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Cellular Binding Mechanism on Rat Macrophages for Sialylated Glycoconjugates, Inhibited by the Monoclonal Antibody ED3
Author(s) -
Damoiseaux J.G.M.C.,
Döpp E.A.,
Dijkstra C.D.
Publication year - 1991
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.49.5.434
Subject(s) - glycoconjugate , biology , monoclonal antibody , mechanism (biology) , antibody , microbiology and biotechnology , immunology , biochemistry , philosophy , epistemology
The mAb ED3 recognizes a subpopulation of rat macrophages, with a highly restricted tissue distribution. The tissue distribution as well as the in vitro expression of the ED3 antigen and of the sheep erythrocyte receptor (SER), binding unopsonized erythrocytes in the mouse, are very similar. This receptor has almost the same binding characteristics, although a different tissue distribution, as the sialic acid binding receptor (SAR), binding ganglioside‐coated erythrocytes in the rat In this study we summarize the available literature concerning these sialic acid binding receptors (SER and SAR). Furthermore we have identified ED3 as SER by inhibition studies of erythrocyte binding with mAb ED3, as well as by the newly developed equivalents ED16 and ED17. We also show that light trypsin treatment of alveolar macrophages, expressing SAR, results in SER‐like activity. This obtained SER‐like activity could not be blocked by the mAb ED3, indicating that SER and SAR are different receptors. It appears that rat macrophages can express two receptors for sialylated glycoconjugates, a high‐affinity receptor SER, recognized by mAb ED3, and a low‐affinity receptor SAR, not recognized by mAb ED3.