Nonenzymatic galactosylation of human LDL decreases its metabolism by human skin fibroblasts

Incubation of human LDL with galactose in vitro resulted in a glycosylated-LDL containing radiolabel covalently attached to apo B. The rate of radiolabel incorporation was proportional to the time of incubation and concentration of carbohydrate. The rate of incorporation of galactose into apo B was higher than with glucose or mannose. The nonenzymatic glycosylation of LDL decreased its uptake and metabolism by the high affinity, receptor dependent process for LDL in normal human skin fibroblasts.