    • (1990) J. Immunol. , vol.144 , pp. 4101-4109
    • Davidson, H.W.1    West, M.A.2    Collins, C.3
  • 8
    • 0025010857 scopus 로고
    • Cleavage of disulfide bonds in endocytosed macromolecules: A processing not associated with lysosomes or endosomes
    • Feener, E.P., Shen, W.-C., and Ryser, H.J.-P. (1990) Cleavage of disulfide bonds in endocytosed macromolecules: A processing not associated with lysosomes or endosomes. J. Biol. Chem., 265:18780-18785.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18780-18785
    • Feener, E.P.1    Shen, W.-C.2    Ryser, H.J.-P.3
  • 9
    • 0014118789 scopus 로고
    • A spectrophometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitonde, M.K. (1967) A spectrophometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem. J., 104:627-633.
    • (1967) Biochem. J. , vol.104 , pp. 627-633
    • Gaitonde, M.K.1
  • 10
    • 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
  • 11
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J., and Sambrook, J. (1992) Protein folding in the cell. Nature, 355:33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 13
    • 0025014816 scopus 로고
    • Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment
    • Guagliardi, L.E., Koppelman, B., Blum, J.S., Marks, M.S., Cresswell, P., and Brodsky, F.M. (1990) Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment. Nature, 343:133-139.
    • (1990) Nature , vol.343 , pp. 133-139
    • Guagliardi, L.E.1    Koppelman, B.2    Blum, J.S.3    Marks, M.S.4    Cresswell, P.5    Brodsky, F.M.6
  • 14
    • 0026554717 scopus 로고
    • In vitro processing of insulin for recognition by murine T cells results in the generation of A chains with free CysSH
    • Hampl, J., Gradehandt, G., Kalbacher, H., and Rüde, E. (1992) In vitro processing of insulin for recognition by murine T cells results in the generation of A chains with free CysSH. J. Immunol., 148:2664-2671.
    • (1992) J. Immunol. , vol.148 , pp. 2664-2671
    • Hampl, J.1    Gradehandt, G.2    Kalbacher, H.3    Rüde, E.4
  • 15
    • 0025101104 scopus 로고
    • Low-temperature inhibition of antigen processing and iron uptake from transferrin: Deficits in endosome functions at 18°C
    • Harding, C.V., and Unanue, E.R. (1990) Low-temperature inhibition of antigen processing and iron uptake from transferrin: Deficits in endosome functions at 18°C. Eur. J. Immunol., 20:323-329.
    • (1990) Eur. J. Immunol. , vol.20 , pp. 323-329
    • Harding, C.V.1    Unanue, E.R.2
  • 16
    • 0026057743 scopus 로고
    • Liposome-encapsulated antigens are processed in lysosomes, recycled and presented to T cells
    • Harding, C.V., Collins, D.S., Slot, J.W., Geuze, H.J., and Unanue, E.R. (1991) Liposome-encapsulated antigens are processed in lysosomes, recycled and presented to T cells. Cell, 64:393-401.
    • (1991) Cell , vol.64 , pp. 393-401
    • Harding, C.V.1    Collins, D.S.2    Slot, J.W.3    Geuze, H.J.4    Unanue, E.R.5
  • 17
    • 0025945344 scopus 로고
    • Reduction of disulfide bonds during antigen processing: Evidence from a thiol-dependent insulin determinant
    • Jensen, P.E. (1991) Reduction of disulfide bonds during antigen processing: Evidence from a thiol-dependent insulin determinant. J. Exp. Med., 174:1121-1130.
    • (1991) J. Exp. Med. , vol.174 , pp. 1121-1130
    • Jensen, P.E.1
  • 19
    • 0020483282 scopus 로고
    • Role of thiols in degradation of proteins by cathepsins
    • Kooistra, T., Millard, P.C., and Lloyd, J.B. (1982) Role of thiols in degradation of proteins by cathepsins. Biochem. J., 204:471-477.
