Lipoprotein lipase-mediated selective uptake from low density lipoprotein requires cell surface proteoglycans and is independent of scavenger receptor class B type 1.

@article{Seo2000LipoproteinLS,
  title={Lipoprotein lipase-mediated selective uptake from low density lipoprotein requires cell surface proteoglycans and is independent of scavenger receptor class B type 1.},
  author={Toru Seo and Maysoon Al-Haideri and E Treskova and Tilla S. Worgall and Yuko Kako and Ira J Goldberg and Richard J. Deckelbaum},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 39},
  pages={30355-62}
}
Lipoprotein lipase (LpL) hydrolyzes chylomicron and very low density lipoprotein triglycerides to provide fatty acids to tissues. Aside from its lipolytic activity, LpL promotes lipoprotein uptake by increasing the association of these particles with cell surfaces allowing for the internalization by receptors and proteoglycans. Recent studies also indicate that LpL stimulates selective uptake of lipids from high density lipoprotein (HDL) and very low density lipoprotein. To study whether LpL… CONTINUE READING
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