Open AccessLack of binding between cryoimmunoglobulins, immunoglobulins and fibronectin: implications for immune complex vasculitis
Author(s) -
BRANDAU D. T.,
O'DONNELL R.,
KIMMELTRUITT V. L.
Publication year - 1991
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1991.tb05588.x
Subject(s) - immunology , cryoglobulins , antibody , immune system , immune complex , immunoglobulin g , fibronectin , vasculitis , immunoglobulin m , antigen antibody complex , chemistry , biology , medicine , biochemistry , pathology , disease , cell
SUMMARY Immunc‐complex‐mcdiated vasculitis is a frequent complication of rheumatoid arthritis and systemic lupus erythematosus. The mechanism of deposition of immune complexes within the vessel wall in these diseases remains unknown, but probably involves other proteins. Fibronectin is a likely candidate since it possesses the ability to bind to collagen, endothelial cells, and possibly immunoglobulins and immune complexes. In this study, the hinding of libronectin to IgG and IgM cryoglobulins, cold soluble IgM, IgG, IgG subclasses and IgG fragments was investigated in the solution phase. Static light scattering, fluorescence anisotropy. fluorescence intensity, and PEG precipitation studies were used to investigate binding under different conditions of temperature and ionic strength. These studies failed to demonstrate significant binding between fibronectin and IgM, IgG, IgG subclasses and IgG fragments under the conditions studied These findings argue against solution phase binding of fibronectin and immunoglobulins contributing to immune complex vasculitis. The possibility of important surface interactions between these proteins has not been ruled out.