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Inhibition of lipoprotein lipase by the receptor‐binding domain of apolipoprotein E
Author(s) -
McConathy Walter.J.,
Wang Chi-Sun
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81464-4
Subject(s) - lipoprotein lipase , low density lipoprotein receptor related protein 8 , apolipoprotein e , chemistry , apolipoprotein b , lipase , apolipoprotein c2 , ldl receptor , lipoprotein , biochemistry , very low density lipoprotein , medicine , cholesterol , enzyme , disease
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 μM 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.