메뉴 건너뛰기




Volumn 8, Issue 2, 1996, Pages 211-219

Monoclonal IgG as antigens: Reduction is an early intracellular event of their processing by antigen-presenting cells

Author keywords

Antigen; IgG; Partial reduction; Presentation; Processing

Indexed keywords

ANTIGEN; CD4 ANTIGEN; IMMUNOGLOBULIN G; IMMUNOGLOBULIN KAPPA CHAIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MONOCLONAL ANTIBODY; PARAPROTEIN;

EID: 0030060413     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/8.2.211     Document Type: Article
Times cited : (11)

References (49)
  • 1
    • 0025943152 scopus 로고
    • Imaging and therapy with monoclonal antibodies in non-hematopoietic tumors
    • Mach, J -P., Pèlegrin, A. and Buchegger, F. 1991 Imaging and therapy with monoclonal antibodies in non-hematopoietic tumors. Curr Opin Immunol. 3:685
    • (1991) Curr Opin Immunol. , vol.3 , pp. 685
    • Mach, J.-P.1    Pèlegrin, A.2    Buchegger, F.3
  • 2
    • 0026613775 scopus 로고
    • Antibody conjugates for the treatment of cancer
    • Pietersz, G A. and McKenzie, I. F. C. 1992. Antibody conjugates for the treatment of cancer Immunol Rev 129:57.
    • (1992) Immunol Rev , vol.129 , pp. 57
    • Pietersz, G.A.1    McKenzie, I.F.C.2
  • 3
    • 0023850125 scopus 로고
    • Antibodies as antigens. the use of mouse monoclonal antibodies to focus human T cells against selected targets
    • Lanzavecchia, A., Abrignani, S., Scheidegger, D., Obrist, R., Dörken, B. and Moldenhauer, G. 1988. Antibodies as antigens. The use of mouse monoclonal antibodies to focus human T cells against selected targets J. Exp. Med. 167:345.
    • (1988) J. Exp. Med. , vol.167 , pp. 345
    • Lanzavecchia, A.1    Abrignani, S.2    Scheidegger, D.3    Obrist, R.4    Dörken, B.5    Moldenhauer, G.6
  • 4
    • 0025826979 scopus 로고
    • Patients receiving murine monoclonal antibody therapy for malignancy develop T cells that proliferate in vitro in response to these antibodies as antigens
    • Kosmas, C., Epenetos, A A. and Courtenay-Luck, N. S. 1991. Patients receiving murine monoclonal antibody therapy for malignancy develop T cells that proliferate in vitro in response to these antibodies as antigens. Br. J. Cancer 64:494.
    • (1991) Br. J. Cancer , vol.64 , pp. 494
    • Kosmas, C.1    Epenetos, A.A.2    Courtenay-Luck, N.S.3
  • 5
    • 0001581895 scopus 로고
    • Peptide binding to the major histocompatiblity complex molecules
    • Madden, D. R. and Wiley, D. C. 1992. Peptide binding to the major histocompatiblity complex molecules. Curr. Opin. Struc. Biol. 2:1411
    • (1992) Curr. Opin. Struc. Biol. , vol.2 , pp. 1411
    • Madden, D.R.1    Wiley, D.C.2
  • 7
    • 0027513540 scopus 로고
    • Cell biology of antigen presentation
    • Neefjes, J J and Momburg, F 1993. Cell biology of antigen presentation. Curr Opin Immunol 5:27.
    • (1993) Curr Opin Immunol , vol.5 , pp. 27
    • Neefjes, J.J.1    Momburg, F.2
  • 9
    • 0028200118 scopus 로고
    • Transient accumulation of new class II MHC molecules in a novel endocytic compartment in B lymphocytes
    • Amigorena, S., Drake, J. R., Webster, P. and Meliman, I 1994. Transient accumulation of new class II MHC molecules in a novel endocytic compartment in B lymphocytes. Nature 369:113.
    • (1994) Nature , vol.369 , pp. 113
    • Amigorena, S.1    Drake, J.R.2    Webster, P.3    Meliman, I.4
  • 10
    • 0028229009 scopus 로고
    • Isolation and characterization of the intracellular MHC class II compartment
    • Tulp, A., Verwoerd, D., Dobberstein, B , Ploegh, H. L. and Pieters, J. 1994. Isolation and characterization of the intracellular MHC class II compartment. Nature 369:120
    • (1994) Nature , vol.369 , pp. 120
    • Tulp, A.1    Verwoerd, D.2    Dobberstein, B.3    Ploegh, H.L.4    Pieters, J.5
  • 11
    • 0028303848 scopus 로고
    • Antigen processing and class II MHC peptide-loading compartments in human B-lymphoblastoid cells
    • West, M. A., Lucocq, J. M. and Watts, C. 1994. Antigen processing and class II MHC peptide-loading compartments in human B-lymphoblastoid cells. Nature 369:147.
    • (1994) Nature , vol.369 , pp. 147
    • West, M.A.1    Lucocq, J.M.2    Watts, C.3
  • 12
    • 0021099317 scopus 로고
