High throughput contract analysis of plasma glycans

Glycosylation is a post-translational modification that enriches protein complexity and function. Multiple proteins are modified by covalently bound glycans, which is important for normal physiological processes, including protein folding, degradation and secretion, cell signaling, immune function and transcription. This process is not template driven, so that the complexity of the glycoproteome is estimated to be several orders of magnitude greater than for the proteome itself. Dysregulation of glycosylation is implicated in a wide range of diseases, including cancer, diabetes, cardiovascular, congenital, immunological and infectious disorders. Protein based medicaments (immunoglobulins, erythropoietin, etc) are in use for autoimmune diseases, tumors and anemia but sometimes these medicaments are not efficient because of inadequate glycosylation.

Protein based medicaments are often synthesized in bacterial cells or cell cultures and these conditions do not always correspond to glycosylation environment in normal physiological cell. Result can be a protein with correct amino acid sequence but with different pattern of glycosylation. As glycosylation controls protein targeting and in general its proper function, the efficiency of that medicament is frequently reduced. To develop efficient protein based medicaments but also functional recombinant protein for other purposes, it is necessary to analyze glycosylation of native proteins, as any progress can be possible only if we know and understand the natural processes.