Title : Interaction of lipoprotein lipase with phospholipid vesicles. Role of apolipoprotein C-II and heparin - Shirai_1981_Biochim.Biophys.Acta_665_504
Author(s) : Shirai K , Matsuoka N , Jackson RL
Ref : Biochimica & Biophysica Acta , 665 :504 , 1981
Abstract :

Lipoprotein lipase is bound to heparin-like molecules at the surface of capillary endothelial cells. For maximal activity, the enzyme requires apolipoprotein C-II, a protein constituent of triacylglycerol-rich lipoproteins. In this report, the interactions of apolipoprotein C-II, heparin and sonicated vesicles of dipalmitoylphosphatidylcholine with purified bovine milk lipoprotein lipase were studied by gel filtration on Bio-Gel A5m. In the presence of vesicles of dipalmitoylphosphatidylcholine (1 mg), lipoprotein lipase (25 micrograms) associated with phospholipids even in the absence of apolipoprotein C-II. With limited phospholipid (40 micrograms), the amount of enzyme which associated with lipid decreased in the presence of apolipoprotein C-II (20 micrograms). Human plasma apolipoprotein C-III, another protein constituent of triacylglycerol-rich lipoproteins, also caused a decrease in the amount of enzyme associated with phospholipid. These results suggest that apolipoprotein C-II does not increase the activity of the enzyme by facilitating its interaction with a lipid interface. In the absence of lipid, lipoprotein lipase and apolipoprotein C-II (molar ratio, 1 : 1) eluted from Bio-Gel A5m as two separate components. The interaction of heparin with lipoprotein lipase was studied using a specific [3H]heparin, which was isolated by affinity chromatography on immobilized lipoprotein lipase; the [3H]heparin eluted with 0.6 M NaCl. Specific [3H]heparin coeluted with lipoprotein lipase when the enzyme was associated with phospholipid; the [3H]heparin was released from the enzyme by 0.75 M NaCl.

PubMedSearch : Shirai_1981_Biochim.Biophys.Acta_665_504
PubMedID: 6895327

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Citations formats

Shirai K, Matsuoka N, Jackson RL (1981)
Interaction of lipoprotein lipase with phospholipid vesicles. Role of apolipoprotein C-II and heparin
Biochimica & Biophysica Acta 665 :504

Shirai K, Matsuoka N, Jackson RL (1981)
Biochimica & Biophysica Acta 665 :504