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Article

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

Journal of atherosclerosis and thrombosis - 1 Jan 2011

Wang Xiao Li, Osuga Jun-ichi, Tazoe Fumiko, Okada Kenta, Nagashima Shuichi, Takahashi Manabu, Ohshiro Taichi, Bayasgalan Tumenbayar, Yagyu Hiroaki, Okada Koji, Ishibashi Shun

Abstract excerpt

Lecithin-cholesterol acyltransferase (LCAT) is an important enzyme involved in the esterification of cholesterol. Here, we report a novel point mutation in the LCAT gene of a 63-year-old female with characteristics of classic familial LCAT deficiency. The patient's clinical manifestations included corneal opacity, mild anemia, mild proteinuria and normal renal function. She had no sign of coronary heart disease....

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

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Source

Identifiers

PMID: 21597230
DOI: 10.5551/jat.8003

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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Molecular analysis of a novel LCAT mutation (Gly179 → Arg) found in a patient with complete LCAT deficiency.PMID 21597230Read ↗

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