    • Intracellular dissociation of receptor-bound asialoglycoproteins in cultured hepatocytes
    • Harford, J., Bridges, K., Ashwell, G and Klausner, R. D. 1983. Intracellular dissociation of receptor-bound asialoglycoproteins in cultured hepatocytes. J. Biol. Chem. 258:3191.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3191
    • Harford, J.1    Bridges, K.2    Ashwell, G.3    Klausner, R.D.4
  • 13
    • 0020508846 scopus 로고
    • The binding and processing of monoclonal human IgG1 by cells of a human macrophage-like cell line (U937)
    • Kurlander, J. R. and Gartrell, J. E 1983 The binding and processing of monoclonal human IgG1 by cells of a human macrophage-like cell line (U937). Blood 62:652
    • (1983) Blood , vol.62 , pp. 652
    • Kurlander, J.R.1    Gartrell, J.E.2
  • 14
    • 0021220948 scopus 로고
    • Internalization and degradation of macrophages Fc receptors bound to polyvalent immune complexes
    • Mellman, I. and Plutner, H. 1984 Internalization and degradation of macrophages Fc receptors bound to polyvalent immune complexes J. Cell Biol. 98:1170.
    • (1984) J. Cell Biol. , vol.98 , pp. 1170
    • Mellman, I.1    Plutner, H.2
  • 15
    • 0013401957 scopus 로고
    • Internalization and rapid recycling of macrophage Fc receptors tagged with monovalent antireceptor antibody possible role of a prelysosomal compartment
    • Mellman, I , Plutner, H. and Ukkonen, P 1984. Internalization and rapid recycling of macrophage Fc receptors tagged with monovalent antireceptor antibody possible role of a prelysosomal compartment. J. Cell Biol. 98:1163.
    • (1984) J. Cell Biol. , vol.98 , pp. 1163
    • Mellman, I.1    Plutner, H.2    Ukkonen, P.3
  • 17
    • 0027741225 scopus 로고
    • Bases moléculaires de la diversité fonctionnelle des récepteurs des anticorps
    • Bonnerot, C and Fridman, H. 1993. Bases moléculaires de la diversité fonctionnelle des récepteurs des anticorps. Médecine/Sciences 9:1236.
    • (1993) Médecine/Sciences , vol.9 , pp. 1236
    • Bonnerot, C.1    Fridman, H.2
  • 18
    • 0023838601 scopus 로고
    • Processing by accessory cells for presentation to murine T cells of apamin, a disulfide-bonded 18 amino acid peptide
    • Régnier-Vigouroux, A , El Ayeb, M , Defendini, M -L., Gragnier. C and Pierres, M. 1988 Processing by accessory cells for presentation to murine T cells of apamin, a disulfide-bonded 18 amino acid peptide. J. Immunol. 140:1069.
    • (1988) J. Immunol. , vol.140 , pp. 1069
    • Régnier-Vigouroux, A.1    El Ayeb, M.2    Defendini, M.-L.3    Gragnier, C.4    Pierres, M.5
  • 19
    • 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 Immuol 147:4054
    • (1991) J Immuol , vol.147 , pp. 4054
    • Collins, D.S.1    Unanue, E.R.2    Harding, C.V.3
  • 20
    • 0027155945 scopus 로고
    • Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class II MHC
    • Jensen, P E 1993 Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class II MHC. J Immunol 150:3347.
    • (1993) J Immunol , vol.150 , pp. 3347
    • Jensen, P.E.1
  • 22
    • 0022636572 scopus 로고
    • A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells
    • Buus, S. and Werdelin, O. 1986. A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells. J. Immunol 136:452
    • (1986) J. Immunol , vol.136 , pp. 452
    • Buus, S.1    Werdelin, O.2
  • 23
    • 0023732394 scopus 로고
    • Selective inhibition of antigen presentation to cloned T cells by protease inhibitors
    • Puri, J. and Factorovich, Y 1988. Selective inhibition of antigen presentation to cloned T cells by protease inhibitors. J Immunol. 141:3313.
    • (1988) J Immunol. , vol.141 , pp. 3313
    • Puri, J.1    Factorovich, Y.2
  • 24
    • 0024519165 scopus 로고
    • Identification of proteases that process distinct epitopes on the same protein
    • Takahashi, H., Cease, K. B. and Berzofsky, J. A. 1989 Identification of proteases that process distinct epitopes on the same protein. J. Immunol 142:2221.
    • (1989) J. Immunol , vol.142 , pp. 2221
    • Takahashi, H.1    Cease, K.B.2    Berzofsky, J.A.3
  • 25
    • 0025074904 scopus 로고
    • Different roles for thiol and aspartyl proteases in antigen presentation of ovalbumin
