Abstract
We have examined IgG Fc receptor (FcR) activity of human and rabbit arachnoid granulations and leptomeninges using antibody (IgG)-coated erythrocytes (EIgG), covalently crosslinked IgG dimers, trimers and oligomers, immune complexes, aggregated Fc fragments and a monoclonal anti-human neutrophil Fc receptor antibody, 3G8. EIgG bound specifically to cells of the leptomeninges and arachnoid granulations; uncoated erythrocytes, F(ab')2-coated, or IgM-coated erythrocytes failed to bind. The specificity of this interaction was demonstrated by inhibition studies. Monomeric IgG and Fc fragments blocked EIgG adherence, whereas bovine serum albumin (BSA), Fab fragments of IgG and the monoclonal anti-neutrophil FcR antibody failed to inhibit EIgG adherence. Monomeric IgG inhibited FcR function in a dose-dependent fashion; maximal inhibition was achieved at 1.7 X 10(-5)M IgG, indicating a relatively low avidity receptor. Oligomers of IgG inhibited EIgG adherence more effectively and inhibition was directly related to oligomer size. Additionally, these tissues were positive for specific and non-specific esterases. These studies suggest that the CSF pathway from the perivascular spaces to the arachnoid granulations plays a protective role in the clearance of IgG and IgG immune complexes in infections and immune-mediated disorders.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
