Add time:08/10/2019         Source:sciencedirect.com

Immunoglobulin G autoantibodies selectively bind to senescent human red blood cells (RBC) in situ and initiate their removal by phagocytosis. In this paper, we characterize the IgG binding receptor appearing on senescent RBC using glycophorin-enriched vesicles prepared by Triton X-100 extraction of young, middle-aged, and old RBC populations. These vesicles contain all known sialoglycoproteins and trace contaminants of other proteins. IgG binds predominantly to vesicles from old cells, as determined by both 125I-labeled protein A binding to IgG molecules and an erythrophagocytosis-inhibition assay. Addition of lipids does not alter IgG binding. Liposomes prepared from lipids of young and old cell fractions do not bind significant amounts of IgG. IgG binding is reduced following trypsin treatment of vesicles. The data suggest that the age-specific cell antigen is a protein which co-purifies with sialoglycoproteins, but is not identical with glycophorin. Since it is extracted predominantly from senescent cells, a chemical modification within the membrane may either form the age-specific cell antigen during aging or render it accessible during senescence.

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