Glycan analysis of human neutrophil granules implicates a maturation-dependent glycosylation machinery
Vignesh Venkatakrishnan, Régis Dieckmann, Ian Loke, Harry C. Tjondro, Sayantani Chatterjee, Johan Bylund, Morten Thaysen‐Andersen, Niclas G. Karlsson, Anna Karlsson
Abstract
-acetyllactosamine repeats with Lewis epitopes. Immunoblotting and histochemical analysis confirmed the expression of Lewis X and sialyl-Lewis X in the intracellular granules and on the cell surface, respectively. Many glycans identified are unique to neutrophils, and their complexity increased progressively from azurophil granules to specific granules and then to gelatinase granules, suggesting temporal changes in the glycosylation machinery indicative of "glycosylation by timing" during granulopoiesis. In summary, this comprehensive neutrophil granule glycome map, the first of its kind, highlights novel granule-specific glycosylation features and is a crucial first step toward a better understanding of the mechanisms regulating protein glycosylation during neutrophil granulopoiesis and a more detailed understanding of neutrophil biology and function.