ABSTRACT
Befi tting its classifi cation as adipokine, Angptl4 is produced by various adipose depots and is specifi cally well expressed in mouse adipocytes (Kersten et al. 2000, Yoon et al. 2000). Additionally, Angptl4 is expressed in numerous other organs and cell types including liver, muscle, intestine, and the endothelium. Angptl4 is part of a larger family of angiopoietins and angiopoietin-like proteins that share structural and functional similarities (Fig. 1). Many of these proteins, including Angptl4, undergo proteolytic processing to yield N-and C-terminal fragments via proprotein convertases (Chomel et al. 2009, Ge et al. 2004a, 2004b, Mandard et al. 2004). Moreover, Angptl4 forms higher order oligomeric structures via intermolecular disulfi de bonds and hydrophobic interactions.
