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Article

Relationship between structure and biochemical phenotype of lecithin:cholesterol acyltransferase (LCAT) mutants causing fish-eye disease.

Journal of lipid research - 1 May 2000

Vanloo B, Peelman F, Deschuymere K, Taveirne J, Verhee A, Gouyette C, Labeur C, Vandekerckhove J, Tavernier J, Rosseneu M

Abstract excerpt

In order to test the hypothesis that fish-eye disease (FED) is due to a deficient activation of lecithin:cholesterol acyltransferase (LCAT) by its co-factor apolipoprotein (apo) A-I, we overexpressed the natural mutants T123I, N131D, N391S, and other engineered mutants in Cos-1 cells. Esterase activity was measured on a monomeric phospholipid enelogue, phospholipase A(2) activity was measured on reconstituted...

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Identifiers

PMID: 10787436

Genes

LCAT

Variants

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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Relationship between structure and biochemical phenotype of lecithin:cholesterol acyltransferase (LCAT) mutants causing fish-eye disease.PMID 10787436Read ↗

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Compound heterozygosity (G71R/R140H) in the lecithin:cholesterol acyltransferase (LCAT) gene results in an intermediate phenotype between LCAT-deficiency and fish-eye disease.Semantic proximity Read ↗

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The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes.Semantic proximity Read ↗

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