[10] It is most widely distributed in adipose, heart, and skeletal muscle tissue, as well as in lactating mammary glands.

The N-terminus domain has an α/β hydrolase fold, which is a globular structure containing a central β sheet surrounded by α helices.

[5][11][15] The ApoC-II binding site is currently unknown, but it is predicted that residues on both N-and C-terminal domains are necessary for this interaction to occur.

Importantly, LPL binding to the cell surface or receptors is not dependent on its catalytic activity.

The β5 loop folds back into the protein core, bringing one of the electrophiles of the oxyanion hole into position for lipolysis.

[5] In regard to kinetics, it is believed that release of product into circulation is the rate-limiting step in the reaction.

[11] LPL gene encodes lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue.

[34] Specifically, feeding induces ANGPTL8, activating the ANGPTL8–ANGPTL3 pathway, which inhibits LPL in cardiac and skeletal muscles, thereby making circulating triglycerides available for uptake by white adipose tissue, in which LPL activity is elevated owing to diminished ANGPTL4; the reverse is true during fasting, which suppresses ANGPTL8 but induces ANGPTL4, thereby directing triglycerides to muscles.

[34] Lipoprotein lipase deficiency leads to hypertriglyceridemia (elevated levels of triglycerides in the bloodstream).

[30] A high adipose tissue LPL response to a high-carbohydrate diet may predispose toward fat gain.

One study reported that subjects gained more body fat over the next four years if, after following a high-carbohydrate diet and partaking of a high-carbohydrate meal, they responded with an increase in adipose tissue LPL activity per adipocyte, or a decrease in skeletal muscle LPL activity per gram of tissue.

[39] In this haematological disorder, LPL appears to provide fatty acids as an energy source to malignant cells.

[23] LPL has been shown to be a ligand for LRP2, albeit at a lower affinity than for other receptors; however, most of the LPL-dependent VLDL degradation can be attributed to the LRP2 pathway.

Lipoprotein lipase is involved in lipid transport in the placentae of live bearing lizards (Pseudemoia entrecasteauxii).