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Fibronectin Binding to C1 q Associated with Antigen‐Antibody Complexes in EDTA‐treated Plasma
Author(s) -
SORVILLO J.,
GIGLI I.,
PEARLSTEIN E.
Publication year - 1986
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1986.tb01953.x
Subject(s) - fibronectin , antigen , incubation , antibody , ovalbumin , immune system , chemistry , antigen antibody complex , immune complex , complement c1q , microbiology and biotechnology , biochemistry , biology , immunology , extracellular matrix , complement system
In this report we have investigated the association of fibronectin with antigen‐antibody‐C1q complexes incubated in fibronectin‐depleted and C1 q ‐depleted plasma. When BSA‐anti‐BSA immune aggregates arc incubated in plasma depleted of both fibronectin and C1 q to which‘ 125 I fibronectin has been reconstituted, little radioactivity is bound to the immune complexes. However, pre‐incubation of immune complexes with purified C1q prior to incubation in the plasma causes an approximately l0‐fold increase in the amount of radioactivity bound. The binding of 125 I‐M‐fibronectin to preformed antigen‐antibody‐C1 q complexes is specific, since the reaction is inhibited by the addition of unlabelled fibronectin but not by ovalbumin When antigen‐antibody ‐C1 q complexes are incubated in CI q ‐depleted plasma containing physiogical concentrations of fibronectin. and analysed by immunoblotting. fibronectin antigens are detected on the immune Complexes. Identical results are obtained using imune complexes composed of sheep erythrocyte rabbit anti‐sheep erythrocyte C1 q (EAC1q) cells, There is no specific requirement for preformed antigen‐antibody‐C1 q complexes. since fibronectin can be detected on antigen ‐antibody complexes after incubation in normal human serum or in C1 q ‐depleted ethylenediamineteraacetic acid (EDIA) serum reconstituted with purified C1q prior to incubation with the complexes, Finally, we also demonstrate that in the presence of C1 q , 125 I‐fibronectin will associate with soluble antigen‐antibody complexes.