Binding of human fibronectin to antigen-antibody complexes

Fernando G Cosio, A. P. Bakaletz

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


We examined the capacity of human fibronectin (FN) to bind to antigen-antibody (IgG) complexes (IC) in the absence of complement components. Binding of FN to IC was not significantly different at 37 °C and 4 °C and reached equilibrium after 60 minutes of incubation. The binding was markedly enhanced by decreasing the ionic strength and lowering the pH of the incubation media. The effect of ionic strength on binding was caused at least in part by an increase in the percent of the total FN able to bind to IC. Binding of radiolabeled FN to IC was saturable and was inhibited by the addition of an excess of unlabeled FN. In addition, soluble IC prepared in antigen excess but not antigen or antibody alone inhibited the binding of FN to precipitable IC. FN binding to precipitable IC Increased with increasing antibody concentrations in the IC. Heparin and gelatin, which bind to specific locations in the FN molecule, did not inhibit the binding of FN to IC. In conclusion, human FN binds to IC in the absence of C1q, and the binding is enhanced under conditions of antibody excess.

Original languageEnglish (US)
Pages (from-to)447-452
Number of pages6
JournalThe Journal of Laboratory and Clinical Medicine
Issue number5
StatePublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • General Medicine
  • Pathology and Forensic Medicine


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