Activation of hepatic lipase catalyzed phosphatidylcholine hydrolysis by apolipoprotein E

Biochim Biophys Acta. 1991 May 8;1083(2):217-20. doi: 10.1016/0005-2760(91)90046-k.

Abstract

The effect of apolipoproteins A-I, A-II, C-II, C-III and E on the hydrolysis of phosphatidylcholine and triacylglycerol by hepatic lipase was studied. Hepatic lipase catalyzed phospholipid hydrolysis was 1.8-fold activated by apolipoprotein E while the other apolipoproteins did not affect the hydrolysis by this enzyme. Triacylglycerol hydrolysis by hepatic lipase was 1.5-fold activated by apolipoprotein E while the other apolipoproteins inhibited hepatic lipase. These results suggest that lipoproteins containing apolipoprotein E may be preferred substrates for hepatic lipase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apolipoproteins / physiology
  • Apolipoproteins E / physiology*
  • Catalysis
  • Enzyme Activation
  • Hydrolysis
  • In Vitro Techniques
  • Lipase / antagonists & inhibitors
  • Lipase / metabolism*
  • Liver / enzymology*
  • Phosphatidylcholines / metabolism*
  • Rats
  • Triglycerides / metabolism

Substances

  • Apolipoproteins
  • Apolipoproteins E
  • Phosphatidylcholines
  • Triglycerides
  • Lipase