The effect of acute phase proteins on clearance of chromatin from the circulation of normal mice

Journal of Immunology

Volumn 156, Issue 12, 1996, Pages 4783-4788

  Burlingame, Rufus W ^a   Volzer, Michael A ^a   Harris, James ^b   Du Clos, Terry W ^a  

^a VA Medical Center   (United States)

^b UNIVERSITY OF NEW MEXICO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

C REACTIVE PROTEIN; CASEIN;

ANIMAL EXPERIMENT; ANTIGEN ANTIBODY COMPLEX; ARTICLE; AUTOIMMUNITY; CHROMATIN; FEMALE; LIVER CLEARANCE; MALE; MOUSE; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN SECRETION; SYSTEMIC LUPUS ERYTHEMATOSUS;

ACUTE-PHASE PROTEINS; ACUTE-PHASE REACTION; ANIMALS; C-REACTIVE PROTEIN; CHROMATIN; COMPLEMENT SYSTEM PROTEINS; FEMALE; MALE; METABOLIC CLEARANCE RATE; MICE; MICE, INBRED BALB C; MICE, INBRED C57BL; SERUM AMYLOID P-COMPONENT;

EID: 0029945786     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (44)

1. Tan, E. M., A. S. Cohen, J. F. Fries, A. T. Masi, D. J. McShane, N. F. Rothfield, J. G. Schaller, N. Talal, and R. J. Winchester. 1982. The 1982 revised criteria for the classification of systemic lupus erythematosus. Arthritis Rheum. 25:1271.
2. Burlingame, R. W., R. L. Rubin, R. S. Balderas, and A. N. Theofilopoulos. 1993. Genesis and evolution of antichromatin autoantibodies in murine lupus implicates T-dependent immunization with self antigen. J. Clin. Invest. 91:1687.
3. Stockl, F., S. Muller, S. Batsford, T. Schmiedeke, R. Waldherr, K. Andrassy, Y. Sugisaki, K. Nakabayashi, T. Nagasawa, and B. Rodriguez-Iturbe. 1994. A role for histones and ubiquitin in lupus nephritis. Clin. Nephrol. 41:10.
4. Burlingame, R. W., M. L. Boey, G. Starkebaum, and R. L. Rubin. 1994. The central role of chromatin in autoimmune responses to histones and DNA in systemic lupus erythematosus. J. Clin. Invest. 94:184.
5. Tsumita, T., and M. Iwanaga. 1963. Fate of injected deoxyribonucleic acid in mice. Nature 198:1088.
6. Chused, T. M., A. D. Steinberg, and N. Talal. 1972. The clearance and localization of nucleic acids by New Zealand and normal mice. Clin. Exp. Immunol. 12:465.
7. Emlen, W., and M. Mannik. 1978. Kinetics and mechanisms for removal of circulating single-stranded DNA in mice. J. Exp. Med. 147:684.
8. Emlen, W., and M. Mannik. 1982. Clearance of circulating DNA-anti-DNA immune complexes in mice. J. Exp. Med. 155:1210.
9. Emlen, W., and M. Mannik. 1980. Effect of preformed immune complexes on the clearance and tissue localization of single-stranded DNA in mice. Clin. Exp. Immunol. 40:264.
10. Emlen, W., and M. Mannik. 1984. Effect of DNA size and strandedness on the in vivo clearance and organ localization of DNA. Clin. Exp. Immunol. 56:185.
11. Osmand, A. P., B. Friedenson, H. Gewurz, R. H. Painter, T. Hofmann, and E. Shelton. 1977. Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins). Proc. Natl. Acad. Sci. USA 74:739.
12. Pepys, M. B., and P. J. G. Butler. 1987. Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum. Biochem. Biophys. Res. Commun. 148:308.
13. Du Clos, T. W. 1989. C-reactive protein reacts with the U1 small nuclear ribonucleoprotein. J. Immunol. 143:2553.
14. Robey, F. A., K. D. Jones, T. Tanaka, and T-Y. Liu. 1984. Binding of C-reactive protein to chromatin and nucleosome core particles: a possible physiological role of C-reactive protein. J. Biol. Chem. 259:7311.
15. Du Clos, T. W., L. T. Zlock, and R. L. Rubin. 1988. Analysis of the binding of C-reactive protein to histones and chromatin. J. Immunol. 141:4266.
16. Pepys, M. B., M. L. Baltz, K. Gomer, J. S. Davis, and M. Doenhoff. 1979. Serum amyloid P component is an acute phase reactant in mouse. Nature 278:259.
17. Pepys, M. B., A. C. Dash, R. E. Markham, H. C. Thomas, B. D. Williams, and A. Petrie. 1978. Comparative clinical study of protein SAP (amyloid P component) and C-reactive protein in serum. Clin. Exp. Immunol. 32:119.
18. Nelson, S. R., G. A. Tennent, D. Sethi, P. E. Gower, F. W. Ballardie, S. Amatayakul-Chantler, and M. B. Pepys. 1991. Serum amyloid P component in chronic renal failure and dialysis. Clin. Chim. Acta 200:191.
