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Human Membrane‐bound C3 Receptors I. Serological and Immunohistological Demonstration of C3 Receptors
Author(s) -
STEIN H.,
GERDES J.,
TOLKSDORF G.,
KLATT U.
Publication year - 1981
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1981.tb00112.x
Subject(s) - tonsil , agglutination (biology) , receptor , antiserum , microbiology and biotechnology , antibody , staining , biology , chemistry , pathology , immunology , medicine , biochemistry
The aim of the present study was to present further evidence of the specific reactivity of an anti‐C3 receptor serum (AC3RS), to demonstrate membrane‐bound C3 receptors by using this AC3RS in different serological and immunohistological methods, and to investigate the relationship between membrane‐bound C3 receptor and α 1 ‐antitrypsin. The AC3RS, or F(ab) 2 fragments of the IgG fraction of this antiserum, stained a percentage on various viable cell populations roughly equivalent to the number of cells that bound EAC3b and or EAC3d; C3 receptor‐negative T cells and thymocytes were not stained. On frozen sections of tonsils and kidneys it was found that the AC3RS stained the area to which EAC3b adhered. After absorption with neutrophils or E hu , the AC3RS Inhibited the agglutination of EAC3d with tonsil cells, not the agglutination of tonsil cells or neutrophils with EAC3b; this absorbed AC3RS still stained tonsil cells but not neutrophils, in frozen tonsil sections it Stained only those areas to which AC3d adhered. The absorbed AC3RS did not stain glomeruli. Antisera to α 1 ‐antitrypsin failed to in‐hibit EAC agglutination with C3 receptor‐bearing cells or to stain C3 receptor‐positive cells either in suspension or in frozen sections. Absorption of the AC3RS with purified α 1 ‐antitrypsin did not affect its specific reactivity.