Purification of the human alveolar macrophage mannose receptor.
We report here the first isolation of a mannose receptor from human lung, and identify the alveolar macrophage as the cell of origin. The receptor was purified from detergent-solubilized lung tissue by absorption to mannose- and fucose-Sepharose, and elution with EDTA. The eluted protein had a molecular weight of 175 kD. Maximum binding of 125I-mannan-2 to the isolated receptor occurred at pH 7.5. Binding was inhibited by 40 micrograms/ml mannan (75%); 200 mM mannose (89%); and 200 mM fucose (93%). Galactose (200 mM) had no effect. Polyclonal antibodies raised against the purified receptor reacted with the purified 175 kD protein and a 175 kD protein from detergent extracts of human alveolar macrophages by immunoblot analysis. The antibody immunoprecipitated a 175 kD protein from solubilized 125I-labeled human alveolar macrophage membranes. These studies indicate that the 175 kD protein purified from human lung is the cell surface alveolar macrophage mannose receptor.
Department of Medicine, University of Tennessee, Memphis 38163.
J D
JD
Stephenson
V L
VL
Shepherd
D001667:Binding, Competitive; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D037181:Lectins, C-Type; D008168:Lung; D008264:Macrophages / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism; D000090323:Mannose Receptor; D037241:Mannose-Binding Lectins; D008970:Molecular Weight; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic / Q000302:isolation & purification* / Q000378:metabolism
D037181:Lectins, C-Type; D000090323:Mannose Receptor; D037241:Mannose-Binding Lectins; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; D008358:Mannose