Key change of malignant tissue glycosylation is altered sialic acid processingDuring malignant transformation, glycosylation is heavily altered compared with healthy tissue due to differential expression of glycosyltransferases, glycosidases and monosacharide transporters within the cancer environment. One key change of malignant tissue glycosylation is the alteration of sialic acid processing that leads to a general upregulation of sialylated glycans (hypersialylation) on cell surfaces and an increased introduction of the non-human sialic acid N-glycolyl-neuraminic acid (Neu5Gc) instead of N-acetyl-neuraminic acid into cell surface glycans [3,4]. These changes have been shown to be the result of altered sialyltransferase and sialydase expression. Functionally, cancer associated hypersialylation appears to directly impact tumor cell interaction with the microenvironment, in particular the modulation of sialic acid-binding lectins on immune cells. Moreover, Neu5Gc expression in human tissues enhances inflammation due to an anti-Neu5Gc immune response, which can potentially influence inflammation-induced cancer and cancer-associated inflammation [5].Changes in glycosylation are a classic hallmark of malignant transformation. The mechanisms that produce these aberrant glycosylation patterns are broad, because glycosylation is not template driven, but dependent on multiple interactions resulting from gene expression, substrate availability, the cellular environment and the underlying protein structure. Glycans are attached to both proteins and lipids to make glycoproteins and glycolipids respectively. Classical types of glycosylation are N-and O-linked (on proteins), glycosphunolipids (on cell-membrane sphingosine), glycosaminoglycans (GAGs) (protein-bund and