Identification and characterization of Sarcophaga lectin receptor on the surface of murine macrophages by use of monoclonal antibodies.
The structure of Sarcophaga lectin receptor on the surface of murine macrophages was analyzed using monoclonal antibodies. This receptor was found by gel filtration to have a molecular weight of 460 kDa. SDS-polyacrylamide gel electrophoresis showed that this receptor consists of two subunits of 170 kDa and 110 kDa. The results indicated that it is probably a heterotetramer of two molecules of each subunit. Two monoclonal antibodies recognized epitopes in the 110 kDa subunit, and one of them specifically inhibited the binding of Sarcophaga lectin to macrophages and the cytotoxic reaction mediated by this lectin in the presence of macrophages. Therefore, it is likely that the 110 kDa protein in the receptor plays a role in activation of macrophages by this lectin.
Ohkuma
Y
Y
Faculty of Pharmaceutical Sciences, University of Tokyo.
Komano
H
H
Natori
S
S
D000818:Animals; D000911:Antibodies, Monoclonal; D004175:Diptera; D004591:Electrophoresis, Polyacrylamide Gel; D007120:Immunochemistry; D019476:Insect Proteins; D037102:Lectins / Q000032:analysis*; D037181:Lectins, C-Type; D008264:Macrophages / Q000032:analysis*; D008297:Male; D051379:Mice; D008970:Molecular Weight; D011975:Receptors, Mitogen / Q000032:analysis*
C043030:20kDa lectin protein, Sarcophaga; D000911:Antibodies, Monoclonal; D019476:Insect Proteins; D037102:Lectins; D037181:Lectins, C-Type; D011975:Receptors, Mitogen