The Interaction of Human Plasma Glycosaminoglycans with Plasma Lipoproteins

Formalinized, tannic acid-treated sheep erythrocytes coated with low density lipoproteins (LDL) or apoprotein B (apo-B) are agglutinated by anti-apo-B immunserum. Those coated with high density lipoproteins (HDL) or apoprotein A-I (apo-A-I) are agglutinated by anti-apo-A-I immunserum. These coated formocells have been used to study the interactions of lipoproteins and apoproteins with plasma glycosaminoglycans (GAG). The sulfate-rich species of plasma GAG agglutinates cells coated with LDL, HDL, apo-B, and apo-A-I at ionic concentrations above 0.15 M. The less-sulfated species of plasma GAG does not agglutinate the coated cells but inhibits the agglutination caused by the sulfaterich species. Treatment of the sulfate-rich GAG with papain causes a reduction in molecular weight by one-half and also causes a loss of its agglutinating activity. These results suggest that the sulfate-rich plasma GAG, consisting of two glycan chains linked to a peptide backbone, cause agglutination by binding to two or more formocells. In contrast, the less-sulfated plasma GAG, consisting of single, short glycan chains, are incapable of causing agglutination but may prevent it by covering specific binding sites present on the coated cells.