Linked Life Data

10487497

Source:http://linkedlifedata.com/resource/pubmed/id/10487497

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-10-28
pubmed:abstractText
Lecithin: cholesterolacyltransferase (LCAT) transacylates the fatty acid at the sn-2 position of lecithin to the 3beta-OH group of cholesterol forming lysolecithin and the majority of cholesteryl ester found in plasma. LCAT participates in the reverse cholesterol transport pathway in man where it esterifies tissue-derived cholesterol following efflux from peripheral cells into HDL. Only 38 unique mutations in the human LCAT gene have been reported worldwide. Our French female proband presented with corneal opacity and no detectable plasma LCAT activity using either endogenous or exogenous assays. Her total plasma cholesterol and HDL cholesterol were low (2.34 mmol/l and 0.184 mmol/l, respectively) with a very high cholesterol/cholesteryl ester molar ratio (10.9:1). Plasma triglycerides were 0.470 mmol/l with low apo B (40.5 mg/dl), apo A-I (14.7 mg/dl), apo A-II (6.8 mg/dl) and apo E (2.1 mg/dl) levels. Plasma lipoprotein analysis by ultracentrifugation showed very low HDL concentrations and a characteristic shift of the lipoprotein profile towards larger, less dense particles. No proteinuria, renal dysfunction or signs of atherosclerosis were noted at age 45. Sequence analysis of her LCAT gene showed a novel homozygous TG-deletion at residues 138-139 that resulted in a frameshift causing the generation of a stop codon and premature termination of the LCAT protein at amino acid residue 144. Western blotting of the patient's plasma using a polyclonal IgY primary antibody against human LCAT failed to demonstrate the presence of a truncated LCAT protein. A 53 bp mismatched PCR primer was designed to generate an Fsp 1 restriction site in the wild type sequence of exon 4 where the mutation occurred. The 155 bp PCR product from the wild type allele produced a 103 bp and 52 bp fragment with Fsp 1 and no cleavage products with the mutant allele thus permitting rapid screening for this novel mutation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9150
pubmed:author
pubmed:issnType
Print
pubmed:volume
146
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
141-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10487497-Adolescent, pubmed-meshheading:10487497-Apolipoproteins, pubmed-meshheading:10487497-Base Sequence, pubmed-meshheading:10487497-Codon, pubmed-meshheading:10487497-Cornea, pubmed-meshheading:10487497-Corneal Opacity, pubmed-meshheading:10487497-DNA Mutational Analysis, pubmed-meshheading:10487497-Electrophoresis, Agar Gel, pubmed-meshheading:10487497-Exons, pubmed-meshheading:10487497-Female, pubmed-meshheading:10487497-Frameshift Mutation, pubmed-meshheading:10487497-Gene Deletion, pubmed-meshheading:10487497-Humans, pubmed-meshheading:10487497-Lecithin Acyltransferase Deficiency, pubmed-meshheading:10487497-Molecular Sequence Data, pubmed-meshheading:10487497-Phenotype, pubmed-meshheading:10487497-Phosphatidylcholine-Sterol O-Acyltransferase, pubmed-meshheading:10487497-Phosphatidylcholines, pubmed-meshheading:10487497-Polymerase Chain Reaction
pubmed:year
1999
pubmed:articleTitle
Classical LCAT deficiency resulting from a novel homozygous dinucleotide deletion in exon 4 of the human lecithin: cholesterol acyltransferase gene causing a frameshift and stop codon at residue 144.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Canada.
pubmed:publicationType
Journal Article, Case Reports, Research Support, Non-U.S. Gov't