    • Diment, S 1990. Different roles for thiol and aspartyl proteases in antigen presentation of ovalbumin. J. Immunol. 145:417
    • (1990) J. Immunol. , vol.145 , pp. 417
    • Diment, S.1
  • 26
    • 0025830862 scopus 로고
    • Antigen processing by endosomal proteases determines which sites of sperm-whale myoglobin are eventually recognized by T cells
    • Van Noort, J M., Boon, J., Van der Drift, A. C. M., Wagenaar, J P. A., Boots, A. M. H. and Boog, C. J. P 1991 Antigen processing by endosomal proteases determines which sites of sperm-whale myoglobin are eventually recognized by T cells Eur J Immunol 21:1989
    • (1991) Eur J Immunol , vol.21 , pp. 1989
    • Van Noort, J.M.1    Boon, J.2    Van Der Drift, A.C.M.3    Wagenaar, J.P.A.4    Boots, A.M.H.5    Boog, C.J.P.6
  • 28
    • 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., Creswell, P. and Brodsky, F. M 1990 Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment. Nature 343:133.
    • (1990) Nature , vol.343 , pp. 133
    • Guagliardi, L.E.1    Koppelman, B.2    Blum, J.S.3    Marks, M.S.4    Creswell, P.5    Brodsky, F.M.6
  • 29
    • 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 1992. Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E. Eur. J. Immunol. 22:1519.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1519
    • 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
  • 30
    • 0027161614 scopus 로고
    • Participation of cathepsin B in processing of antigen presentation to MHC class II
    • Matsunaga, Y., Saibara, T., Kido, H. and Katunuma, N. 1993 Participation of cathepsin B in processing of antigen presentation to MHC class II FEBS Lett 324:325.
    • (1993) FEBS Lett , vol.324 , pp. 325
    • Matsunaga, Y.1    Saibara, T.2    Kido, H.3    Katunuma, N.4
  • 31
    • 0026640688 scopus 로고
    • Role of cathepsin D in antigen presentation of ovalbumin
    • Rodriguez, G M. and Diment, S. 1992. Role of cathepsin D in antigen presentation of ovalbumin. J. Immunol. 149.2894.
    • (1992) J. Immunol. , vol.149 , pp. 2894
    • Rodriguez, G.M.1    Diment, S.2
  • 32
    • 0025895698 scopus 로고
    • The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins
    • Kominami, E , Ueno, T , Muno, D and Katunuma, N 1991. The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins. FEBS Lett. 287 189
    • (1991) FEBS Lett. , vol.287 , pp. 189
    • Kominami, E.1    Ueno, T.2    Muno, D.3    Katunuma, N.4
  • 33
    • 0025987838 scopus 로고
    • The endo/lysosomal protease cathepsin B is able to process conalbumin fragments for presentation to T cells
    • Gradehandt, G. and Ruede, E 1991 The endo/lysosomal protease cathepsin B is able to process conalbumin fragments for presentation to T cells. Immunology 74.393
    • (1991) Immunology , vol.74 , pp. 393
    • Gradehandt, G.1    Ruede, E.2
  • 34
    • 0028275823 scopus 로고
    • Covalent binding of C3b to monoclonal antibodies selectively up-regulates heavy chain epitope recognition by T cells
    • Santoro, L., Drouet, C , Reboul, A., Mach, J.-P. and Colomb, M. G. 1994. Covalent binding of C3b to monoclonal antibodies selectively up-regulates heavy chain epitope recognition by T cells. Eur J Immunol. 24:1620.
    • (1994) Eur J Immunol. , vol.24 , pp. 1620
    • Santoro, L.1    Drouet, C.2    Reboul, A.3    Mach, J.-P.4    Colomb, M.G.5
  • 36
    • 0004648779 scopus 로고
    • Chemical studies on immunoglobulins in a new preparative procedure for γ-globulins employing glycine-rich solvent systems
    • Porath, J. and Ui, N. 1964. Chemical studies on immunoglobulins in a new preparative procedure for γ-globulins employing glycine-rich solvent systems. Biochim. Biophys. Acta 90:324.
    • (1964) Biochim. Biophys. Acta , vol.90 , pp. 324
    • Porath, J.1    Ui, N.2
  • 37
    • 0019817187 scopus 로고
    • Iodination of proteins, glycoproteins and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3α,6α-diphenyl glycoluril (lodogen)
    • Salacinski, P. R. P , McLean, C , Sykes, J. E. C., Clement-Jones, V. V. and Lowry, P J 1981. Iodination of proteins, glycoproteins and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3α,6α-diphenyl glycoluril (lodogen) Anal. Biochem 117:136.
    • (1981) Anal. Biochem , vol.117 , pp. 136
