Human Genetics

, Volume 85, Issue 2, pp 195–199

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
Original Investigations

DOI: 10.1007/BF00193195

Cite this article as:
Taramelli, R., Pontoglio, M., Candiani, G. et al. Hum Genet (1990) 85: 195. doi:10.1007/BF00193195

Summary

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.

Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • Roberto Taramelli
    • 1
  • Marco Pontoglio
    • 2
  • Giulia Candiani
    • 1
  • Sergio Ottolenghi
    • 1
  • Hans Dieplinger
    • 3
  • Alberico Catapano
    • 4
  • John Albers
    • 5
  • Carlo Vergani
    • 6
  • John McLean
    • 7
  1. 1.Dipartimento di Genetica e di Biologia dei MicrorganismiMilanItaly
  2. 2.Istituto Scientifico S. RaffaeleMilanItaly
  3. 3.Institut für Medizinische Biologie der UniversitätInnsbruckAustria
  4. 4.Istituto di FarmacologiaMilanItaly
  5. 5.Department of MedicineUniversity of WashingtonSeattleUSA
  6. 6.Istituto di Semeiotica MedicaMilanItaly
  7. 7.Department of Cardiovascular ResearchGenentech Inc.San FranciscoUSA

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