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Isolation, characterization, and immunoprecipitation studies of immune
complexes from membranes of beta-thalassemic erythrocytes
J Yuan, R Kannan, E Shinar, EA Rachmilewitz and PS Low
Department of Chemistry, Purdue University, West Lafayette, IN.
beta-Thalassemia, a hemoglobinopathy that results in the precipitation of
denatured alpha-globin chains on the membrane, is characterized by
erythrocytes with significantly reduced lifespans. We have demonstrated
previously that hemoglobin denaturation on the membrane can promote
clustering of integral membrane proteins, and that this clustering in turn
leads to autologous antibody binding, complement fixation, and rapid
removal of the cell by macrophages. To evaluate whether this pathway also
occurs in beta-thalassemic cells, we have isolated and characterized the
immune complexes from the membranes of these cells. We observe that
autologous IgG-containing complexes obtained by either immunoprecipitation
or simple centrifugation of nondenaturing detergent extracts of
beta-thalassemic cell membranes contain globin, band 3, IgG, and complement
as major components. Absorption spectra of these complexes demonstrate that
the globin is, indeed, mainly in the form of hemichromes. Immunoblotting
studies further show that much of the band 3 protein in the aggregates is
covalently cross-linked to a dimeric or tetrameric form, consistent with
the preference of the autologous IgG for clustered band 3. Although the
insoluble aggregates constitute only approximately 1.6% of the total
membrane protein, they still contain 27% of the total IgG and 35% of the
total complement C3 on the thalassemic cell surface. Because cell surface
IgG and complement component C3 are thought to trigger removal of
erythrocytes from circulation, the hemichrome-induced clustering of band 3
may contribute to the beta-thalassemic cell's shortened lifespan.
Volume 79,
Issue 11,
pp. 3007-3013,
06/01/1992
Copyright © 1992 by The American Society of Hematology
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