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Article

Biochemical Analysis of the Lipoprotein Lipase Truncation Variant, LPLS447X, Reveals Increased Lipoprotein Uptake.

Biochemistry - 24 Jan 2017

Hayne Cassandra K, Lafferty Michael J, Eglinger Brian J, Kane John P, Neher Saskia B

Abstract excerpt

Lipoprotein lipase (LPL) is responsible for the hydrolysis of triglycerides from circulating lipoproteins. Whereas most identified mutations in the LPL gene are deleterious, one mutation, LPLS447X, causes a gain of function. This mutation truncates two amino acids from LPL's C-terminus. Carriers of LPLS447X have decreased VLDL levels and increased HDL levels, a cardioprotective phenotype. LPLS447X is used in...

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Share to Angiopoietins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Open in PubMed Open full text

Identifiers

PMID: 27984852
DOI: 10.1021/acs.biochem.6b00945
PMCID: PMC5848218

Genes

LPL
ANGPTL4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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