Mouse complement component C4 is devoid of classical pathway C5 convertase subunit activity

Molecular Immunology

Volumn 33, Issue 3, 1996, Pages 297-309

  Ebanks, Roger O ^a   Isenman, David E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

C5 convertase; Complement; Mouse C4

Indexed keywords

CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C4; RECOMBINANT PROTEIN;

ADULT; ARTICLE; COMPLEMENT ACTIVATION; GUINEA PIG; HUMAN; MOUSE; NONHUMAN; NORMAL HUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

CAVIA PORCELLUS; MAMMALIA; SUS SCROFA;

EID: 0029971956     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/0161-5890(95)00135-2     Document Type: Article

References (51)

1. Alsenz J., Avila D., Huemaer H. P., Esparza L., Hack C. E. and Lambris J. D. (1992) Phylogeny of the third component of complement, C3: analysis of the conservation of human CR1, CR2, H and B binding sites, concanavalin A binding sites and thioester bond in the C3 from different species. Dev. Comp. Immun. 16, 63-76.
2. Anderson M. J., Milner C. M., Cotton R. G. H. and Campbell R. D. (1992) Identification of a single amino acid substitution in the β chain of the hemolytically inactive human complement component C4 allotype C4A6. J. Immun. 148, 2795-2802.
3. Atkinson L. P., McGinnis K. and Shreffler D. (1980) Development and characterization of a hemolytic assay for mouse C4. J. immunol. Meth. 33, 351-368.
4. Borsos T. and Cooper M. (1961) Proc. Soc. exp. biol. Med. 107, 227-232
5. Brown G. C. (1943) The complementary activity of mouse serum. J. Immun. 46, 319-323.
6. Carroll M. C., Fathallah D. M., Bergamaschini L., Alicot E. M. and Isenman D. E. (1990) Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A. Proc. natl. Acad. Sci. U.S.A. 87, 6868-6872.
7. Carroll M. C. and Capra J. D. (1978) Studies on the murine Ss protein: demonstration that the Ss protein is functionally the fourth component of complement. Proc. natl. Acad. Sci. U.S.A. 75, 2424-2428.
8. s), two incompletely processed two-subunit C4 molecules (β-α+γ and β+α-γ), and pro-C4. J. Immun. 132, 1967-1971.
9. Chaplin D. D., Woods D. E., Whitehead A. S., Goldberger G., Colten H. R. and Siedman J. G. (1983) Molecular map of the murine S region. Proc. natl. Acad. Sci. U.S.A. 80, 6947-6951.
10. Cinader B., Dubiski S. and Wardlaw A. C. (1964) Distribution, inheritance and properties of an antigen, MuB1 and its relationship to hemolytic complement. J. exp. Med. 120, 897-994.
11. Cole F. S., Auerbach H. S., Goldberger G. and Colten H. R. (1985) Tissue-specific pretranslational regulation of complement production in human mononuclear phagocytes. J. Immun. 134, 2610-2616.
12. Colten H. R. and Rosen F. S. (1992) Complement deficiencies. A. Rev. Immun. 10, 809-834.
13. Cooper N. R. and Müller-Eberhard H. J. (1968) A comparison of the methods for the molecular quantitation of the fourth component of human complement. Immunochemistry 5, 155-169.
14. Cooper N. R. and Müller-Eberhard H. J. (1970) The reaction mechanism of human C5 in immune hemolysis. J. exp. Med. 132, 775-793.
15. Démant P., Capková J., Hinzová E. and Vorácová B. (1973) The role of the histocompatibility-2-linked Ss-Slp region in the control of mouse complement. Proc. natl. Acad. Sci. U.S.A. 70, 863-864.
16. Dodds A. M., Law S. K. and Porter R. R. (1985) The origin of the very variable haemolytic activities of the common human complement component C4 allotypes including C4-A6. EMBO J. 4, 2239-2244.
