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

Roberto Taramelli, Marco Pontoglio, Giulia Candiani, Sergio Ottolenghi, Hans Dieplinger, Alberico Catapano, John Albers, Carlo Vergani, John McLean

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)195-199
Number of pages5
JournalHuman Genetics
Issue number2
Publication statusPublished - Jul 1990

ASJC Scopus subject areas

  • Genetics(clinical)
  • Genetics


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