[Durgical](https://durgical.com/en/) › [DurgiPedia](https://durgical.com/en/durgipedia/) › [Biochemistry](https://durgical.com/en/biochemistry/) › Lipoprotein lipase (LPL)

[Biochemistry](https://durgical.com/en/biochemistry/) · Enzyme

# Lipoprotein lipase (LPL)

Lipoprotein lipase, anchored in capillaries, cuts the triglycerides of chylomicrons and VLDL so muscle and fat can take up the fatty acids.

Updated 2026-11-01

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## Key facts

- Hydrolyses chylomicron and VLDL triglycerides to free fatty acids and monoacylglycerol.
- Adipose tissue, muscle and heart make it; it works on the luminal face of the endothelium, held by GPIHBP1.
- ApoC-II activates it; ApoC-III and ANGPTL3, 4 and 8 inhibit it.
- Insulin raises it in adipose tissue after meals; in fasting it prevails in muscle and heart.
- Heparin releases it from the endothelium into the blood (post-heparin activity).

**Also called**
LPL

**EC number**
[3.1.1.34](https://www.enzyme-database.org/query.php?ec=3.1.1.34)

**Genes**
LPL

**Structure (PDB)**
[6E7K](https://www.rcsb.org/structure/6E7K)

## Structure

- A 475-residue protein with a catalytic domain (Ser–Asp–His triad) and a lipid-binding C-terminal domain.
- Structure 6E7K shows human LPL bound to GPIHBP1, its endothelial transporter and anchor.

## Regulation

- Insulin increases adipose LPL.
- ApoC-II activates it; ApoC-III and ANGPTL3, 4 and 8 inhibit it.
- In fasting, ANGPTL4 turns it off in adipose tissue and fat is routed to muscle.

## Inhibitors and toxins

- Physiological inhibitors: ApoC-III, ANGPTL3, ANGPTL4
- Drugs against ApoC-III or ANGPTL3 free LPL from these brakes and lower triglycerides.

## Clinical notes

- Its deficiency, or that of ApoC-II, GPIHBP1, LMF1 or ApoA-V, causes familial chylomicronaemia syndrome: very high triglycerides and pancreatitis.
- Poorly controlled diabetes lowers LPL and raises triglycerides.
- Fibrates activate PPAR-α, which increases LPL and lowers ApoC-III.

## Related conditions

- [Familial chylomicronemia syndrome (lipoprotein lipase deficiency)](https://durgical.com/en/conditions/familial-chylomicronemia-syndrome/)
- [Acute pancreatitis](https://durgical.com/en/conditions/acute-pancreatitis/)
- [Atherosclerosis and dyslipidaemia](https://durgical.com/en/conditions/atherosclerosis-and-dyslipidaemia/)
- [Type 2 diabetes mellitus](https://durgical.com/en/conditions/type-2-diabetes-mellitus/)

## Related

- [Chylomicron](https://durgical.com/en/biochemistry/topics/chylomicron/)
- [VLDL (very-low-density lipoprotein)](https://durgical.com/en/biochemistry/topics/vldl/)
- [Lipoprotein metabolism](https://durgical.com/en/biochemistry/topics/lipoprotein-metabolism/)
- [Apolipoprotein B (ApoB-100 and ApoB-48)](https://durgical.com/en/biochemistry/enzymes/apolipoprotein-b/)

## Test yourself

Think of the answer, then tap the question to see it.

## Which apolipoprotein activates lipoprotein lipase?

ApoC-II, which chylomicrons and VLDL receive from HDL.

## Where does LPL act?

On the luminal surface of capillaries in adipose tissue, muscle and heart, anchored by GPIHBP1.

## How does insulin favour fat storage through LPL?

It raises adipose LPL after meals, so dietary fatty acids go into fat stores.

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Educational information, not medical advice. For any symptom, see a health professional.

Sources: [LPL: Lipoprotein lipase (human)](https://rest.uniprot.org/uniprotkb/P06858.txt) (UniProt, 2026); [LPL gene: MedlinePlus Genetics](https://medlineplus.gov/genetics/gene/lpl/) (MedlinePlus, US National Library of Medicine, 2026); [6E7K: Structure of the lipoprotein lipase GPIHBP1 complex that mediates plasma triglyceride hydrolysis](https://www.rcsb.org/structure/6E7K) (RCSB Protein Data Bank, 2026); [Plasma lipoprotein remodeling (R-HSA-8963899)](https://reactome.org/PathwayBrowser/#/R-HSA-8963899) (Reactome, 2026).

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Representative model, for educational purposes only.

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Source: https://durgical.com/en/biochemistry/enzymes/lipoprotein-lipase/
License: CC BY 4.0 (https://creativecommons.org/licenses/by/4.0/). Cite as: DurgiPedia (durgical.com), https://durgical.com/en/biochemistry/enzymes/lipoprotein-lipase/