Angptl8 Antibody

1. ANGPTL8 has a functional LPL inhibitory motif, but only inhibits LPL and increases plasma TG levels in mice in the presence of ANGPTL3 PMID: 28413163
2. knock-down of Angptl8 in adipocytes suggests that the protein acts to inhibit intracellular lipolysis, analogous to its activity in the circulation. Depletion of Angptl8 results in an altered cellular phospholipid composition. The findings identify Angptl8 as a central insulin-regulated controller of adipocyte lipid metabolism. PMID: 28528274
3. The high levels of ANGPTL8 found in fetal life together with its relationship with newborn adiposity and brown adipose tissue point to ANGPTL8 as a potential new player in the modulation of the thermogenic machinery during the fetal-neonatal transition. PMID: 27469268
4. Obesity is associated with increased betatrophin suppression after an oral glucose load; this response appears to be driven by hyperglycemia. Data suggest that insulin or low glucose (as in hypoglycemia) increases betatrophin expression/secretion in adipocytes (3T3-L1 cells here); elevation of glucose levels blunts this effect. PMID: 27459526
5. circulating betatrophin is increased in mice and humans with NAFLD and its expression was induced by endoplasmic reticulum stress in hepatocytes PMID: 27045862
6. The expression of betatrophin is upregulated in the liver, white adipose tissue (WAT) and brown adipose tissue in obese hyperinsulinemic type 2 diabetes but decreased in WAT in hypoinsulinemic type 1 diabetes, suggesting its positive correlation with body weight and plasma insulin but not blood glucose. PMID: 27097546
7. This model suggests a general mechanism by which TAG trafficking is coordinated by lipasin, Angptl3 and Angptl4 at different nutritional statuses. PMID: 26687026
8. ANGPTL8 is a stress-response protein that down-regulates expression of ATGL. PMID: 26569053
9. no substantial change in beta cell replication, mass or glucose homeostasis was observed following ANGPTL8 overexpression PMID: 25917759
10. A monoclonal antibody against Angptl8, a feeding-induced hepatokine, lowers serum triglyceride levels when injected into mice. Angptl8 inhibits the activity of lipoprotein lipase in cardiac and skeletal muscle, but not in white adipose tissue. Therefore, Angptl8 acts, at least in part, in an endocrine manner, and its inhibition has therapeutical potential in treating hypertriglyceridemia. PMID: 26687026
11. ANGPTL8 is not required for beta cell function or the compensatory beta cell growth response to insulin resistance, overexpression of ANGPTL8 does not increase beta cell area nor improve glycemic control, and ANGPTL8 regulates plasma triglyceride levels. PMID: 25417115
12. Mice lacking ANGPTL8 (Betatrophin) manifest disrupted triglyceride metabolism without impaired glucose homeostasis. PMID: 24043787
13. These results suggest Lipasin and some ANGPTLs play distinct physiological roles in mediating thermogenesis and energy homeostasis. PMID: 23261442
14. Lipasin is a novel but atypical member of the angiopoietin-like protein family. PMID: 23261442
15. Lipasin is thus a novel nutritionally-regulated liver-enriched factor that plays a role in lipid metabolism. PMID: 22809513
16. RIFL is an important new regulator of lipid metabolism. PMID: 22569073

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KEGG: mmu:624219

STRING: 10090.ENSMUSP00000058951

UniGene: Mm.440264