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A more recent version of this article appeared on April 1, 2004

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J. Lipid Res., doi:10.1194/jlr.M300299-JLR200
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Submitted on July 3, 2003
Revised on December 22, 2003
Accepted on December 26, 2003

ASP enhances in situ lipoprotein lipase activity by increasing fatty acid trapping in adipocytes

May Faraj, Allan Sniderman, and Katherine Cianflone

Department of Medicine, McGill University Health Centre, Montreal, Quebec H3A 1A1

Corresponding Author: Katherine.Cianflone{at}mcgill.ca

Acylation stimulating protein (ASP) increases triglyceride (TG) storage (fatty acid trapping) in adipose tissue and plays an important role in postprandial TG clearance. We examined the capacity of ASP and insulin to stimulate the activity of lipoprotein lipase (LPL) and the trapping of LPL-derived non-esterified fatty acid (NEFA) in 3T3-L1 adipocytes. While insulin increased total LPL activity (secreted and cell-associated, p<0.001) in 3T3-L1 adipocytes, ASP moderately stimulated secreted LPL activity (p=0.04, 5% of total LPL activity). Neither hormone increased LPL translocation from adipocytes to endothelial cells in a co-culture system. However, both ASP and insulin increased Vmax of in situ LPL activity (3H-TG synthetic lipoprotein hydrolysis and 3H-NEFA incorporation into adipocytes) by 60% and 41% respectively (p<0.01) without affecting KM. Tetrahydrolipstatin (LPL inhibitor) diminished baseline, ASP and insulin-stimulated in situ LPL activity resulting in 3H-TG accumulation (p<0.0001). Unbound oleate inhibited in situ LPL activity (p<0.0001) but did not eliminate ASP stimulatory effect. Therefore 1) the clearance of TG-rich lipoproteins is enhanced by ASP through increasing TG storage and relieving NEFA inhibition of LPL, and 2) the effectiveness of adipose tissue trapping of LPL-derived NEFA determines overall LPL activity, which in turn, determines the efficiency of postprandial TG clearance.


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