17. Ebanks R. O. and Isenman D. E. (1995) Evidence for the involvement of Arginine 462 and the flanking sequence of human C4 β-chain in mediating C5 binding to the C4b sub-component of the classical complement pathway C5 convertase. J. Immun. 154, 2808-2820.
18. Ebanks R. O., Jaikaran A., Carroll M. C., Anderson M. J., Campbell R. D. and Isenman D. E. (1992) A single arginine to tryptophan interchange at β-chain residue 458 of human complement component C4 accounts for the defect in the classical pathway C5 convertase activity of allotype C4A6. Implications for the location of a C5 binding site in C4. J. Immun. 148, 2803-2811.
19. Erickson R. P., Tachibana D. K., Herzenberg L. A. and Rosenberg L. T. (1964) A single gene controlling the hemolytic complement and a serum antigen in the mouse. J. Immun. 92, 611-615.
20. Fearon D. T. (1978) Regulation by membrane sialic acid of β1H-dependent decay-dissociation of amplification C3 convertase of the alternative complement pathway. Proc. natl. Acad. Sci. U.S.A. 75, 1971-1975.
21. Gigli I., Porter R. R. and Sim R. B. (1976) The unactivated form of the first component of human complement, C1. Biochem. J. 157, 541-548.
22. Goldman M. B. and Goldman J. N. (1976) Relationship of the functional levels of early components of complement to the H-2 complex of mice. J. Immun. 117, 1584-1588.
23. Goldman M. B., Bangalore S. and Goldman J. N. (1978a) Functional and biochemical properties of the early classical complement system of mice. J. Immun. 120, 216-224.
24. Goldman J. N., Gleason K. R. and Goldman M. B. (1978b) Immunochemical properties of the murine Ss protein. J. Immun. 120, 225-232.
25. Götze O. and Müller-Eberhard H. J. (1971) The C3 activator system: an alternative pathway of complement activation. J. exp. Med. 134, 90s-108s.
26. Hong K., Kinoshita T., Pramoonjago P., Kim Y. U., Seya T. and Inoue K. (1991) Reconstitution of C5 convertase of the alternative complement pathway with isolated C3b-dimer and factors B and D. J. Immun. 146, 1868-1873.
27. Inouye S. and Inouye M. (1987) Oligonucleotide-directed site-specific mutagenesis using double-stranded plasmid DNA. In Synthesis and Applications of DNA and RNA (Edited by Narang S.), Ch. 8, p. 181. Academic Press, Orlando, FL.
28. Isenman D. E., Sundsmo J. S. and Cooper N. R. (1980) The effects of mild reduction on the structure and function of C3. J. Immun. 125, 1798-1805.
29. Janatova J. and Tack B. F. (1981) Fourth component of human complement: studies of an amine-sensitive site comprised of a thiol component. Biochemistry 20, 2394-2402.
30. Kim Y. U., Carroll M. C., Isenman D. E., Nonaka M., Pramoonjago P., Takeda L., Inoue K. and Kinoshita T. (1992) Covalent binding of C3b to C4b within the classical pathway C5 convertase: determination of the amino acid residues involved in ester linkage formation. J. biol. Chem. 267, 4171-4176.
31. Kinoshita T., Dodds A. W., Law S. K. A. and Inoue K. (1989) The low C5 convertase activity of the C4A6 allotype of human complement C4. Biochem. J. 261, 743-748.
32. Kinoshita T., Takata Y., Kozono H., Takeda L, Hong K. and Inoue K. (1988) C5 convertase of the alternative complement pathway: covalent linkage between C3b molecules within the trimolecular complex enzyme. J. Immun. 141, 3895-3901.
