The Human Blood <i>N</i>-Glycome: Unraveling Disease Glycosylation Patterns
Tamás Pongrácz, Oleg A. Mayboroda, Manfred Wuhrer
Abstract
High Resolution Image Download MS PowerPoint Slide Most of the proteins in the circulation are N -glycosylated, shaping together the total blood N -glycome (TBNG). Glycosylation is known to affect protein function, stability, and clearance. The TBNG is influenced by genetic, environmental, and metabolic factors, in part epigenetically imprinted, and responds to a variety of bioactive signals including cytokines and hormones. Accordingly, physiological and pathological events are reflected in distinct TBNG signatures. Here, we assess the specificity of the emerging disease-associated TBNG signatures with respect to a number of key glycosylation motifs including antennarity, linkage-specific sialylation, fucosylation, as well as expression of complex, hybrid-type and oligomannosidic N -glycans, and show perplexing complexity of the glycomic dimension of the studied diseases. Perspectives are given regarding the protein- and site-specific analysis of N -glycosylation, and the dissection of underlying regulatory layers and functional roles of blood protein N -glycosylation.