A glycosaminoglycan activator of lipoprotein lipase in human plasma.
By use of ion exchange chromatography we have isolated two discrete classes of "free" glycosaminoglycans (GAG) from human plasma. The GAG fractions were tested for their effects on two lipoprotein lipase (LPL) enzyme systems containing an apolipoprotein C-II activated emulsion as the triglyceride substrate and bovine serum albumin as the free fatty acid acceptor. The lowcharge GAG (Fraction I) had essentially no effect on the LPL reaction. The high-charge GAG (Fraction II) stimulated the LPL reaction 100 to 300%. The GAG composition of each fraction was investigated with chemical and enzymatic techniques. Fraction I consisted of low-charge chondroitin sulfate noncovalently bound to protein. Fraction II consisted of a mixture of high-charge GAG non-covalently bound to protein. Degradation with nitrous acid eliminated the ability of high-charge GAG to stimulate LPL. This and other evidence suggests that the high-charge GAG in human plasma responsible for LPL activation is heparan sulfate (HS). We suggest that plasma HS may modulate triglyceride clearance mechanisms in vivo by its interaction with LPL.
D053304:Apolipoprotein C-II; D001053:Apolipoproteins / Q000097:blood; D001056:Apolipoproteins C; D002852:Chromatography, Ion Exchange; D004789:Enzyme Activation; D006025:Glycosaminoglycans / Q000494:pharmacology*; D006497:Heparan Sulfate / Q000494:pharmacology; D006801:Humans; D008071:Lipoprotein Lipase / Q000097:blood*
D053304:Apolipoprotein C-II; D001053:Apolipoproteins; D001056:Apolipoproteins C; D006025:Glycosaminoglycans; D006497:Heparan Sulfate; D008071:Lipoprotein Lipase