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Volumn 5, Issue 3, 1996, Pages 197-207

Natural Catalytic Antibodies

Author keywords

Antibody engineering; Autoimmune disease; Catalytic antibodies; Enzyme evolution; Monoclonal antibodies; Multiple myeloma; Thyroglobulin; VH domain; VL domain; VIP

Indexed keywords

ANTIGEN; CATALYTIC ANTIBODY;

EID: 0030157640     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02900358     Document Type: Review
Times cited : (42)

References (49)
  • 1
    • 0024382917 scopus 로고
    • Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody
    • Paul, S., Volle, D. J., Beach, C. M., Johnson, D. R., Powell, M. J., and Massey, R. J. (1989) Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody. Science 244, 1158-1162.
    • (1989) Science , vol.244 , pp. 1158-1162
    • Paul, S.1    Volle, D.J.2    Beach, C.M.3    Johnson, D.R.4    Powell, M.J.5    Massey, R.J.6
  • 2
    • 0026042026 scopus 로고
    • Cleavage of vasoactive intestinal peptide at multiple sites by autoantibodies
    • Paul, S., Sun, M., Mody, R., Eklund, S. H., Beach, C. M., Massey, R. J., and Hamel, F. (1991) Cleavage of vasoactive intestinal peptide at multiple sites by autoantibodies. J. Biol. Chem. 266, 16,128-16,134.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16128-16134
    • Paul, S.1    Sun, M.2    Mody, R.3    Eklund, S.H.4    Beach, C.M.5    Massey, R.J.6    Hamel, F.7
  • 3
    • 0000951071 scopus 로고
    • Human autoantibodies that catalyze the hydrolysis of vasoactive intestinal polypeptide
    • Suzuki, H., Imanishi, H., Nakai, T., and Konishi, Y. K. (1992) Human autoantibodies that catalyze the hydrolysis of vasoactive intestinal polypeptide. Biochem. (Life Sci. Adv.) 11, 173-177.
    • (1992) Biochem. (Life Sci. Adv.) , vol.11 , pp. 173-177
    • Suzuki, H.1    Imanishi, H.2    Nakai, T.3    Konishi, Y.K.4
  • 7
    • 0028435833 scopus 로고
    • Catalytic activity of anti-ground state antibodies, antibody subunits and human autoantibodies
    • Paul, S. (1994) Catalytic activity of anti-ground state antibodies, antibody subunits and human autoantibodies. Appl. Biochem. Biotechnol. 47, 241-255.
    • (1994) Appl. Biochem. Biotechnol. , vol.47 , pp. 241-255
    • Paul, S.1
  • 8
    • 0010982153 scopus 로고
    • Chemical reactivity at an antibody binding site elicited by mechanistic design of a synthetic antigen
    • Tramontano, A., Janda, K. D., and Lerner, R. A. (1986) Chemical reactivity at an antibody binding site elicited by mechanistic design of a synthetic antigen. Proc. Natl. Acad. Sci. USA 83, 6736-6740.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6736-6740
    • Tramontano, A.1    Janda, K.D.2    Lerner, R.A.3
  • 9
    • 0025730616 scopus 로고
    • At the crossroads of chemistry and immunology: Catalytic antibodies
    • Lerner, R. A., Benkovic, S. J., and Schultz, P. G. (1991) At the crossroads of chemistry and immunology: catalytic antibodies. Science 252, 659-667.
    • (1991) Science , vol.252 , pp. 659-667
    • Lerner, R.A.1    Benkovic, S.J.2    Schultz, P.G.3
  • 10
    • 0027489204 scopus 로고
    • Monoclonal anti-idiotypic antibodies as functional internal images of enzymes active sites: Production of a catalytic antibody with a cholinesterase activity
    • Izadyar, L., Friboulet, A., Remy, M. H., Roseto, A., and Thomas, D. (1993) Monoclonal anti-idiotypic antibodies as functional internal images of enzymes active sites: production of a catalytic antibody with a cholinesterase activity. Proc. Natl. Acad. Sci. USA 90, 8876-8880.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8876-8880
    • Izadyar, L.1    Friboulet, A.2    Remy, M.H.3    Roseto, A.4    Thomas, D.5
  • 11
    • 0028134956 scopus 로고
    • Un abzyme DNase polyclonal produit par la methode de image interne anti-idiotypique
    • Crespeau, H., Laouar, A., and Rochu, D. (1994) Un abzyme DNase polyclonal produit par la methode de image interne anti-idiotypique. C. R. Acad. Sci. Paris de la vie/Life Sci. 317, 819-823.
