Journal of Lipid Research, Vol 38, 2465-2472, Copyright © 1997 by Lipid Research, Inc.

ARTICLES

Lipolysis of very low density lipoproteins by heparan sulfate proteoglycan-bound lipoprotein lipase

FH de Man, F de Beer, A van der Laarse, AH Smelt and LM Havekes
Department of Cardiology, Leiden University Medical Centre, The Netherlands.

An in vitro assay to study lipolysis of very low density lipoproteins (VLDL) by heparan sulfate proteoglycan (HSPG-bound lipoprotein lipase (LPL) was developed. Optimal conditions for VLDL lipolysis by HSPG- bound LPL were obtained by incubating plastic wells with 0.5 microg HSPG and 1.5 microg LPL, subsequently. Control experiments with heparinase indicate that at least 90% of the LPL activity is derived from LPL bound to heparan sulfate chains. For HSPG-LPL-mediated lipolysis, the apparent Km and Vmax values were 0.36 +/- 0.11 mM VLDL- triglycerides and 1.2 +/- 0.1 microM free fatty acids/min x ng LPL, respectively. The mean intra-assay and inter-assay coefficients of variance were 5% and 8%, respectively.
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