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.
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McConathy et al. (1989) studied this question.
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