[HTML][HTML] Apolipoproteins CI and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets
M Larsson, E Vorrsjö, P Talmud, A Lookene… - Journal of Biological …, 2013 - ASBMB
Apolipoproteins (apo) CI and C-III are known to inhibit lipoprotein lipase (LPL) activity, but
the molecular mechanisms for this remain obscure. We present evidence that either apoC-I
or apoC-III, when bound to triglyceride-rich lipoproteins, prevent binding of LPL to the
lipid/water interface. This results in decreased lipolytic activity of the enzyme. Site-directed
mutagenesis revealed that hydrophobic amino acid residues centrally located in the apoC-III
molecule are critical for attachment to lipid emulsion particles and consequently inhibition of …
the molecular mechanisms for this remain obscure. We present evidence that either apoC-I
or apoC-III, when bound to triglyceride-rich lipoproteins, prevent binding of LPL to the
lipid/water interface. This results in decreased lipolytic activity of the enzyme. Site-directed
mutagenesis revealed that hydrophobic amino acid residues centrally located in the apoC-III
molecule are critical for attachment to lipid emulsion particles and consequently inhibition of …