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Purification and characterization of the d-mannose receptor from J774 mouse macrophage cells

1991; Elsevier BV; Volume: 213; Linguagem: Inglês

10.1016/s0008-6215(00)90605-0

1873-426X

Janice S. Blum, Philip D. Stahl, Rubén Díaz, Maria Luisa Fiani,

Polyamine Metabolism and Applications

Macrophages display on their cell surface a d-mannose-specific receptor which facilitates the scavenging of certain pathogens and deleterious macromolecules from the extracellular fluid as part of the host defense mechanism. The mouse d-mannose receptor was purified from J774 E macrophages and an antiserum was generated against the receptor protein. In mouse macrophages, the newly synthesized receptor has an Mr of 157 000 Da and rapidly matures to a protein with an Mr of 172 000 Da. Both forms of the receptor protein are tightly associated with cell membranes. The receptor is found in a number of mouse macrophage cell types but is not present in mouse fibroblasts. An assay was developed to characterize d-mannose receptor-ligand binding based on immunoprecipitation of the detergent-solubilized receptor protein. The dissociation constant, determined for receptor and the neoglycoprotein d-mannose-BSA, was 1.67nm. Receptor-ligand binding was calcium and pH dependent. Monosaccharides, such as d-mannose and l-fucose, partially inhibited receptor binding to the ligand d-mannose-BSA.