Publications by authors named "Ivory J Mintah"
Article Synopsis
- Recent studies have linked specific genetic variants in the MARC1 gene to lower liver fat, reduced liver enzymes, and a lower risk of cirrhosis in humans.
- Researchers confirmed these findings in a large group of diverse individuals and found new rare variants with similar effects.
- However, experiments in mice showed that deleting Marc1 did not protect against liver issues, suggesting that a related gene, Marc2, is more important for liver function in mice than MARC1 is in humans.
Activin E-ACVR1C cross talk controls energy storage via suppression of adipose lipolysis in mice.
Proc Natl Acad Sci U S A
August 2023
Article Synopsis
- - Body fat distribution is influenced by genetics and rare variants of Inhibin beta E (activin E) can lower waist-to-hip ratios and protect against type 2 diabetes.
- - Activin E plays a crucial role in regulating energy storage in fat tissue by inhibiting fat breakdown and contributing to the enlargement of fat cells (adipocytes) in mice.
- - The research shows that activin E functions through ACVR1C signaling, and its absence leads to healthier fat metabolism and reduced fat storage, highlighting its role in maintaining fat mass during fasting, which is problematic in obesity.
Angiopoietin-like protein (ANGPTL)3 regulates plasma lipids by inhibiting LPL and endothelial lipase (EL). ANGPTL3 inactivation lowers LDL-C independently of the classical LDLR-mediated pathway and represents a promising therapeutic approach for individuals with homozygous familial hypercholesterolemia due to mutations. Yet, how ANGPTL3 regulates LDL-C levels is unknown.
View Article and Find Full Text PDFAngiopoietin-like (ANGPTL)3 and ANGPTL8 are secreted proteins and inhibitors of LPL-mediated plasma triglyceride (TG) clearance. It is unclear how these two ANGPTL proteins interact to regulate LPL activity. ANGPTL3 inhibits LPL activity and increases serum TG independent of ANGPTL8.
View Article and Find Full Text PDFAngiopoietin-like protein (ANGPTL)8 is a negative regulator of lipoprotein lipase-mediated plasma triglyceride (TG) clearance. In this study, we describe a fully human monoclonal antibody (REGN3776) that binds monkey and human ANGPTL8 with high affinity. Inhibition of ANGPTL8 with REGN3776 in humanized ANGPTL8 mice decreased plasma TGs and increased lipoprotein lipase activity.
View Article and Find Full Text PDFAngiopoietin-like protein 3 (ANGPTL3) is a circulating protein synthesized exclusively in the liver that inhibits LPL and endothelial lipase (EL), enzymes that hydrolyze TGs and phospholipids in plasma lipoproteins. Here we describe the development and testing of a fully human monoclonal antibody (REGN1500) that binds ANGPTL3 with high affinity. REGN1500 reversed ANGPTL3-induced inhibition of LPL activity in vitro.
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