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Angptl3 Deficiency Is Associated With Increased Insulin Sensitivity, Lipoprotein Lipase Activity, and Decreased Serum Free Fatty Acids
Abstract
Objective—: Angiopoietin-like 3 (Angptl3) is a regulator of lipoprotein metabolism at least by inhibiting lipoprotein lipase activity. Loss-of-function mutations in ANGPTL3 cause familial combined hypolipidemia through an unknown mechanism. Approach and Results—: We compared lipolytic activities, lipoprotein composition, and other lipid-related enzyme/lipid transfer proteins in carriers of the S17X loss-of-function mutation in ANGPTL3 and in age- and sex-matched noncarrier controls. Gel filtration analysis revealed a severely disturbed lipoprotein profile and a reduction in size and triglyceride content of very low density lipoprotein in homozygotes as compared with heterozygotes and noncarriers. S17X homozygotes had significantly higher lipoprotein lipase activity and mass in postheparin plasma, whereas heterozygotes showed no difference in these parameters when compared with noncarriers. No changes in hepatic lipase, endothelial lipase, paraoxonase 1, phospholipid transfer protein, and cholesterol ester transfer protein activities were associated with the S17X mutation. Plasma free fatty acid, insulin, glucose, and homeostatic model assessment of insulin resistance were significantly lower in homozygous subjects compared with heterozygotes and noncarriers subjects. Conclusions—: These results indicate that, although partial Angptl3 deficiency did not affect the activities of lipolytic enzymes, the complete absence of Angptl3 results in an increased lipoprotein lipase activity and mass and low circulating free fatty acid levels. This latter effect is probably because of decreased mobilization of free fatty acid from fat stores in human adipose tissue and may result in reduced hepatic very low density lipoprotein synthesis and secretion via attenuated hepatic free fatty acid supply. Altogether, Angptl3 may affect insulin sensitivity and play a role in modulating both lipid and glucose metabolism.
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In humans, loss of functional ANGPTL3 protein leads to decreased triglyceride levels.
“In humans, loss of functional ANGPTL3 protein also leads to decreased triglyceride levels (40, 108–110).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [110]
Loss of ANGPTL function can improve glucose homeostasis.
“Interestingly, there is evidence that loss of ANGPTL function can also improve glucose homeostasis (110, 163, 167).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [110]
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Metadata
- Authors
- Robciuc, M. R., Maranghi, M., Lahikainen, A., Rader, D., Bensadoun, A., Öörni, K., Metso, J., Minicocci, I., Ciociola, E., Ceci, F., Montali, A., Arca, M., Ehnholm, C., & Jauhiainen, M.
- Affiliations
- From the Public Health Genomics Unit, National Institute for Health and Welfare, Biomedicum, Helsinki, Finland (M.R.R., A.L., J. Metso, C.E., M. Jauhiainen); Wihuri Research Institute, Biomedicum, Helsinki, Finland (M.R.R., K.Ö.); Institute for Translational Medicine and Therapeutics, Perelman School of Medicine at the University of Pennsylvania, 11-125 Translational Research Center, Philadelphia, PA, (D.R.); Division of Nutritional Science, Cornell University, Ithaca, NY (A.B.); and Department of...
- Venue
- Arteriosclerosis, Thrombosis, and Vascular Biology
- Published
- 2013-07
- Volume
- 33
- Issue
- 7
- Pages
- 1706-1713
- ISSN
- 1079-5642
- 1524-4636
- Cited by
- 163
- References
- 5
- Language
- en
- Update notices
- correction (2013-07-01)
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