Abstract
Mature macrophages (Mφ) differ from other rat leukocytes by their ability to bind soybean agglutinin (SBA). In this study we identify the SBA-binding structure on rat bone marrow-derived Mφ (BMDMφ). Precipitation of iodinated membrane proteins from rat bone marrow cells (BMC) and BMDMφ with SBA revealed a major glycoprotein of Mr 160 kDa on BMDMφ but not on BMC. In addition minor bands migrating at 70 and 26 kDa were seen. Stimulation of BMDMφ with 100 nM SBA induced a decrease in surface density of Thy1.1 (MRC OX7) and His54 and an increase in the expression of MRC OX6 (RT1.B/I-A), MRC OX17 (RT1.D/I-E), MRC OX41 (gp 110 120 ), MRC OX42 ( CD11b c ), Mac1 ( CD11b CR3 ) and Mac2 (galectin-3/IgE binding protein) antigen. Expression of other Mφ differentiation antigens recognized by mAb MRC OX43 (Mφ, endothelial cells) and ED9 ( Mφ CD14 like) were not significantly altered. BMDMφ derived from cultures with Mφ colony-stimulating factor (M-CSF) and SBA showed increased oxidative burst and phagocytic activity compared to cells cultured with M-CSF alone. Our data suggest that binding of a 160-kDa membrane glycoprotein on Mφ by N-acetylgalactosamine-specific lectins stimulates Mφ differentiation and activation.
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