    • (1994) C. R. Acad. Sci. Paris de la Vie/Life Sci. , vol.317 , pp. 819-823
    • Crespeau, H.1    Laouar, A.2    Rochu, D.3
  • 12
    • 1842617723 scopus 로고
    • Hypotheses about mechanism of action of antimetabolites
    • Wiley, New York
    • Woolley, D. W. (1952) Hypotheses about mechanism of action of antimetabolites, A Study of Antimetabolites, Wiley, New York, p. 82.
    • (1952) A Study of Antimetabolites , pp. 82
    • Woolley, D.W.1
  • 13
    • 0016311758 scopus 로고
    • Do immunoglobulins have proteolytic activity?
    • Erhan, S. and Greller, L. D. (1974) Do immunoglobulins have proteolytic activity? Nature 251, 353-355.
    • (1974) Nature , vol.251 , pp. 353-355
    • Erhan, S.1    Greller, L.D.2
  • 15
    • 0019154676 scopus 로고
    • Monoclonal immunoglobulin G augments hydrolysis of an ester of the homologous hapten
    • Kohen, F., Kim, J. B., Linder, H. R., Eshhar, Z., and Green, B. (1980) Monoclonal immunoglobulin G augments hydrolysis of an ester of the homologous hapten. FEBS Lett. 111, 427-431.
    • (1980) FEBS Lett. , vol.111 , pp. 427-431
    • Kohen, F.1    Kim, J.B.2    Linder, H.R.3    Eshhar, Z.4    Green, B.5
  • 17
    • 0028435991 scopus 로고
    • Hapten design for the generation of catalytic antibodies
    • Thomas, N. (1994) Hapten design for the generation of catalytic antibodies. Appl. Biochem. Biotechnol 47, 345-373.
    • (1994) Appl. Biochem. Biotechnol , vol.47 , pp. 345-373
    • Thomas, N.1
  • 18
    • 0024362047 scopus 로고
    • The role of somatic hypermutation in the generation of antibody diversity
    • French, D. L., Laskow, R., and Scharff, M. D. (1989) The role of somatic hypermutation in the generation of antibody diversity. Science 244, 1152-1157.
    • (1989) Science , vol.244 , pp. 1152-1157
    • French, D.L.1    Laskow, R.2    Scharff, M.D.3
  • 19
    • 0015956495 scopus 로고
    • Towards a network theory of the immune system
    • Jerne, N. K. (1974) Towards a network theory of the immune system. Ann. Immunol. (Inst. Pasteur) 125C, 373-389.
    • (1974) Ann. Immunol. (Inst. Pasteur) , vol.125 C , pp. 373-389
    • Jerne, N.K.1
  • 21
    • 0001047001 scopus 로고
    • The subunits of purified rabbit antibody
    • Utsumi, S. and Karush, F. (1964) The subunits of purified rabbit antibody. Biochemistry 9, 1329-1342.
    • (1964) Biochemistry , vol.9 , pp. 1329-1342
    • Utsumi, S.1    Karush, F.2
  • 22
    • 0040680982 scopus 로고
    • Reconstitution of immunologic activity by interaction of polypeptide chains of antibodies
    • Edelman, G. M., Olins, D. E., Gaily, J. A., and Zinder, N. D. (1963) Reconstitution of immunologic activity by interaction of polypeptide chains of antibodies. Proc. Natl. Acad. Sci. USA 50, 753-761.
    • (1963) Proc. Natl. Acad. Sci. USA , vol.50 , pp. 753-761
    • Edelman, G.M.1    Olins, D.E.2    Gaily, J.A.3    Zinder, N.D.4
  • 23
    • 0028154125 scopus 로고
    • Antigen recognition by an antibody light chain
    • Sun, M., Li, L., Gao, Q. S., and Paul, S. (1994) Antigen recognition by an antibody light chain. J. Biol. Chem. 269, 734-738.
    • (1994) J. Biol. Chem. , vol.269 , pp. 734-738
    • Sun, M.1    Li, L.2    Gao, Q.S.3    Paul, S.4
  • 24
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted for Escherichia coli
    • Ward, E. S., Gussow, D., Griffiths, A. D., Jones, P. T., and Winter, G. (1989) Binding activities of a repertoire of single immunoglobulin variable domains secreted for Escherichia coli. Nature 341, 544-546.
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Gussow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 27
    • 0026040192 scopus 로고
    • Vasoactive intestinal peptide hydrolysis by antibody light chains
    • Sun, M., Mody, B., Eklund, S. H., and Paul, S. (1991) Vasoactive intestinal peptide hydrolysis by antibody light chains. J. Biol. Chem. 266, 15,571-15,574.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15571-15574
