Metabolism of glycosylated very-low-density lipoproteins in human skin fibroblasts.

Very-low-density lipoproteins (VLDL) were glycosylated using glucose and sodium cyanoborohydride. The binding and rate of degradation of glycosylated VLDL in human skin fibroblasts were reduced significantly compared to native VLDL. These glycosylated VLDL were not able to activate acyl-CoA:cholesterol acyltransferase or inhibit cholesterol synthesis in fibroblasts. Glycosylated VLDL showed higher mobility on agarose electrophoresis, and apolipoprotein E in these lipoproteins showed higher molecular weight on SDS-polyacrylamide gel electrophoresis. The physiological significance of glycosylation of VLDL in hyperglycemic subjects is speculated.