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Article

Endothelial-derived lipoprotein lipase is bound to postprandial triglyceride-rich lipoproteins and mediates their hepatic clearance in vivo.

Journal of molecular medicine (Berlin, Germany) - 1 Sept 2002

Heeren Joerg, Niemeier Andreas, Merkel Martin, Beisiegel Ulrike

Abstract excerpt

Lipoprotein lipase (LPL) is the key enzyme in the intravascular hydrolysis of triglyceride-rich lipoproteins (TRL). Furthermore, it has been shown that inactive LPL can mediate cellular binding and uptake of TRL in vitro. This study investigated whether LPL is bound to postprandial human TRL in vivo, and whether it plays a role in the hepatic clearance of these particles independent of its catalytic activity. LPL...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 12226739
DOI: 10.1007/s00109-002-0351-5

Genes

LPL

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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