    • Salacinski, P.R.P.1    McLean, C.2    Sykes, J.E.C.3    Clement-Jones, V.V.4    Lowry, P.J.5
  • 38
    • 0017368370 scopus 로고
    • Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase
    • Penefsky, H. S. 1977 Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase J. Biol Chem. 252 2891.
    • (1977) J. Biol Chem. , vol.252 , pp. 2891
    • Penefsky, H.S.1
  • 39
    • 0021327612 scopus 로고
    • Epstein-Barr virus susceptibility of normal B lymphocyte populations
    • Aman, P., Ehlin-Henriksson, B and Klein, G 1984 Epstein-Barr virus susceptibility of normal B lymphocyte populations J. Exp. Med 159:208.
    • (1984) J. Exp. Med , vol.159 , pp. 208
    • Aman, P.1    Ehlin-Henriksson, B.2    Klein, G.3
  • 40
    • 0023205553 scopus 로고
    • Human T clones reactive to the sexual stages of Plasmodium falciparum malaria. High frequency of gamete-reactive T cells in peripheral blood from nonexposed donors
    • Good, M. F., Quakyi, I. A., Saul, A , Berzofsky, J A., Carter, R. and Miller, L. H. 1987. Human T clones reactive to the sexual stages of Plasmodium falciparum malaria. High frequency of gamete-reactive T cells in peripheral blood from nonexposed donors J Immunol. 138.306.
    • (1987) J Immunol. , vol.138 , pp. 306
    • Good, M.F.1    Quakyi, I.A.2    Saul, A.3    Berzofsky, J.A.4    Carter, R.5    Miller, L.H.6
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U K 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 42
    • 0021343351 scopus 로고
    • Measurement of cell numbers by means of the endogenous enzyme hexosaminidase Applications to detection of lymphokines and cell surface antigens
    • Landegren, U. 1984. Measurement of cell numbers by means of the endogenous enzyme hexosaminidase Applications to detection of lymphokines and cell surface antigens J Immunol Methods 67.379.
    • (1984) J Immunol Methods , vol.67 , pp. 379
    • Landegren, U.1
  • 43
    • 0024498412 scopus 로고
    • Binding to la protects an immunogenic peptide from proteolytic degradation
    • Donermeyer, D L. and Allen, P M. 1989. Binding to la protects an immunogenic peptide from proteolytic degradation. J. Immunol. 142.1063.
    • (1989) J. Immunol. , vol.142 , pp. 1063
    • Donermeyer, D.L.1    Allen, P.M.2
  • 44
    • 0024411158 scopus 로고
    • Secretion, cleavage and binding of complement component C3 by human monocytic cell line U937
    • Maison, C. M., Villiers, C. L. and Colomb, M G. 1989. Secretion, cleavage and binding of complement component C3 by human monocytic cell line U937. Biochem. J. 261:407.
    • (1989) Biochem. J. , vol.261 , pp. 407
    • Maison, C.M.1    Villiers, C.L.2    Colomb, M.G.3
  • 45
    • 0022485546 scopus 로고
    • Disulphide reduction in lysosomes. The role of cysteine
    • Lloyd, J. B. 1986. Disulphide reduction in lysosomes. The role of cysteine. Biochem. J. 237:271.
    • (1986) Biochem. J. , vol.237 , pp. 271
    • Lloyd, J.B.1
  • 46
    • 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.
    • (1990) J. Cell. Biol. , vol.110 , pp. 327
    • Pisoni, R.L.1    Acker, T.L.2    Lisowski, K.M.3    Lemons, R.M.4    Thoene, J.G.5
  • 47
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. 1989. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264:13963
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963
    • Holmgren, A.1
  • 48
    • 0027375166 scopus 로고
    • Major involvement of cathepsin B in the intracellular proteolytic processing of exogenous IgGs in U937 cells
    • Santoro, L., Reboul, A., Journet, A M. and Colomb, M. G. 1993. Major involvement of cathepsin B in the intracellular proteolytic processing of exogenous IgGs in U937 cells. Mol. Immunol. 30 1033
    • (1993) Mol. Immunol. , vol.30 , pp. 1033
    • Santoro, L.1    Reboul, A.2    Journet, A.M.3    Colomb, M.G.4
  • 49
    • 0024362181 scopus 로고
    • Capacity of intact proteins to bind to MHC class II molecules
    • Sette, A., Adorini, L., Colon, S. M., Buus, S and Grey, H. M. 1989. Capacity of intact proteins to bind to MHC class II molecules J. Immunol. 143:1265.
    • (1989) J. Immunol. , vol.143 , pp. 1265
    • Sette, A.1    Adorini, L.2    Colon, S.M.3    Buus, S.4    Grey, H.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.