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

✍ Scribed by Roberto Taramelli; Marco Pontoglio; Giulia Candiani; Sergio Ottolenghi; Hans Dieplinger; Alberico Catapano; John Albers; Carlo Vergani; John McLean

• Book ID: 104658417
• Publisher: Springer
• Year: 1990
• Tongue: English
• Weight: 618 KB
• Volume: 85
• Category: Article
• ISSN: 0340-6717
• DOI: 10.1007/bf00193195

✦ Synopsis

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 a C to T transition in the fourth exon of the gene; this causes a substitution of Arg for Trp at position 147 of the mature Protein. The functional significance of such a substitution with respect to the enzyme defect was demonstrated by transfecting the mutated LCAT gene in the cell line COS-1.