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Article

GPIHBP1 autoantibodies in a patient with unexplained chylomicronemia.

Journal of clinical lipidology - 1 Jan 2000

Hu Xuchen, Dallinga-Thie Geesje M, Hovingh G Kees, Chang Sandy Y, Sandoval Norma P, Dang Tiffany Ly P, Fukamachi Isamu, Miyashita Kazuya, Nakajima Katsuyuki, Murakami Masami, Fong Loren G, Ploug Michael, Young Stephen G, Beigneux Anne P

Abstract excerpt

BACKGROUND: GPIHBP1, a glycolipid-anchored protein of capillary endothelial cells, binds lipoprotein lipase (LPL) in the interstitial spaces and transports it to the capillary lumen. GPIHBP1 deficiency prevents LPL from reaching the capillary lumen, resulting in low intravascular LPL levels, impaired intravascular triglyceride processing, and severe hypertriglyceridemia (chylomicronemia). A recent study showed...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to LPL gene

Share to Hyperlipoproteinemia Type I

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Share to Receptors, Lipoprotein

Source

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Identifiers

PMID: 28666713
DOI: 10.1016/j.jacl.2017.05.017
PMCID: PMC5568906

Genes

GPIHBP1
LPL

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.

Related research

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GPIHBP1 autoantibodies in a patient with unexplained chylomicronemia.PMID 28666713Read ↗

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GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons.Semantic proximity Read ↗

The GPIHBP1-LPL complex and its role in plasma triglyceride metabolism: Insights into chylomicronemia.Semantic proximity Read ↗

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A novel mutation in GPIHBP1 causes familial chylomicronemia syndrome.Semantic proximity Read ↗

A novel homozygous variant in GPIHBP1: A case series of familial chylomicronemia syndrome from Colombia.Semantic proximity Read ↗

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<i>GPIHBP1</i> Missense Mutations Often Cause Multimerization of GPIHBP1 and Thereby Prevent Lipoprotein Lipase BindingSemantic proximity Read ↗

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