Description

Genorise Recombinant Bovine ANGPTL3 Protein Summary

Alternative names for ANGPTL3: Angiopoietin-like 3

Alternative name for bovine: Cattle, cow, bull

Product Specifications

Background: 

Angiopoietin-like 3 ( ANGPTL3) is a protein that is encoded by the ANGPTL3 gene^[1] and a member of the angiopoietin-like family of secreted factors. It is expressed predominantly in the liver, and has the characteristic structure of angiopoietins, consisting of a signal peptide, N-terminal coiled-coil domain, and the C-terminal fibrinogen (FBN)-like domain. The FBN-like domain in ANGPTL3 protein was shown to bind alpha-5/beta-3 integrins, and this binding induced endothelial cell adhesion and migration. ANGPTL3 may also play a role in the regulation of angiogenesis. Angptl3 also acts as dual inhibitor of lipoprotein lipase (LPL) and endothelial lipase (EL),^[2] thereby increasing plasma triglyceride, LDL cholesterol and HDL cholesterol in mice and humans.^[2] ANGPTL3 inhibits endothelial lipase hydrolysis of HDL-phospholipid (PL), thereby increasing HDL-PL levels. Circulating PL-rich HDL particles have high cholesterol efflux abilities. Angptl3 plays a major role in promoting uptake of circulating triglycerides into white adipose tissue in the fed state,^[3] likely through activation by Angptl8, a feeding-induced hepatokine,^[4][5] to inhibit postprandial LPL activity in cardiac and skeletal muscles,^[6] as suggested by the ANGPTL3-4-8 model.^[7] ANGPTL3 is a determinant factor of HDL level and positively correlates with plasma HDL cholesterol. In humans with genetic loss-of-function variants in one copy of ANGPTL3, the serum LDL-C levels are reduced. In those with loss-of-function variants in both copies of ANGPTL3, low LDL-C, low HDL-C, and low triglycerides are seen (“familial combined hypolipidemia“).^[8]

References

1. Conklin D, et al. (1999). Genomics. 62 (3): 477–82.
2. Tikka A, Jauhiainen M (2016). Endocrine. 52 (2): 187–93.
3. Wang Y, et al. (2015). Proc Natl Acad Sci USA. 112 (37): 11630–5.
4. Zhang R (2012). Biochemical and Biophysical Research Communications. 424 (4): 786–92.
5. Ren G, et al. (2012). Am J Physiol Endocrinology and Metabolism. 303 (3): E334-51.
6. Fu Z, et al. (2015). Scientific Reports. 5: 18502. doi:1038/srep18502.
7. Zhang R (2016). Open Biology. 6 (4): 150272. doi:1098/rsob.150272.
8. Musunuru K, et al. (2010). The New England Journal of Medicine. 363 (23): 2220–7.

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