The encoded 22 kDa protein contains an N-terminal secretion signal and two coiled-coil domains and is a member of the angiopoietin-like <unk>  protein family. However, in contrast to other<unk> proteins,<unk>  lacks the C-terminal fibrinogen-like domain, and therefore it is an atypical member of the<unk> family. It shares with<unk>  and<unk>  the ability to inhibit the enzyme Lipoprotein lipase (LPL), and its hepatic overexpression causes elevation of circulating Triglyceride levels in mice. In mice<unk>  is secreted by the liver and by adipose tissue. Despite having elevated post-heparin plasma LPL activity, mice lacking<unk>  exhibit markedly decreased uptake of Very low-density lipoprotein-derived fatty acids into white adipose tissue (WAT). The defect in fatty acids uptake by WAT in<unk> -null mice is likely due to the enhanced fatty acid uptake by the heart and skeletal muscle, because of the elevated LPL activity in these two tissues, as suggested by the<unk> -4-8 model.<unk>  was proposed to increase the rate at which beta-cells undergo cell division. Injection of mice with<unk>  cDNA lowered blood sugar (i.e. hypoglycemia), presumably due to action at the pancreas. However, treatment of human islets with<unk>  is unable to increase beta-cell division. Furthermore, studies in<unk>  knock-out mice do not support a role of<unk>  in controlling beta cell growth, yet point to a clear role in regulating plasma triglyceride levels. Based on these studies, it is fairly safe to say that the notion that<unk>  promotes beta cell expansion is dead, which was made official by the retraction of the original paper. Deletion of<unk>  does not seem to impact glucose and insulin tolerance in mice.
ANGPTL8
SCALPEL
COCIR
OPCS-4
NLRP3
Limp
HVTN 702
IPrEx