    • (1982) Biochem. J. , vol.204 , pp. 471-477
    • Kooistra, T.1    Millard, P.C.2    Lloyd, J.B.3
  • 20
    • 0023678814 scopus 로고
    • Functional analysis of cloned macrophage hybridomas. VI. Differential ability to induce immunity or suppression
    • Kuchroo, V.K., Minami, M., Diamond, B., and Dorf, M.E. (1988) Functional analysis of cloned macrophage hybridomas. VI. Differential ability to induce immunity or suppression. J. Immunol., 141:10-16.
    • (1988) J. Immunol. , vol.141 , pp. 10-16
    • Kuchroo, V.K.1    Minami, M.2    Diamond, B.3    Dorf, M.E.4
  • 21
    • 0022485546 scopus 로고
    • Disulfide reduction in lysosomes: The role of cysteine
    • Lloyd, J.B. (1986) Disulfide reduction in lysosomes: The role of cysteine. Biochem. J., 237:271-272.
    • (1986) Biochem. J. , vol.237 , pp. 271-272
    • Lloyd, J.B.1
  • 22
    • 0026657375 scopus 로고
    • Lysosomal handling of cystine residues: Stoichiometry of cysteine involvement
    • Lloyd, J.B. (1992) Lysosomal handling of cystine residues: Stoichiometry of cysteine involvement. Biochem. J., 286:979-980.
    • (1992) Biochem. J. , vol.286 , pp. 979-980
    • Lloyd, J.B.1
  • 23
    • 0027425130 scopus 로고
    • Antigen presentation by B lymphoma cells: Requirements for processing of exogenous antigen internalized through transferrin receptors
    • McCoy, K.L., Gainey, D., Inman, J.K., and Stutzman, R. (1993a) Antigen presentation by B lymphoma cells: Requirements for processing of exogenous antigen internalized through transferrin receptors. J. Immunol., 151:4583-4594.
    • (1993) J. Immunol. , vol.151 , pp. 4583-4594
    • McCoy, K.L.1    Gainey, D.2    Inman, J.K.3    Stutzman, R.4
  • 25
    • 0027133498 scopus 로고
    • Differences among various lineages of antigen-presenting cell in processing exogenous antigen internalized through transferrin receptors
    • McCoy, K.L., Page, M.S., Merkel, B.J., Inman, J.K., and Stutzman, R. (1993c) Differences among various lineages of antigen-presenting cell in processing exogenous antigen internalized through transferrin receptors. J. Immunol., 151:6757-6768.
    • (1993) J. Immunol. , vol.151 , pp. 6757-6768
    • McCoy, K.L.1    Page, M.S.2    Merkel, B.J.3    Inman, J.K.4    Stutzman, R.5
  • 26
    • 0021342631 scopus 로고
    • Role of thiols, pH, and cathepsin D in the lysosomal catabolism of serum albumin
    • Mego, J.L. (1984) Role of thiols, pH, and cathepsin D in the lysosomal catabolism of serum albumin. Biochem. J., 218:775-783.
    • (1984) Biochem. J. , vol.218 , pp. 775-783
    • Mego, J.L.1
  • 27
    • 0028869984 scopus 로고
    • Characterization of fibroblasts with a unique defect in processing antigens with disulfide bonds
    • Merkel, B.J., Mandel, R., Ryser, H.J.-P., and McCoy, K.L. (1995) Characterization of fibroblasts with a unique defect in processing antigens with disulfide bonds. J. Immunol., 154:128-136.
