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Article

Rare loss-of-function mutations in ANGPTL family members contribute to plasma triglyceride levels in humans.

The Journal of clinical investigation - 1 Jan 2009

Romeo Stefano, Yin Wu, Kozlitina Julia, Pennacchio Len A, Boerwinkle Eric, Hobbs Helen H, Cohen Jonathan C

Abstract excerpt

The relative activity of lipoprotein lipase (LPL) in different tissues controls the partitioning of lipoprotein-derived fatty acids between sites of fat storage (adipose tissue) and oxidation (heart and skeletal muscle). Here we used a reverse genetic strategy to test the hypothesis that 4 angiopoietin-like proteins (ANGPTL3, -4, -5, and -6) play key roles in triglyceride (TG) metabolism in humans. We...

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Share to Amino Acid Sequence
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19075393
DOI: 10.1172/JCI37118
PMCID: PMC2613476

Genes

ANGPTL3
ANGPTL4
ANGPTL5
LPL
ANGPTL6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Rare loss-of-function mutations in ANGPTL family members contribute to plasma triglyceride levels in humans.PMID 19075393Read ↗

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Characterization of three kindreds with familial combined hypolipidemia caused by loss-of-function mutations of ANGPTL3.Semantic proximity Read ↗

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Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery diseaseSemantic proximity Read ↗

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