Yang_2015_Biochim.Biophys.Acta_1851_1327

Reference

Title : Regulation of hepatic lipase activity by sphingomyelin in plasma lipoproteins - Yang_2015_Biochim.Biophys.Acta_1851_1327
Author(s) : Yang P , Subbaiah PV
Ref : Biochimica & Biophysica Acta , 1851 :1327 , 2015
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.
ESTHER : Yang_2015_Biochim.Biophys.Acta_1851_1327
PubMedSearch : Yang_2015_Biochim.Biophys.Acta_1851_1327
PubMedID: 26193433

Citations formats

Yang P, Subbaiah PV (2015)
Regulation of hepatic lipase activity by sphingomyelin in plasma lipoproteins
Biochimica & Biophysica Acta 1851 :1327

Yang P, Subbaiah PV (2015)
Biochimica & Biophysica Acta 1851 :1327

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    [paper] => Yang_2015_Biochim.Biophys.Acta_1851_1327
    [author] => Yang P || Subbaiah PV
    [year] => 2015
    [title] => Regulation of hepatic lipase activity by sphingomyelin in plasma lipoproteins
    [journal] => Biochimica & Biophysica Acta
    [volume] => 1851
    [page] => 1327
    [medline] => 26193433
    [abstract] => Yang_2015_Biochim.Biophys.Acta_1851_1327
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            [longtext] => Yang_2015_Biochim.Biophys.Acta_1851_1327
            [content] => 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.
        )

)