Increased [alpha]3-fucosylation of [alpha]1-acid glycoprotein in Type I diabetic patients is related to vascular function

Diabetic mellitus is attended by the development of endothelial dysfunction which is suggested to be accompanied with a chronic low-degree of inflammation. During a chronic hepatic inflammatory response, specific changes in glycosylation of the acute phase protein α^sub 1^-acid glycoprotein (AGP) can be detected. In this report we studied the changes in glycosylation of AGP in more detail and evaluated the relation between a change in glycosylation of AGP and urinary albumin secretion in Type I diabetic patients. The glycosylation of AGP, studied by crossed affinity immunoelectrophoresis (CAIE) and high pH anion exchange chromatography with pulse amperometric detection (HPAEC-PAD), showed an increase in α3-fucosylation. Staining with an antibody against sialyl Lewis^sup x^ (sLe^sup x^) implied that part of the α3-fucosylation was present in a sLe^sup x^-conformation. In the group of Type I diabetic patients with increased urinary albumin excretion, a significant increase in α3-fucosylation of AGP (p[emsp4 ]