RGD Reference Report - Activation of hepatic lipase catalyzed phosphatidylcholine hydrolysis by apolipoprotein E. - Rat Genome Database

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Activation of hepatic lipase catalyzed phosphatidylcholine hydrolysis by apolipoprotein E.

Authors: Thuren, T  Sisson, P  Waite, M 
Citation: Thuren T, etal., Biochim Biophys Acta. 1991 May 8;1083(2):217-20.
RGD ID: 2307436
Pubmed: PMID:2036455   (View Abstract at PubMed)

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.



Objects referenced in this article
Gene Lipc lipase C, hepatic type Rattus norvegicus

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