Journal of Lipid Research (Dec 1997)

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

  • F H de Man,
  • F de Beer,
  • A van der Laarse,
  • A H Smelt,
  • L M Havekes

Journal volume & issue
Vol. 38, no. 12
pp. 2465 – 2472

Abstract

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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.