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Genetic Variation in ANGPTL4 Provides Insights into Protein Processing and Function
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The 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 [89]
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 [8]
Oligomerization appears to be required for LPL inhibition.
“Oligomerization appears to be required for LPL inhibition (22, 89),”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [89]
When cleaved, the C-terminal domain dissociates to monomers, but the N-terminal region can remain oligomerized.
“When cleaved, the C-terminal domain dissociates to monomers, but the N-terminal region can remain oligomerized (89, 96).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [89]
The N-terminal coiled-coil domain of ANGPTL4 mediates the formation of oligomers, mostly dimers and tetramers.
“The N-terminal coiled-coil domain of ANGPTL4 mediates the formation of oligomers, mostly dimers and tetramers (22, 89, 96).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [89]
Proteolytic cleavage is known to increase the ability of ANGPTL4 to inhibit LPL.
“As proteolytic cleavage is known to increase the ability of ANGPTL4 to inhibit LPL (51, 89, 90),”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [89]
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Cites
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Cited by
Sorted by citations
Coding Variation in ANGPTL4, LPL, and SVEP1 and the Risk of Coronary Disease
Myocardial Infarction Genetics and CARDIoGRAM Exome Consortia Investigators (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1507652 · Cited by 493
Inactivating Variants in ANGPTL4 and Risk of Coronary Artery Disease
Dewey, F. E., Gusarova, V., O’Dushlaine, C., Gottesman, O., Trejos, J., Hunt, C., Van Hout, C. V., Habegger, L., Buckler, D., Lai, K.-M. V., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1510926 · Cited by 497
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
Self-citationRegulation 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 Protein 4 Inhibition of Lipoprotein Lipase
Lafferty, M. J., Bradford, K. C., Erie, D. A., & Neher, S. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497602 · Cited by 88
Pellegata, N. S., Berriel Diaz, M., Rohm, M., & Herzig, S. (2022) · Cancer and Metastasis Reviews · doi:10.1007/s10555-022-10058-y · Cited by 33
Vienberg, S. G., Kleinridders, A., Suzuki, R., & Kahn, C. R. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2014.11.003 · Cited by 33
Angiopoietin-like protein 4: a therapeutic target for triglycerides and coronary disease?
Olshan, D. S., & Rader, D. J. (2018) · Journal of Clinical Lipidology · doi:10.1016/j.jacl.2018.01.012 · Cited by 30
Impact of loss-of-function in angiopoietin-like 4 on the human phenome
Gagnon, E., Bourgault, J., Gobeil, É., Thériault, S., & Arsenault, B. J. (2024) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2024.117558 · Cited by 17
Metadata
- Authors
- Yin, W., Romeo, S., Chang, S., Grishin, N. V., Hobbs, H. H., & Cohen, J. C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 284
- Issue
- 19
- Pages
- 13213-13222
- ISSN
- 0021-9258
- PMC
- PMC2676053
- Cited by
- 129
- References
- 1
- Language
- en
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