Characterization of human neutrophil glycoproteins expressing the CD15 differentiation antigen (3-fucosyl-N-acetyllactosamine).

The expression of the CD15 antigen, 3-fucosyl N-acetyllactosamine, on neutrophil glycoproteins has been studied by SDS gel electrophoresis and immunoblotting. The antigen is expressed on several glycoproteins, both intracellularly and on the cell surface. Each subcellular compartment appears to contain a specific antigen. A soluble, granule glycoprotein (Mr 80-90K) probably accounts for most of the intracellular staining detected immunohistochemically. Membrane glycoproteins of Mr, 85-90K and 25K are associated with granule membranes, the latter being an integral membrane protein. The CD15 antigen is expressed on several cell surface glycoproteins with Mr in the range of 165K and 105K. These antigens are also contained in an intracellular pool which is brought to the surface on activation of the cells with chemotactic peptides. The 165K and 105K antigens show identical electrophoretic mobility to two of the major glycoproteins detectable by PAS or protein staining of gels of detergent extracts of cell membranes. These glycoproteins include the complement receptor, CR3. The beta chain of CR3 (105K) and to a lesser extent the alpha chain (165K) express CD15; however, most of the CD15 antigen is associated with other glycoproteins of these molecular masses.