ArticleBiochimica et biophysica acta2015
Regulation of hepatic lipase activity by sphingomyelin in plasma lipoproteins.
Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
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- A rapid increase in lysophospholipids after geranylgeranoic acid treatment in human hepatoma-derived HuH-7 cells revealed by metabolomics analysis.Biochemistry and biophysics reports · 2021Article
- Potential role of hepatic lipase in the accretion of docosahexaenoic acid (DHA) by the brain.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021Article
- Cloning of hepatic lipase and the effects of dietary nutrition on hepatic lipase expression in genetically improved farmed tilapia (Oreochromis niloticus).Fish physiology and biochemistry · 2020Article
- Patients with Concurrent Tuberculosis and Diabetes Have a Pro-Atherogenic Plasma Lipid Profile.EBioMedicine · 2018Article
- Dietary docosahexaenoic acid (DHA) as lysophosphatidylcholine, but not as free acid, enriches brain DHA and improves memory in adult mice.Scientific reports · 2017Article
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- Enhanced incorporation of dietary DHA into lymph phospholipids by altering its molecular carrier.Biochimica et biophysica acta · 2016Article
- Hypolipidemic effects of chitosan and its derivatives in hyperlipidemic rats induced by a high-fat diet.Food & nutrition research · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Hepatic lipase (HL) is an important enzyme in the clearance of triacylglycerol (TAG) from the circulation, and has been proposed to have pro-atherogenic as well as anti-atherogenic properties. It hydrolyzes both phospholipids and TAG of lipoproteins, and its activity is negatively correlated with HDL levels. Although it is known that HL acts preferentially on HDL lipids, the basis for this specificity is not known, since it does not require any specific apoprotein for activity. In this study, we tested the hypothesis that sphingomyelin (SM), whose concentration is much higher in VLDL and LDL compared to HDL, is an inhibitor of HL, and that this could explain the lipoprotein specificity of the enzyme. The results presented show that the depletion of SM from normal lipoproteins activated the HL roughly in proportion to their SM content. SM depletion stimulated the hydrolysis of both phosphatidylcholine (PC) and TAG, although the PC hydrolysis was stimulated more. In the native lipoproteins, HL showed specificity for PC species containing polyunsaturated fatty acids at sn-2 position, and produced more unsaturated lyso PC species. The enzyme also showed preferential hydrolysis of certain TAG species over others. SM depletion affected the specificity of the enzyme towards PC and TAG species modestly. These results show that SM is a physiological inhibitor of HL activity in lipoproteins and that the specificity of the enzyme towards HDL is at least partly due to its low SM content.
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