Effects of glycosylation on the structure and function of the extracellular chaperone clusterin

A technique is developed to enzymatically remove attached sugars from human serum-derived clusterin under native conditions and a series of assays is performed to compare the structure and in vitro function of wild type and deglycosylated clusterin. Evidence suggests that the normally conjugated sugars are important in the interaction of secreted clusterin with a lectin-type receptor on liver cells.