Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A normal rate of cellular cholesterol removal can be mediated by plasma from a patient with familial lecithin-cholesterol acyltransferase (LCAT) deficiency.

Clinica chimica acta; international journal of clinical chemistry - 1 Dec 2001

Bérard A M, Clerc M, Brewer B, Santamarina-Fojo S

Abstract excerpt

Lecithin-cholesterol acyltransferase (LCAT) is the major enzyme involved in the esterification of cholesterol in circulating plasma lipoproteins. In the present study, we describe the molecular defects in the LCAT gene and in lipoprotein metabolism of a 34-year-old patient presenting with features of classic familial LCAT deficiency. DNA sequencing revealed two separate point mutations in exon 3 of the patient's...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Apolipoproteins
Share to Arginine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cholesterol

Share to Cystine

Share to DNA, Complementary

Share to Fibroblasts

Share to Lipids

Share to Lipoproteins

Source

Identifiers

PMID: 11718688
DOI: 10.1016/s0009-8981(01)00689-1

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A normal rate of cellular cholesterol removal can be mediated by plasma from a patient with familial lecithin-cholesterol acyltransferase (LCAT) deficiency.PMID 11718688Read ↗

Genetic lecithin:cholesterol acyltransferase deficiency and cardiovascular disease.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 ↗

Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in the LCAT gene.Semantic proximity Read ↗

Recombinant human LCAT normalizes plasma lipoprotein profile in LCAT deficiency.Semantic proximity Read ↗

Fish eye syndrome: a molecular defect in the lecithin-cholesterol acyltransferase (LCAT) gene associated with normal alpha-LCAT-specific activity. Implications for classification and prognosis.Semantic proximity Read ↗

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

Activation of Naturally Occurring Lecithin:Cholesterol Acyltransferase Mutants by a Novel Activator Compound.Semantic proximity Read ↗

Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele.Semantic proximity Read ↗

Transmission of two novel mutations in a pedigree with familial lecithin:cholesterol acyltransferase deficiency: structure-function relationships and studies in a compound heterozygous proband.Semantic proximity Read ↗

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

Novel therapeutic opportunities for familial lecithin:cholesterol acyltransferase deficiency: promises and challenges.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.