The features and function of IgM-FcR of rat peritoneal macrophages were studied. Macrophages specifically bind and phagocytose ox red blood cells coated with rat IgM (EA-IgM) through a specific receptor. This receptor is trypsin sensitive and its activity requires Ca++ ions. Both sodium azide and low temperature (4°) inhibit the binding as well as ingestion of EA-IgM by macrophages, suggesting the metabolically dependent character of the interaction between EA-IgM and macrophages. Colchicine inhibits the binding of EA-IgM by macrophages. Similarly, the ingestion of EA-IgM was also inhibited when peritoneal exudate cells (PEC) were pretreated with colchicine or vinblastine or cytochalasin B. It is suggested that cytoskeletal elements of macrophages play an important role both in the binding of EA-IgM to their receptors and in the subsequent internalization of the receptor-ligand complexes. Ingestion of soluble IgM antibodies containing immune complexes resulted in a release of β-glucuronidase from macrophages.
|Number of pages||7|
|Publication status||Published - jan. 1 1981|
ASJC Scopus subject areas
- Immunology and Allergy