    • (1995) J. Immunol. , vol.154 , pp. 128-136
    • Merkel, B.J.1    Mandel, R.2    Ryser, H.J.-P.3    McCoy, K.L.4
  • 28
    • 0027510933 scopus 로고
    • Cell penetration of diphtheria toxin: Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol
    • Papini, E., Rappuoli, R., Murgia, M., and Montecucco, C. (1993) Cell penetration of diphtheria toxin: Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol. J. Biol. Chem., 268:1567-1574.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1567-1574
    • Papini, E.1    Rappuoli, R.2    Murgia, M.3    Montecucco, C.4
  • 29
    • 0025746712 scopus 로고
    • The transport systems of mammalian lysosomes
    • Pisoni, R.L., and Thoene, J.G. (1991) The transport systems of mammalian lysosomes. Biochim. Biophys. Acta, 1071:351-373.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 351-373
    • Pisoni, R.L.1    Thoene, J.G.2
  • 30
    • 0025098737 scopus 로고
    • A cysteine-specific lysosomal transport system provides a major route for the delivery of thiol to human fibroblast lysosomes: Possible role in supporting lysosomal proteolysis
    • Pisoni, R.L., Acker, T.L., Lisowski, K.M., Lemons, R.M., and Thoene, J.G. (1990) A cysteine-specific lysosomal transport system provides a major route for the delivery of thiol to human fibroblast lysosomes: Possible role in supporting lysosomal proteolysis. J. Cell Biol., 110:327-335.
    • (1990) J. Cell Biol. , vol.110 , pp. 327-335
    • Pisoni, R.L.1    Acker, T.L.2    Lisowski, K.M.3    Lemons, R.M.4    Thoene, J.G.5
  • 31
    • 0019413925 scopus 로고
    • Spontaneous release of a factor with properties of T cell growth factor from a continuous line of primate tumor T cells
    • Rabin, H., Hopkins, R.F., Ruscetti, F.W., Neubauer, R.H., Brown, R.L., and Kawakami, T.G. (1981) Spontaneous release of a factor with properties of T cell growth factor from a continuous line of primate tumor T cells. J. Immunol., 127:1852-1856.
    • (1981) J. Immunol. , vol.127 , pp. 1852-1856
    • Rabin, H.1    Hopkins, R.F.2    Ruscetti, F.W.3    Neubauer, R.H.4    Brown, R.L.5    Kawakami, T.G.6
  • 32
    • 0018400155 scopus 로고
    • Two species of lysosomal organelles in cultured human fibroblasts
    • Rome, L.H., Garvin, A.J., Allietta, M.M., and Neufeld, E.F. (1979) Two species of lysosomal organelles in cultured human fibroblasts. Cell, 17:143-153.
    • (1979) Cell , vol.17 , pp. 143-153
    • Rome, L.H.1    Garvin, A.J.2    Allietta, M.M.3    Neufeld, E.F.4
  • 33
    • 0025104207 scopus 로고
    • Disappearance of certain acidic organelles (endosomes and Langerhans cell granules) accompanies loss of antigen processing capacity upon culture of epidermal Langerhans cells
    • Stössel, H., Koch, F., Kämpgen, E., Stöger, P., Lenz, A., Heufler, C., Romani, N., and Schuler, G. (1990) Disappearance of certain acidic organelles (endosomes and Langerhans cell granules) accompanies loss of antigen processing capacity upon culture of epidermal Langerhans cells. J. Exp. Med., 172:1471-1482.
    • (1990) J. Exp. Med. , vol.172 , pp. 1471-1482
    • Stössel, H.1    Koch, F.2    Kämpgen, E.3    Stöger, P.4    Lenz, A.5    Heufler, C.6    Romani, N.7    Schuler, G.8
  • 35
    • 0026649769 scopus 로고
    • Diversity in MHC class II ovalbumin T cell epitopes generated by distinct proteases
    • Vidard, L., Rock, K.L., and Benacerraf, B. (1992) Diversity in MHC class II ovalbumin T cell epitopes generated by distinct proteases. J. Immunol., 149:498-504.
    • (1992) J. Immunol. , vol.149 , pp. 498-504
    • Vidard, L.1    Rock, K.L.2    Benacerraf, B.3
  • 36
    • 0029157082 scopus 로고
    • The novelty of antigen-processing compartments
    • Xu, X., and Pierce, S.K. (1995) The novelty of antigen-processing compartments. J. Immunol., 155:1652-1654.
    • (1995) J. Immunol. , vol.155 , pp. 1652-1654
    • Xu, X.1    Pierce, S.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.