# Mechanism of Intracellular ANGPTL3 and ANGPTL8 Trafficking

> **NIH NIH F31** · UNIV OF NORTH CAROLINA CHAPEL HILL · 2024 · $40,064

## Abstract

Abstract
Lipids circulate in the blood in lipoproteins including chylomicrons and very low-density lipoproteins (VLDLs).
Lipoprotein Lipase (LPL) is the main enzyme that hydrolyzes the triglycerides from circulating lipoproteins into
free fatty acids that can be taken up by cells. Without LPL, dangerously high levels of lipoproteins circulate in
the blood, which can lead to cardiovascular disease, amongst other diseases. LPL inhibitors, known as
angiopoietin-like (ANGPTL) proteins have key roles in the regulation of lipid metabolism. ANGPTL3 is a potent
inhibitor of LPL. ANGPTL8 can form a complex with ANGPTL3 which results in even greater inhibition of LPL.
ANGPTL8 is only found in the bloodstream in complex with ANGPTL3. However, where this complex forms, and
why ANGPTL8 requires ANGPTL3 for secretion remains a mystery. This proposal aims to understand why
ANGPTL8 is unstable when it is not in a complex with ANGPTL3, as well as visualizing the ANGPTL3/8 complex
trafficking dynamics.

## Key facts

- **NIH application ID:** 10998676
- **Project number:** 1F31HL176142-01
- **Recipient organization:** UNIV OF NORTH CAROLINA CHAPEL HILL
- **Principal Investigator:** Christina So
- **Activity code:** F31 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $40,064
- **Award type:** 1
- **Project period:** 2024-09-30 → 2026-09-29

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10998676

## Citation

> US National Institutes of Health, RePORTER application 10998676, Mechanism of Intracellular ANGPTL3 and ANGPTL8 Trafficking (1F31HL176142-01). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/10998676. Licensed CC0.

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