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Abstract
To gain insight into sialic acid biology and sialidase/neuraminidase (NEU) expression in mature human neutrophil (PMN)s, we studied NEU activity and expression in PMNs and the HL60 promyelocytic leukemic cell line, and changes that might occur in PMNs undergoing apoptosis and HL60 cells during their differentiation into PMN-like cells. Mature human PMNs contained NEU activity and expressed NEU2, but not NEU1, the NEU1 chaperone, protective protein/cathepsin A(PPCA), NEU3, and NEU4 proteins. In proapoptotic PMNs, NEU2 protein expression increased > 30.0-fold. Granulocyte colony-stimulating factor protected against NEU2 protein upregulation, PMN surface desialylation and apoptosis. In response to 3 distinct differentiating agents, dimethylformamide, dimethylsulfoxide, and retinoic acid, total NEU activity in differentiated HL60 (dHL60) cells was dramatically reduced compared to that of nondifferentiated cells. With differentiation, NEU1 protein levels decreased > 85%, PPCA and NEU2 proteins increased > 12.0-fold, and 3.0-fold, respectively, NEU3 remained unchanged, and NEU4 increased 1.7-fold by day 3, and then returned to baseline. In dHL60 cells, lectin blotting revealed decreased α2,3-linked and increased α2,6-linked sialylation. dHL60 cells displayed increased adhesion to and migration across human bone marrow-derived endothelium and increased bacterial phagocytosis. Therefore, myeloid apoptosis and differentiation provoke changes in NEU catalytic activity and protein expression, surface sialylation, and functional responsiveness.
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1 Research Service, Baltimore Veterans Affairs Medical Center, Baltimore, USA (GRID:grid.56061.34) (ISNI:0000 0000 9560 654X); University of Maryland School of Medicine, Department of Medicine, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)
2 University of Maryland School of Medicine, Department of Medicine, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264); University of Maryland School of Medicine, Center for Vaccine Development and Global Health, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)
3 University of Maryland School of Medicine, Department of Pediatrics, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)
4 University of Maryland School of Medicine, Department of Medicine, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264); University of Maryland School of Medicine, Department of Pathology, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)
5 University of Maryland School of Medicine, Department of Physiology, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264); University of Maryland School of Medicine, Marlene and Stewart Greenebaum Cancer Center, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)
6 University of Maryland School of Medicine, Department of Medicine, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264); University of Maryland School of Medicine, Department of Pathology, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264); University of Maryland School of Medicine, Marlene and Stewart Greenebaum Cancer Center, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)
7 University of Maryland School of Medicine, Department of Medicine, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)
8 Food and Drug Administration, Division of Parasitic and Allergenic Products, Center for Biologics Evaluation and Research, Silver Spring, USA (GRID:grid.417587.8) (ISNI:0000 0001 2243 3366)
9 Research Service, Baltimore Veterans Affairs Medical Center, Baltimore, USA (GRID:grid.56061.34) (ISNI:0000 0000 9560 654X); University of Maryland School of Medicine, Department of Medicine, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264); University of Maryland School of Medicine, Department of Pathology, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264); University of Maryland School of Medicine, Marlene and Stewart Greenebaum Cancer Center, Baltimore, USA (GRID:grid.411024.2) (ISNI:0000 0001 2175 4264)