Inhibition of lipoprotein lipase by the receptor-binding domain of apolipoprotein E.
A synthetic peptide (residues 139-153) corresponding to the receptor-binding domain of apolipoprotein E (ApoE) was tested for lipoprotein lipase (LPL) inhibitory properties. In systems using both natural and synthetic substrates, inhibition of LPL was observed. Using the synthetic substrate, 50% inhibition was observed at 50 microM while high concentrations completely inhibited LPL activity. These studies suggest an additional functional role for the receptor-binding domain of ApoE-modulation of LPL activity.
McConathy
W J
WJ
Lipoprotein and Atherosclerosis Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.
Wang
C S
CS
D000818:Animals; D001057:Apolipoproteins E / Q000378:metabolism / Q000494:pharmacology*; D001665:Binding Sites; D002417:Cattle; D008071:Lipoprotein Lipase / Q000037:antagonists & inhibitors*; D008079:Lipoproteins, VLDL / Q000378:metabolism; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D010446:Peptide Fragments / Q000378:metabolism / Q000494:pharmacology*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D014280:Triglycerides / Q000378:metabolism
D001057:Apolipoproteins E; D008079:Lipoproteins, VLDL; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D014280:Triglycerides; D008071:Lipoprotein Lipase