33. Kozono H., Kinoshita T., Kim Y. U., Takata-Kozono Y., Tsunasawa S., Sakiyama R, Takeda J., Hong K. and Inoue K. (1990) Localization of the covalent C3b-binding site on C4b within the complement classical pathway C5 convertase. C4b2a3b. J. biol. Chem. 265, 14,444-14,449.
34. Lesavre P. H., Hugli T. E., Esser A. F. and Müller-Eberhard H. J. (1979) The alternative pathway C3/C5 convertase: chemical basis of factor B activation. J. Immun. 123, 529-534.
35. Marchalonis J. J. (1969) An enzymatic method for trace iodination of immunoglobulins and other proteins. Biochem. J. 113, 299-305.
36. McGhee R. B. (1952) Presence of complement in serum of the mouse. Proc. Soc. exp. biol. Med. 80, 419-420.
37. McLean R. H., Niblack G., Julian B., Wang T., Wyatt R., Phillips III J. A., Collins T. S., Winkelstein J. and Valle D. (1994) Hemolytically inactive C4B complement allotype caused by a proline to leucine mutation in the C5-binding site. J. biol. Chem. 269, 27727-27731.
38. Nagasawa S. and Stroud R. M. (1977) Cleavage of C2 by C1s̄ into antigenically distinct fragments C2a and C2b. Demonstration of binding of C2b to C4b. Proc. natl. Acad. Sci. U.S.A. 74, 2981-3001.
39. Nakayama K., Pattanakitsakul S., Yokoyama S., Kimura H., Nonaka M. and Takahashi M. (1990) Post-transcriptional regulation of complement C4 in low C4-producing strain of mouse. Immunogenetics 31, 361-367.
40. Nilsson U. R. and Müller-Eberhard H. J. (1967) Deficiency of the fifth component of complement in mice with an inherited complement defect. J. exp. Med. 126, 1-16.
41. Ogata R. T. and Sepich D. S. (1984) Genes for murine fourth complement component (C4) and sex-limited protein (Slp) identified by hybridization to C4-and Slp-specific cDNA. Proc. natl. Acad. Sci. U.S.A. 81, 4908-4911.
42. Ogata R. T., Shreffler D. C., Sepich D. S. and Lilly S. P. (1983) eDNA clone spanning the α-γ subunit junction of the precursor of the murine fourth complement component (C4). Proc. natl. Acad. Sci. U.S.A. 80, 5061-5065.
43. Ong G. L. and Mattes M. J. (1989) Mouse strains with typical mammalian levels of complement activity. J. immunol. Meth. 125, 147-158.
44. Pangburn M. K. and Müller-Eberhard H. J. (1978) Complement C3 convertase: cell surface restriction of β1H control and generation of restriction on neuraminidase-treated cells. Proc. natl. Acad. Sci. U.S.A. 75, 2416-2420.
45. k mice. J. biol. Chem. 267, 7814-7820.
46. gp and functionally pure human second component. J. Immun. 99, 1162-1172.
47. Sepich D. S., Noonan D. J. and Ogata R. T. (1985) Complete cDNA sequence of the fourth component of murine complement. Proc. natl. Acad. Sci. U.S.A. 82, 5895-5899.
48. Tack B. F., Janatova J., Thomas M. L., Harrison R. A. and Hammer C. H. (1981) The third, fourth and fifth components of human complement: isolation and biochemical properties. Meth. Enzymol. 80, 64-101.
49. Takata Y., Kinoshita T., Kozono H., Takeda L., Tanaka E., Hong K. and Inoue K. (1987) Covalent association of C3b with C4b within C5 convertase of the classical complement pathway. J. exp. Med. 165, 1494-1507.
50. Taniguchi-Sidle A. and Isenman D. E. (1992) Mutagenesis of the arg-gly-asp triplet in human complement component C3 does not abolish binding of iC3b to the leukocyte integrin complement receptor type III (CR3, CD11b/CD18). J. biol. Chem. 267, 635-643.
51. von Zabern E., Nolte R. and Vogt W. (1979) Incompatibility between complement components C3 and C5 of guinea pig and man, an indication of their interaction in C5 activation by classical and alternative C5 convertases. Scand. J. Immun. 9, 69-74.