    • Sun, M.1    Mody, B.2    Eklund, S.H.3    Paul, S.4
  • 28
    • 0028127014 scopus 로고
    • Proteolytic activity of an antibody light chain
    • Sun, M., Gao, Q.-S., Li, L., and Paul, S. (1994) Proteolytic activity of an antibody light chain. J. Immunol. 153, 5121-5126.
    • (1994) J. Immunol. , vol.153 , pp. 5121-5126
    • Sun, M.1    Gao, Q.-S.2    Li, L.3    Paul, S.4
  • 30
    • 0025835310 scopus 로고
    • Making antibody fragments using phage display libraries
    • Clackson, T., Hoogenboom, H. R., Griffiths, A. D., and Winter, G. (1991) Making antibody fragments using phage display libraries. Nature 352, 624-628.
    • (1991) Nature , vol.352 , pp. 624-628
    • Clackson, T.1    Hoogenboom, H.R.2    Griffiths, A.D.3    Winter, G.4
  • 31
    • 0028435990 scopus 로고
    • Selection of functional human immunoglobulin light chains from a phage display library
    • Tyutyulkova, S. and Paul, S. (1994) Selection of functional human immunoglobulin light chains from a phage display library. Appl. Biochem. Biotechnol. 47, 191-198.
    • (1994) Appl. Biochem. Biotechnol. , vol.47 , pp. 191-198
    • Tyutyulkova, S.1    Paul, S.2
  • 32
    • 0029173723 scopus 로고
    • Selection of human immunoglobulin light chains from a phage display library
    • (Paul, S., ed.), Humana, Totowa, NJ
    • Tyutyulkova, S., Gao, Q.-S. and Paul, S. (1995) Selection of human immunoglobulin light chains from a phage display library, in Methods in Molecular Biology, vol. 51: Antibody Engineering Protocols (Paul, S., ed.), Humana, Totowa, NJ, pp. 15,377-15,394.
    • (1995) Methods in Molecular Biology, Vol. 51: Antibody Engineering Protocols , vol.51 , pp. 15377-15394
    • Tyutyulkova, S.1    Gao, Q.-S.2    Paul, S.3
  • 33
    • 0028835286 scopus 로고
    • Site-directed mutagenesis of proteolytic antibody light chain
    • Gao, Q. S., Sun, M., Rees, A., and Paul, S. (1995) Site-directed mutagenesis of proteolytic antibody light chain. J. Mol. Biol. 253, 658-664.
    • (1995) J. Mol. Biol. , vol.253 , pp. 658-664
    • Gao, Q.S.1    Sun, M.2    Rees, A.3    Paul, S.4
  • 34
    • 0025345903 scopus 로고
    • Site specificity of a catalytic vasoactive intestinal peptide antibody: An inhibitory vasoactive intestinal peptide subsequence distant from the scissile peptide bond
    • Paul, S., Voile, D. J., Powell, M. J., and Massey, R. J. (1990) Site specificity of a catalytic vasoactive intestinal peptide antibody: an inhibitory vasoactive intestinal peptide subsequence distant from the scissile peptide bond. J. Biol. Chem. 265, 11,910-11,913.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11910-11913
    • Paul, S.1    Voile, D.J.2    Powell, M.J.3    Massey, R.J.4
  • 35
    • 0029198369 scopus 로고
    • Molecular cloning of anti-ground state proteolytic antibody fragments
    • (Paul, S., ed.), Humana, Totowa, NJ
    • Gao, Q.-S. and Paul, S. (1995) Molecular cloning of anti-ground state proteolytic antibody fragments, in Methods in Molecular Biology, vol. 51: Antibody Engineering Protocols (Paul, S., ed.), Humana, Totowa, NJ, pp. 281-296.
    • (1995) Methods in Molecular Biology, Vol. 51: Antibody Engineering Protocols , vol.51 , pp. 281-296
    • Gao, Q.-S.1    Paul, S.2
  • 36
    • 0024535462 scopus 로고
    • Solution structure of an analogue of vasoactive intestinal peptide as determined by two-dimensional NMR and circular dichroism spectroscopies and constrained molecular dynamics
    • Fry, D. C., Madison, V. S., Bolin, D. R., Greeley, D. N., Toome, V., and Wegrzynski, B. B. (1989) Solution structure of an analogue of vasoactive intestinal peptide as determined by two-dimensional NMR and circular dichroism spectroscopies and constrained molecular dynamics. Biochemistry 28, 2399-2409.
    • (1989) Biochemistry , vol.28 , pp. 2399-2409
    • Fry, D.C.1    Madison, V.S.2    Bolin, D.R.3    Greeley, D.N.4    Toome, V.5    Wegrzynski, B.B.6
