engleski

N-GLYCOSYLATION OF TOTAL SERUM PROTEINS IN ADULTS WITH TYPE I DIABETES MELLITUS

Previous studies have shown that aberrant plasma protein N-glycosylation exists in children newly diagnosed with T1D, but there is little information on the N-glycome in the adult life of patients. N-glycosylation has been associated with poor glycaemic control and nephropathy, but other common diabetic complications remain to be assessed. Therefore, we compared the serum protein N-glycosylation between patients and controls and analysed its changes in regard to complication status, duration of the disease, glycaemic control and biochemical parameters. Total serum protein N-glycans were analysed in 200 patients with T1D (aged 18-70) and 298 healthy controls (aged 18-79). N-glycome was divided in 39 glycan groups and 16 derived traits calculated based on structural similarities. Patients were further divided based on the status of hypertension, albuminuria and retinopathy. Smoking, a major risk factor for the development of diabetic complications, was noted. Patients with T1D exhibited significant differences in N-glycosylation compared to healthy controls (19/39 glycan groups and 4/16 derived traits), e.g., monogalactosylated glycans were lowered, while digalactosylated, monosialylated and antennary fucosylated were elevated. The duration of the disease or biochemical parameters, other than HbA1c, showed no correlation with N-glycome. HbA1c was positively associated with sialylated and highly branched glycans. The effect of smoking was observed through the increase of high-branched, trigalactosylated and trisialylated glycans and the decrease of low- branched, a- and monogalactosylated, asialylated, bisecting and core-fucosylated glycans. Presence of T1D in adults associates with major changes in total serum N-glycome, some of which were previously reported in children. The duration of T1D, as well as the development of diabetic complications, appear not to further affect these changes. Poor glycaemic control and smoking status are strongly reflected in the N-glycome.

Type 1 diabetes mellitus, N-glycosylation, Serum protein N-glycosylation

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