Chimeric human-mouse IgG antibodies with shuffled constant region exons demonstrate that multiple domains contribute to in vivo half-life

Cancer Research

Volumn 58, Issue 17, 1998, Pages 3905-3908

  Zuckier, Lionel S ^a   Chang, Chee J ^a   Scharff, Matthew D ^a   Morrison, Sherie L ^b  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC ANTIBODY; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2; IMMUNOGLOBULIN G3; IMMUNOGLOBULIN G4;

AMINO TERMINAL SEQUENCE; ARTICLE; CANCER IMMUNOTHERAPY; CONTROLLED STUDY; DRUG CLEARANCE; DRUG HALF LIFE; IMMUNOGLOBULIN STRUCTURE; INTRAVENOUS DRUG ADMINISTRATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN;

ANIMALS; EXONS; HALF-LIFE; HUMANS; IMMUNOGLOBULIN CONSTANT REGIONS; IMMUNOGLOBULIN G; METABOLIC CLEARANCE RATE; MICE; MICE, SCID; RECOMBINANT FUSION PROTEINS;

EID: 0032170063     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (25)

1. Zuckier, L. S., and DeNardo, G. L. Trials and tribulations: oncological antibody imaging comes to the fore. Semin. Nucl. Med., 27: 10-29, 1997.
2. F-D-C Reports, Inc. The NDA pipeline-1996. Chevy Chase, MD: F-D-C Reports, Inc., 1997.
3. Hand, P. H., Kashmiri, S. V. S., and Schlom, J. Potential for recombinant immunoglobulin constructs in the management of carcinoma. Cancer (Phila.), 73 (Suppl. 3): 1105-1113, 1994.
4. Morrison, S. L., Johnson, M. J., Herzenberg, L. A., and Oi, V. T. Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc. Natl. Acad. Sci. USA, 81: 6851-6855, 1984.
5. Winter, G., and Milstein, C. Man-made antibodies. Nature (Lond.), 349: 293-299, 1991.
6. Wright, A., Shin, S-U., and Morrison, S. L. Genetically engineered antibodies: progress and prospects. Crit. Rev. Immunol., 12: 125-168, 1992.
7. Kim, J-K., Tsen, M-F., Ghetie, V., and Ward, E. S. Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis. Eur. J. Immunol., 24: 542-548, 1994.
8. Kim, J. K., Tsen, M. F., Ghetie, V., and Ward, E. S. Catabolism of the murine IgG1 molecule: evidence that both CH2-CH3 domain interfaces are required for persistence of IgG1 in the circulation of mice. Scand. J. Immunol., 40: 457-465, 1994.
9. Junghans, R. P. Finally. The Brambell receptor (FcRB). Mediator of transmission of immunity and protection from catabolism for IgG. Immunol. Res., 16: 29-57, 1997.
10. Zuckier, L. S., Georgescu, L., Chang, C. J., Scharff, M. D., and Morrison, S. L. The use of severe combined immunodeficiency mice to study the metabolism of human immunoglobulin G. Cancer (Phila.), 73 (Suppl. 3): 794-799, 1994.
11. Bosma, G. C., Custer, R. P., and Bosma, M. J. A severe combined immunodeficiency mutation in the mouse. Nature (Lond.), 301: 527-530, 1983.
12. Zuckier, L. S., Rodriguez, L. D., and Scharff, M. D. Immunologic and pharmacologic concepts of monoclonal antibodies. Semin. Nucl. Med., 19: 166-186, 1989.
13. Waldmann, T. A., and Strober, W. Metabolism of immunoglobulins. Prog. Allergy, 13: 1-110, 1969.
14. H2 domain and is modulated by the hinge region. J. Exp. Med., 173: 1483-1491, 1991.
15. H2 domain. J. Exp. Med., 173: 1025-1028, 1991.
16. Fraker, P. J., and Speck, J. C., Jr. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycoluril. Biochem. Biophys. Res. Commun., 80: 849-857, 1978.
17. Ghetie, V., Hubbard, J. G., Kim, T. K., Tsen, M. F., Lee, Y., and Ward, E. S. Abnormally short serum half-lives of IgG in β-2-microglobulin-deficient mice. Eur. J. Immunol., 26: 690-696, 1996.
18. Junghans, R. P., and Andersen, C. L. The protection receptor for IgG catabolism is the β2-microglobulin-containing neonatal intestinal transport receptor. Proc. Natl. Acad. Sci. USA, 93: 5512-5516, 1996.
19. Israel, E. J., Wilsker, D. F., Hayes, K. C., Schoenfeld, D., and Simister, N. E. Increased clearance of IgG in mice that lack β2-microglobulin: possible protective role of FcRn. Immunology, 89: 573-578, 1996.
20. Brambell, F. W. R., Hemmings, W. A., and Morris, I. G. A theoretical model of τ-globulin catabolism. Nature (Lond.), 203: 1352-1355, 1964.
21. Brambell, F. W. R. The transmission of immunity from mother to young and the catabolism of immunoglobulins. Lancet, 2: 1087-1093, 1966.
22. Duncan, A. R., Woof, J. M., Partridge, L. J., Burton, D. R., and Winter, G. Localization of the binding site for the human high-affinity Fc receptor on IgG. Nature (Lond.), 332: 563-564, 1988.
23. Pollock, R. R., French, D. L., Metlay, J. P., Birshtein, B. K., and Scharff, M. D. Intravascular metabolism of normal and mutant mouse immunoglobulin molecules. Eur. J. Immunol., 20: 2021-2027, 1990.
24. Bazin, R., Boucher, G., Monier, G., Chevrier, M-C., Verrette, S., Broly, H., and Lemieux, R. Use of hu-IgG-SCID mice to evaluate the in vivo stability of human monoclonal IgG antibodies. J. Immunol. Methods, 172: 209-217, 1994.
25. 3 in scid mice. Eur. J. Immunol., 21: 1319-1322, 1991.