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 journalArticle

Abstract

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
Volume85
Issue number2
DOIs
Publication statusPublished - Jul 1990

ASJC Scopus subject areas

  • Genetics(clinical)
  • Genetics

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    Taramelli, R., Pontoglio, M., Candiani, G., Ottolenghi, S., Dieplinger, H., Catapano, A., Albers, J., Vergani, C., & McLean, J. (1990). Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele. Human Genetics, 85(2), 195-199. https://doi.org/10.1007/BF00193195