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Article

Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele.

Human genetics - 1 Jul 1990

Taramelli R, Pontoglio M, Candiani G, Ottolenghi S, Dieplinger H, Catapano A, Albers J, Vergani C, McLean J

Abstract excerpt

The enzyme, lecithin cholesterol acyltransferase (LCAT), is responsible for the esterification of plasma cholesterol mediating the transfer of an acyl group from lecithin to the 3-hydroxy group of cholesterol. Deficiency of the enzyme is a well-known syndrome with a widespread geographic occurrence. We have cloned an allele from a patient homozygous for the LCAT deficiency. The only change that we could detect is...

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Source

Identifiers

PMID: 2370048
DOI: 10.1007/BF00193195

Genes

LCAT

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.

Related research

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Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele.PMID 2370048Read ↗

Molecular analysis of a novel LCAT mutation (Gly179 → Arg) found in a patient with complete LCAT deficiency.Semantic proximity Read ↗

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Two different allelic mutations in a Finnish family with lecithin:cholesterol acyltransferase deficiency.Semantic proximity Read ↗

Lecithin: cholesterol acyltransferase deficiency: identification of two defective alleles in fibroblast cDNA.Semantic proximity Read ↗

High prevalence of mutations in LCAT in patients with low HDL cholesterol levels in The Netherlands: identification and characterization of eight novel mutations.Semantic proximity Read ↗

Deficiency of lecithin:cholesterol acyltransferase due to compound heterozygosity of two novel mutations (Gly33Arg and 30 bp ins) in the LCAT gene.Semantic proximity Read ↗

Classical LCAT deficiency resulting from a novel homozygous dinucleotide deletion in exon 4 of the human lecithin: cholesterol acyltransferase gene causing a frameshift and stop codon at residue 144.Semantic proximity Read ↗

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity.Semantic proximity Read ↗

Genetic and phenotypic heterogeneity in familial lecithin: cholesterol acyltransferase (LCAT) deficiency. Six newly identified defective alleles further contribute to the structural heterogeneity in this disease.Semantic proximity Read ↗

Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene.Semantic proximity Read ↗

Two different allelic mutations in the lecithin:cholesterol acyltransferase (LCAT) gene resulting in classic LCAT deficiency: LCAT (tyr83-->stop) and LCAT (tyr156-->asn).Semantic proximity Read ↗

LCAT deficiency: molecular and phenotypic characterization of an Italian family.Semantic proximity Read ↗

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