| Title : Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele - Taramelli_1990_Hum.Genet_85_195 |
| Author(s) : Taramelli R , Pontoglio M , Candiani G , Ottolenghi S , Dieplinger H , Catapano A , Albers J , Vergani C , McLean J |
| Ref : Hum Genet , 85 :195 , 1990 |
|
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. |
| PubMedSearch : Taramelli_1990_Hum.Genet_85_195 |
| PubMedID: 2370048 |
| Gene_locus related to this paper: human-LCAT |
| Mutation | R147W_human-LCAT |
| Gene_locus | human-LCAT |
| Family | PC-sterol_acyltransferase |
| Disease | Lecithin-cholesterol acyltransferase deficiency (LCATD) and fish-eye disease (FED) |
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
Hum Genet
85 :195
Taramelli R, Pontoglio M, Candiani G, Ottolenghi S, Dieplinger H, Catapano A, Albers J, Vergani C, McLean J (1990)
Hum Genet
85 :195