Activation of Mammalian Complement by Chicken C1q

  • Else Marie Nicolaisen


Activation of chicken complement by the classical pathway is still debatable. Both positive and negative evidence of antibody dependent lysis has been reported. The components from C3 to C9 function since activation via the alternative pathway will lyse mammalian erythrocytes in the absence of Ig. Actually the discrepancy in the literature concerning classical activation might be explained by the fact that heterologous erythrocytes were used in most studies. On the other hand, absence of lysis of chicken erythrocytes coated with specific chicken antibodies might be due to the strong anti-complementary effect ascribed to chicken serum.


Human Complement Chicken Erythrocyte Chicken Serum Chicken Antibody Soluble Fibronectin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    H. N. Benson, H. P. Brumfield and B. S. Pomeroy, Requirement of avian C’l for fixation of guinea pig complement by avian antibody-antigen complexes, J. Immunol. 87:2 (1961).Google Scholar
  2. 2.
    E. M. Nicolaisen, C. Koch, K. Hála and M. Simonsen, Antigenantibody complex binding serum protein in the chicken, Foila Biol. (Praha) 23:426 (1977).Google Scholar
  3. 3.
    E. M. Nicolaisen and C. Koch, Haemagglutination-enhancing factor protein in chicken serum, Scand. J. Immunol. 13:11 (1981).CrossRefGoogle Scholar
  4. 4.
    J. Ivanyi and C. Tempelis, Genetic polymorphism of a serum euglobulin of chickens which binds to antigen-antibody complexes, Immunogenetics 10:83 (1980).PubMedCrossRefGoogle Scholar
  5. 5.
    E. M. Nicolaisen and M. Simonsen, Elution of chicken Ig from fixed target cells, J. Immunol. Meth. 29:139 (1979).CrossRefGoogle Scholar
  6. 6.
    R. J. Alexander and L. A. Steiner, The first component of complement from the bullfrog Rana catesbiana: functional properties of C1 and isolation of subcomponent C1q, J. Immunol. 124:1418 (1980).PubMedGoogle Scholar
  7. 7.
    J. D. Conradie, J. E. Volanakis and R. M. Stroud, Evidence for a serum inhibitor of C1q, Immunochemistry 12:967 (1975).PubMedCrossRefGoogle Scholar
  8. 8.
    B. Ghebrehiwet, C1q inhibitor (C1qINH): functional properties and possible relationship to a lymphocyte membrane-associated C1q precipitein, J. Immunol. 126:1837 (1981).PubMedGoogle Scholar
  9. 9.
    R. W. Ewald and A. F. Schubart, Agglutinating activity of the complement component C1q in the FII latex fixation test, J. Immunol. 97:100 (1966).PubMedGoogle Scholar
  10. 10.
    H. Isliker, D. H. Bing and R. O. Hynes, Interactions of fibronectin with C1q, a subcomponent of the first component of complement, in:“The Immune System,” Karger, Basel, 2:231 (1981).Google Scholar
  11. 11.
    M. Vuento, T. Vartio, M. Saraste, C. von Bonsdorf and A. Vaheri, Spontaneous and polyamine-induced formation of filamentous polymers from soluble fibronectin, Eur. J. Biochem. 105:33 (1980).PubMedCrossRefGoogle Scholar
  12. 12.
    F. Jilek and H. Hörmann, Cold-insoluble globulin, II. Plasminolysis of cold-insoluble globulin, Hoppe-Seyler’s Z. Physiol. Chem. 358:133 (1977).PubMedGoogle Scholar
  13. 13.
    K. M. Yamada and D. W. Kennedy, Fibroblast cellular and plasma fibronectins are similar but not identical, J. Cell. Biol. 80:492 (1979).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • Else Marie Nicolaisen
    • 1
  1. 1.Institute for Experimental ImmunologyUniversity of CopenhagenCopenhagen ØDenmark

Personalised recommendations