Angiopoietin-like protein 4 inhibition of lipoprotein lipase: evidence for reversible complex formation.

@article{Lafferty2013AngiopoietinlikeP4,
  title={Angiopoietin-like protein 4 inhibition of lipoprotein lipase: evidence for reversible complex formation.},
  author={Michael J. Lafferty and Kira C. Bradford and Dorothy Erie and Saskia B Neher},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 40},
  pages={28524-34}
}
Elevated triglycerides are associated with an increased risk of cardiovascular disease, and lipoprotein lipase (LPL) is the rate-limiting enzyme for the hydrolysis of triglycerides from circulating lipoproteins. The N-terminal domain of angiopoietin-like protein 4 (ANGPTL4) inhibits LPL activity. ANGPTL4 was previously described as an unfolding molecular chaperone of LPL that catalytically converts active LPL dimers into inactive monomers. Our studies show that ANGPTL4 is more accurately… CONTINUE READING

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