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Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1

25 Apr 2011

Abstract excerpt

GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells, shuttles lipoprotein lipase (LPL) from subendothelial spaces to the capillary lumen. An absence of GPIHBP1 prevents the entry of LPL into capillaries, blocking LPL-mediated triglyceride hydrolysis and leading to markedly elevated triglyceride levels in the plasma (i.e., chylomicronemia). Earlier studies have established that...

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PMID: 21518912
DOI: 10.1073/pnas.1100992108

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Related research

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Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1PMID 21518912Read ↗

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

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Equivalent binding of wild-type lipoprotein lipase (LPL) and S447X-LPL to GPIHBP1, the endothelial cell LPL transporter.Semantic proximity Read ↗

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Mutating a conserved cysteine in GPIHBP1 reduces amounts of GPIHBP1 in capillaries and abolishes LPL binding.Semantic proximity Read ↗

Deletion of GPIHBP1 causing severe chylomicronemia.Semantic proximity Read ↗

Novel combined GPIHBP1 mutations in a patient with hypertriglyceridemia associated with CAD.Semantic proximity Read ↗

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

Chylomicronemia from GPIHBP1 autoantibodiesSemantic proximity Read ↗

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