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Angiopoietin-like 4 Modifies the Interactions between Lipoprotein Lipase and Its Endothelial Cell Transporter GPIHBP1
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In the citing paper
“LPL bound to GPIHBP1 is largely protected from ANGPTL4 (51, 52, 60, 98).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [51]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“In the years since, multiple laboratories have confirmed the ability of ANGPTL4 to inhibit LPL (49–55).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [51]
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In the citing paper
“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 [51]
In the citing paper
“In fact, several studies have found that vascular LPL, bound to its receptor GPIHBP1, is protected from ANGPTL4 inhibition (51, 52, 60).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [51]
In the citing paper
“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 [51]
In the citing paper
“Several studies have indicated that ANGPTL4 catalytically inactivates LPL (49, 51, 52, 97, 98).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [51]
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Citations
Cites
Köster, A., Chao, Y. B., Mosior, M., Ford, A., Gonzalez-DeWhitt, P. A., Hale, J. E., Li, D., Qiu, Y., Fraser, C. C., Yang, D. D., et al. (2005) · Endocrinology · doi:10.1210/en.2005-0476 · Cited by 427 · cited 1×
“Increasing plasma levels of ANGPTL4, either by overexpression in the liver or by direct injection of ANGPTL4 into the bloodstream, can reduce plasma triglycerides in mice (21, 45), suggesting that ANGPTL4 can act on the LPL-GPIHBP1 complexes in the vasculature.”
BackgroundMutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia.
Olivecrona, G., Ehrenborg, E., Semb, H., Makoveichuk, E., Lindberg, A., Hayden, M. R., Gin, P., Davies, B. S. J., Weinstein, M. M., Fong, L. G., et al. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m002717 · Cited by 118
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Flagged first, then by citations
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Cited by
Sorted by citations
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Wu, S. A., Kersten, S., & Qi, L. (2021) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2020.11.005 · Cited by 225
Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8
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Self-citationTriglyceride-rich lipoproteins and remnants: targets for therapy?
Dallinga-Thie, G. M., Kroon, J., Borén, J., & Chapman, M. J. (2016) · Current Cardiology Reports · doi:10.1007/s11886-016-0745-6 · Cited by 90
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
Ingerslev, B., Hansen, J. S., Hoffmann, C., Clemmesen, J. O., Secher, N. H., Scheler, M., Hrabĕ de Angelis, M., Häring, H. U., Pedersen, B. K., Weigert, C., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.06.018 · Cited by 61
“ANGPTL4 inhibits LPL activity on the surface of capillary endothelial cells within muscle tissue [37], and interactions between ANGPTL4 and LPL were also observed intracellularly [6,12].”
Background
Metadata
- Authors
- Chi, X., Shetty, S. K., Shows, H. W., Hjelmaas, A. J., Malcolm, E. K., & Davies, B. S. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2015-05
- Volume
- 290
- Issue
- 19
- Pages
- 11865-11877
- ISSN
- 0021-9258
- Cited by
- 63
- References
- 2
- Language
- en
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