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Release of lipoprotein lipase from cardiac myocytes by low-molecular weight heparin

J E Braun1, D L Severson

  • 1MRC Signal Transduction Group, University of Calgary, Faculty of Medicine, Alberta, Canada.

Lipids
|January 1, 1993
PubMed

Insights

Low-molecular weight heparin (LMWH) effectively releases lipoprotein lipase (LPL) from cardiac myocytes. This suggests LMWH is more efficient than unfractionated heparin in displacing cell-surface bound LPL.

Area of Science:

  • Biochemistry
  • Cardiology
  • Pharmacology

Background:

  • Cardiac myocytes possess cell-surface heparan sulfate proteoglycans that bind lipoprotein lipase (LPL).
  • Understanding LPL release mechanisms is crucial for cardiac metabolism and lipid regulation.

Purpose of the Study:

  • To investigate the effect of low-molecular weight heparin (LMWH) on LPL release from cardiac myocytes.
  • To compare the efficacy of LMWH with unfractionated heparin (UFH) and decavanadate in LPL displacement.

Main Methods:

  • Incubation of rat cardiac myocytes (control and diabetic) with varying concentrations of LMWH, UFH, and decavanadate.
  • Measurement of released lipoprotein lipase (LPL) activity in the incubation medium.
  • Time-course analysis of LPL release.

Main Results:

  • LMWH induced a concentration-dependent release of LPL activity from cardiac myocytes.
  • LMWH (10 µg/mL) significantly increased LPL release compared to UFH (10 and 30 µg/mL) and decavanadate (1 mM) at both 10 and 30 min.
  • LMWH demonstrated greater LPL releasing capacity than UFH even after a short incubation period (10 min).

Conclusions:

  • LMWH is a potent agent for releasing LPL from cardiac myocytes.
  • LMWH appears more effective than UFH in displacing LPL from heparan sulfate proteoglycan binding sites on cardiac myocytes.
  • These findings highlight LMWH's potential in modulating cardiac LPL activity.

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