Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism

J S Hill; K O; X Wang; P H Pritchard

doi:10.1016/0925-4439(93)90039-4

Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism

Biochim Biophys Acta. 1993 Jun 19;1181(3):321-3. doi: 10.1016/0925-4439(93)90039-4.

Authors

J S Hill¹, K O, X Wang, P H Pritchard

Affiliation

¹ University Hospital Lipid Research Group, Department of Pathology, University of British Columbia, Vancouver, Canada.

PMID: 8318557
DOI: 10.1016/0925-4439(93)90039-4

Abstract

We have recreated and expressed two known natural mutations within the LCAT gene which were reported on both alleles in a single case of familial LCAT deficiency. We demonstrate that the Ala-93-->Thr mutation is responsible for the biochemical defect while the Arg-158-->Cys mutation is a co-inherited natural polymorphism of LCAT which results in normal enzyme function.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Alanine
Amino Acid Sequence
Arginine
Base Sequence
Cystine
Humans
Lecithin Cholesterol Acyltransferase Deficiency / genetics*
Lipoproteins / blood
Molecular Sequence Data
Mutation
Phosphatidylcholine-Sterol O-Acyltransferase / chemistry
Phosphatidylcholine-Sterol O-Acyltransferase / genetics*
Polymorphism, Genetic
Threonine

Substances

Lipoproteins
Threonine
Cystine
Arginine
Phosphatidylcholine-Sterol O-Acyltransferase
Alanine