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On the mechanism of angiopoietin-like protein 8 for control of lipoprotein lipase activity
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More recent studies have shown that ANGPTL3 forms a complex with ANGPTL8 and that this complex is most likely the physiologically relevant LPL inhibitor.
“As discussed below, more recent studies have shown that ANGPTL3 forms of complex with ANGPTL8 and that this complex is most likely the physiologically relevant LPL inhibitor (19, 54, 115, 137, 138).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [138]
The Discussion (page unavailable) reports ANGPTL3–ANGPTL8 complex formation and proposes that the complex inactivates LPL in the fed state. But it also says ANGPTL3 can inhibit LPL on its own at concentrations found in human plasma. The paper therefore supports a physiological role for the complex, not the stronger implication that it is the physiologically relevant inhibitor rather than ANGPTL3 alone. (LLM, conf=0.84)
Experimental — accuracy not yet measuredANGPTL4-ANGPTL8 complexes are substantially poorer at inhibiting LPL than ANGPTL4 alone.
“ANGPTL4-ANGPTL8 complexes are substantially poorer at inhibiting LPL than ANGPTL4 alone (39, 54, 138).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [138]
The specific inhibitory activity of ANGPTL4-ANGPTL8 complexes is greatly less than that of ANGPTL4 alone.
“both Chen et al. (54) and Kovrov et al. (138) found that the specific inhibitory activity of ANGPTL4-ANGPTL8 complexes was greatly less than that of ANGPTL4 alone.”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [138]
ANGPTL8 does not inhibit LPL on its own.
“Although ANGPTL8 was initially reported to inhibit LPL on its own (35), later studies found that this not to be the case (115, 137, 138).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [138]
Complex formation appears to require intracellular co-folding.
“and appears to require intracellular co-folding, as mixing ANGPTL3 and ANGPTL8 outside the cell does not result in complex formation (115, 138).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [138]
ANGPTL8 interacts directly with ANGPTL4.
“Recently, it has become clear that ANGPTL8 also interacts directly with ANGPTL4”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [138]
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Lipoprotein lipase and its regulators: an unfolding story
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
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
Metadata
- Authors
- Kovrov, O., Kristensen, K. K., Larsson, E., Ploug, M., & Olivecrona, G.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2019-04
- Volume
- 60
- Issue
- 4
- Pages
- 783-793
- ISSN
- 0022-2275
- Cited by
- 116
- References
- 4
- Language
- en
- Funders
- Swedish Research Council (2015-0292)
- Hjärt Lungfonden (20170465)
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