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Differential regulation and properties of angiopoietin-like proteins 3 and 4
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Angptl4 prevents LPL dimerization and thereby prevents LPL activation.
“Angptl4 is primarily expressed in adipose tissue and liver, induced by fasting and secreted into the circulation [4], where it prevents LPL dimerization and thereby preventing LPL activation [5–8].”
From Differential effects of angiopoietin-like 4 in brain and muscle on regulation of lipoprotein lipase activity (2015) · cites this paper as [5]
The section on Angptl4’s coiled-coil domain reports that Angptl4 inhibits LPL activity in C2C12-LPL cells. It does not say that Angptl4 prevents LPL dimerization or establish that as the mechanism of inhibition. (LLM, conf=0.88)
Experimental — accuracy not yet measuredANGPTL3 oligomerizes, appearing to form trimers or hexamers, and oligomerization is mediated by the N-terminal domain.
“As with ANGPTL4, ANGPTL3 oligomerizes, appearing to form trimers or hexamers, and oligomerization is mediated by the N-terminal domain (72, 100).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [72]
The section on higher-order structures and Fig. 3C report that ANGPTL3 forms oligomeric complexes, supporting the oligomerization claim. The copy does not identify those complexes as trimers or hexamers, or establish that ANGPTL3 oligomerization is mediated by its N-terminal domain; its N-terminal disulfide-bond discussion concerns ANGPTL4. Page numbers are not available in the supplied copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe N-terminal region of ANGPTL4 is necessary and sufficient for LPL inhibition, and once cleaved from the fibrinogen-like domain, it inhibits LPL more efficiently than full-length ANGPTL4.
“Several studies have shown that not only is the N-terminal region of ANGPTL4 necessary and sufficient for LPL inhibition, but also that, once cleaved from the fibrinogen-like domain, the N-terminal region inhibits LPL more efficiently than full-length ANGPTL4 (49, 51, 72, 89, 90).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [72]
Disruption of ANGPTL3 primarily affects triglyceride metabolism and lipid partitioning in the fed state despite ANGPTL3 expression itself not being feeding induced.
“disruption of ANGPTL3 primarily effects triglyceride metabolism and lipid partitioning in the fed state despite the fact that ANGPTL3 expression itself is not feeding induced (72, 106).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [72]
Angptl4 is expressed in several tissues including liver, heart, intestine, and skeletal muscle.
“Although Angptl4 is most highly expressed in adipose, it is also expressed in several other tissues including liver, heart, intestine, and skeletal muscle (40, 46, 47, 72).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [72]
ANGPTL3 is expressed in and secreted from the liver and circulates in the bloodstream.
“ANGPTL3 is expressed in and secreted from the liver and circulates in the bloodstream (15, 40, 72, 103).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [72]
Circulating levels of ANGPTL3 are relatively constant across feeding states.
“circulating levels of ANGPTL3 are relatively constant across feeding states (72, 106, 115).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [72]
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Cites
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Cited by
Sorted by citations
The Role of Angiopoietin-Like Proteins in Angiogenesis and Metabolism
Hato, T., Tabata, M., & Oike, Y. (2008) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2007.10.003 · Cited by 351
Wang, Y., Quagliarini, F., Gusarova, V., Gromada, J., Valenzuela, D. M., Cohen, J. C., & Hobbs, H. H. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315292110 · Cited by 317
Angiopoietin-Like Proteins: A Comprehensive Look
Santulli, G. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00004 · Cited by 320
Angiopoietin-like 3 in lipoprotein metabolism
Kersten, S. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.119 · Cited by 220
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Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8
Sylvers-Davie, K. L., & Davies, B. S. J. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00195.2021 · Cited by 154
Angiopoietin-like 4 directs uptake of dietary fat away from adipose during fasting
Cushing, E. M., Chi, X., Sylvers, K. L., Shetty, S. K., Potthoff, M. J., & Davies, B. S. J. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.06.007 · Cited by 88
Cinkajzlová, A., Mráz, M., Lacinová, Z., Kloučková, J., Kaválková, P., Kratochvílová, H., Trachta, P., Křížová, J., Haluzíková, D., Škrha, J., et al. (2018) · Nutrition & Diabetes · doi:10.1038/s41387-018-0032-2 · Cited by 73
Effects of angiopoietin-like protein 3 deficiency on postprandial lipid and lipoprotein metabolism
Minicocci, I., Tikka, A., Poggiogalle, E., Metso, J., Montali, A., Ceci, F., Labbadia, G., Fontana, M., Di Costanzo, A., Maranghi, M., et al. (2016) · Journal of Lipid Research · doi:10.1194/jlr.p066183 · Cited by 56
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Metadata
- Authors
- Ge, H., Cha, J.-Y., Gopal, H., Harp, C., Yu, X., Repa, J. J., & Li, C.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 46
- Issue
- 7
- Pages
- 1484-1490
- ISSN
- 0022-2275
- Cited by
- 135
- References
- 1
- Language
- en
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