19. Siboo, R., and E. Kulisek. 1978. A fluorescent immunoassay for quantification of C-reactive protein. J. Immunol. Methods 23:59.
20. Pepys, M. B., J. G. Lanham, and F. C. De Beer. 1982. C-reactive protein in SLE. Clin. Rheum. Dis. 8:91.
21. Nakayama, S., C. Mold, H. Gewurz, and T. W. Du Clos. 1982. Opsonic properties of C-reactive protein in vivo. J. Immunol. 128:2435.
22. Nakayama, S., H. Gewurz, T. J. Holzer, T. W. Du Clos, and C. Mold. 1983. The role of the spleen in the protective effect of C-reactive protein in Streptococcus pneumoniae infection. Clin. Exp. Immunol. 54:319.
23. Mold, C., S. Nakayama, T. J. Holzer, H. Gewurz, and T. W. Du Clos. 1981. C-reactive protein is protective against Streptococcus pneumoniae infection in mice. J. Exp. Med. 154:1703.
24. Nakayama, S., T. W. Du Clos, H. Gewurz, and C. Mold. 1984. Inhibition of antibody responses to phosphocholine by C-reactive protein. J. Immunol. 132: 1336.
25. Breathnach, S. M., H. Kofler, N. Sepp, J. Ashworth, D. Woodrow, M. B. Pepys, and H. Hintner. 1989. Serum amyloid P component binds to cell nuclei in vitro and in vivo deposits of extracellular chromatin in systemic lupus erythematosus. J. Exp. Med 170:1433.
26. 1 mice treated with C-reactive protein. Clin. Immunol. Immunopathol. 70:22.
27. Lutter, O. C. 1978. Kinetic analysis of deoxyribonuclease I cleavage in the nucleosome core: evidence for a DNA superhelix. J. Mol. Biol. 124:391.
28. Godfrey, J. E., A. D. Baxevanis, and E. N. Moudrianakis. 1990. Spectropolarimetric analysis of the core histone octamer and its subunits. Biochemistry 29:965.
29. Wells, D., and C. McBride. 1989. A comprehensive compilation and alignment of histones and histone genes. Nucleic Acids Res. [Suppl.] 17:311.
30. Rubin, R. L. 1986. Enzyme-linked immunosorbent assay for anti-DNA and antihistone antibodies. In Manual of Clinical Laboratory Immunology. N. R. Rose, H. Friedman, and J. L. Fahey, eds. American Society for Microbiology, Washington, pp. 744-749.
31. David, G. S., and R. A. Reisfeld. 1974. Protein iodination with solid state lactoperoxidase. Biochemistry 13:1014.
32. Du Clos, T. W., L. Zlock, and L. L. Marnell. 1991. Definition of a C-reactive protein binding determinant on histones. J. Biol. Chem. 266:2167.
33. Hicks, P. S., L. Saunero-Nava, T. W. Du Clos, and C. Mold. 1992. Serum amyloid P component binds to histones and activates the classical complement pathway. J. Immunol. 149:3689.
34. Miller, G. W., and V. Nussenzweig. 1974. Complement as a regulator of interaction between immune complexes and cell membranes. J. Immunol. 113:464.
35. Duvall, E., and A. H. Wylie. 1986. Death and the cell. Immunol. Today 7:115.
36. Fournie, G. J. 1988. Circulating DNA and lupus nephritis. Kidney Int. 33:487.
37. McCoubrey-Hoyer, A., T. B. Okarma, and H. R. Holman. 1984. Partial purification and characterization of plasma DNA and its relation to disease activity in systemic lupus erythematosus. Am. J. Med. 77:23.
38. Hutchinson, W. L., G. E. Noble, P. N. Hawkins, and M. B. Pepys. 1994. The pentraxins, C-reactive protein and serum amyloid P component, are cleared and catabolized by hepatocytes in vivo. J. Clin. Invest. 94:1390.
39. Robey, F. A., K. D. Jones, and A. D. Steinberg. 1985. C-reactive protein mediates the solubilization of nuclear DNA by complement in vitro. J. Exp. Med. 161: 1344.
40. Butler, P. J. G., G. A. Tennent, and M. B. Pepys. 1990. Pentraxin-chromatin interactions: serum amyloid P component specifically displaces H1-type histones and solubilizes native long chromatin. J. Exp. Med. 172:13.
41. Schmiedeke, T. M. J., F. W. Stockl, and R. Weber. 1989. Histones have high affinity for the glomerular basement membrane. J. Exp. Med. 169:1879.
42. Gauthier, V. J., M. Mannik, and G. E. Striker. 1982. Effect of cationized antibodies in preformed immune complexes on deposition and persistence in renal glomeruli. J. Exp. Med. 156:766.
43. Pepys, M. B., and S. L. Rogers. 1980. Complement-independence of the acute phase production of serum amyloid P-component (SAP) in mice. Br. J. Exp. Pathol. 61:156.
44. Gauthier, V. J., L. N. Tyler, and M. Mannik. 1996. Blood clearance kinetics and liver uptake of mononucleosomes in mice. J. Immunol. 156:1151.