Description
General description
Research area: Cell Signaling
Lipoprotein Lipase (LPL) from bovine milk is a glycoprotein. It exists as a homodimer and comprises two N-linked oligosaccharides. It is heat-labile.Lipoprotein lipase is an enzyme found on the surface of vascular endothelial cells, where it is anchored to capillary walls. It is mainly present in adipose tissue, heart, and muscle tissue. It is synthesized by extrahepatic tissues, particularly adipocytes, and the gene encoding the protein is situated on chromosome 8p22.
Application
Lipoprotein Lipase from bovine milk has been used:
as a supplement to test its effect on DiI (1,1′-dioctadecyl-3,3,3′-tetramethyl-indocarbocyanine perchlorate)- very-low-density lipoprotein (VLDL) uptake in breast cancer MDA-MB-231 cells.
to treat human brain microvascular endothelial cells (HBMECs) for the lipolysis of triglyceride-rich lipoproteins (TGRL).
to test its effect on gene expression in normal human astrocytes.
in primary hepatocyte isolation and lipoprotein binding to identify Sulf2 inhibition in T2DM mice for improving diabetic dyslipidemia.
in transforming growth factor-beta (TGF-β1) immunoassay to test if the TGF-β signaling system regulates the up-regulation and activation of activating transcription factor 3 (ATF3) in human aortic endothelial cells (HAEC) induced by lipolysis products.
in human TGRL isolation.
in in vitro lipolysis assay with HSPG-bound LPL, to investigate the effect of human apoE2 (Lys146→Gln) on lipoprotein metabolism.
in hydrolysis of triglycerides.
in developing in vitro model of gastrointestinal digestion to investigate the effects of chlorophyll on lipid digestion.
Biochem/physiol Actions
Lipoprotein Lipase (LPL) from bovine milk contributes to maximal lipolytic activity. It associates with casein micelle. LPL regulates triglyceride utilization and displays positional specificity. Lipases, in general, catalyzes the lipolysis of triglycerides especially at the fatty acid in sn-1 and sn-3 positions of the triglyceride.LPL is known to significantly impact the advancement of atherosclerosis. Studies have indicated that advanced atherosclerosis patients display increased LPL mass and activity in their post-heparin plasma.
Physical form
Suspension in 3.8 M ammonium sulfate, 0.02 M Tris HCl, pH 8.0
Preparation Note
Affinity purified
Other Notes
One unit will release 1.0 nmole of p-nitrophenol per min at pH 7.2 at 37 °C using p-nitrophenyl butyrate as substrate.
