 In this study, researchers examined the effects of albumin, a major protein component in blood plasma on the stability, oligomerization, and ligand interactions of lipoprotein lipase, LPL. They found that albumin binds to LPL with enough affinity to form a complex in both the interstitial space and capillaries. This binding caused LPL to form oligomers, which were structurally different than those formed when heparin was present. Albumin also prevented LPL from being inactivated by its physiological regulator angiopoietin like protein 4. These findings suggest that the interaction between albumin and LPL may play a role in determining whether LPL follows irreversible inactivation and aggregation or reversible oligomer formation, which could have implications for the therapeutic use of LPL. This article was authored by Robert Ristie, Catherine H. Gunn, Christopher Heisz-Hommick, and others. We are article.tv, links in the description below.