  • 37
    • 0022355018 scopus 로고
    • Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431-base complementary DNA
    • Meroken, L., Simons, M. J., Swillens, S., Massaer, M., and Vassart, G. (1985) Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431-base complementary DNA. Nature 316, 647-651.
    • (1985) Nature , vol.316 , pp. 647-651
    • Meroken, L.1    Simons, M.J.2    Swillens, S.3    Massaer, M.4    Vassart, G.5
  • 38
    • 0025101232 scopus 로고
    • Peptidase modulation of the pulmonary effects of tachykinins in tracheal superfused guinea pig lungs
    • Martins, M. A., Shore, S. A., Gerard, N. P., Gerard, C., and Drazen, J. M. (1990) Peptidase modulation of the pulmonary effects of tachykinins in tracheal superfused guinea pig lungs. J. Clin. Invest. 85, 170-176.
    • (1990) J. Clin. Invest. , vol.85 , pp. 170-176
    • Martins, M.A.1    Shore, S.A.2    Gerard, N.P.3    Gerard, C.4    Drazen, J.M.5
  • 39
    • 0024375861 scopus 로고
    • Substrate specificity and affinity of a protein modulated by bound water molecules
    • Quiocho, F. A., Wilson, D. K., and Vyas, N. K. (1989) Substrate specificity and affinity of a protein modulated by bound water molecules. Nature 340, 404-407.
    • (1989) Nature , vol.340 , pp. 404-407
    • Quiocho, F.A.1    Wilson, D.K.2    Vyas, N.K.3
  • 40
    • 0023176519 scopus 로고
    • Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding picket of trypsin
    • Graf, L., Craik, C. S., Patthy, A., Roczniak, S., Fletterick, R. J., and Rutter, W. J. (1987) Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding picket of trypsin. Biochemistry 26, 2616-2623.
    • (1987) Biochemistry , vol.26 , pp. 2616-2623
    • Graf, L.1    Craik, C.S.2    Patthy, A.3    Roczniak, S.4    Fletterick, R.J.5    Rutter, W.J.6
  • 42
    • 0022445901 scopus 로고
    • Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering
    • Estell, D. A., Graycar, T. P., Miller, J. V., Powers, D. B., Burnier, J. P., Ng, P. G., and Wells, J. A. (1986) Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering. Science 233, 659-663.
    • (1986) Science , vol.233 , pp. 659-663
    • Estell, D.A.1    Graycar, T.P.2    Miller, J.V.3    Powers, D.B.4    Burnier, J.P.5    Ng, P.G.6    Wells, J.A.7
  • 43
    • 0001463338 scopus 로고
    • Designing substrate specificity by protein engineering of electrostatic interactions
    • Wells, J. A., Powers, D. B., Bott, R. R., Graycar, T. P., and Estell, D. A. (1987) Designing substrate specificity by protein engineering of electrostatic interactions. Proc. Natl. Acad. Sci. USA 84, 1219-1223.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1219-1223
    • Wells, J.A.1    Powers, D.B.2    Bott, R.R.3    Graycar, T.P.4    Estell, D.A.5
  • 46
    • 0028910170 scopus 로고
    • Unexpectedly high occurrence of catalytic antibodies in MRL/lpr and SJL mice immunized with a transition state analog. Is there a linkage to autoimmunity?
    • Tawfik, D., Chap, R., Green, B., Sela, M., and Eshhar, Z. (1995) Unexpectedly high occurrence of catalytic antibodies in MRL/lpr and SJL mice immunized with a transition state analog. Is there a linkage to autoimmunity? Proc. Natl. Acad. Sci. USA 92, 2145-2149.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2145-2149
    • Tawfik, D.1    Chap, R.2    Green, B.3    Sela, M.4    Eshhar, Z.5
  • 47
    • 0024598564 scopus 로고
    • Absence of immunoreactive vasoactive intestinal polypeptide in tissue from the lungs of patients with asthma
    • Ollerenshaw, S., Jarvis, D., Woolcock, A., Sullivan, C., and Scheibner, T. (1989) Absence of immunoreactive vasoactive intestinal polypeptide in tissue from the lungs of patients with asthma. N. Engl. J. Med. 320, 1244-1248.
    • (1989) N. Engl. J. Med. , vol.320 , pp. 1244-1248
    • Ollerenshaw, S.1    Jarvis, D.2    Woolcock, A.3    Sullivan, C.4    Scheibner, T.5


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