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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0015295,
umls-concept:C0017337,
umls-concept:C0017797,
umls-concept:C0019425,
umls-concept:C0023816,
umls-concept:C0031437,
umls-concept:C0205314,
umls-concept:C0243102,
umls-concept:C0525038,
umls-concept:C0678941,
umls-concept:C0679622,
umls-concept:C1264638,
umls-concept:C1274040,
umls-concept:C1442792,
umls-concept:C1517945
|
| pubmed:issue |
2
|
| pubmed:dateCreated |
1994-6-1
|
| pubmed:abstractText |
We have identified a hitherto unrecognized mutation of the lipoprotein lipase gene (LPL) in a Finnish family with Russian and Swiss ancestors. A single base pair substitution of a guanine for cytosine in codon 183 of exon 5 of the LPL gene results in a change of histidine to glutamine in the mature enzyme protein. Expression of a mutant cDNA construct in COS cells resulted in secretion of inactive LPL enzyme protein confirming the functional significance of the mutation. The proband, a 50-year-old female and her two daughters were all heterozygous for the His183-->Gln mutation. Clinically, the proband was characterized by variable and occasionally severe hypertriglyceridemia, obesity, hypertension, coronary heart disease and non-insulin-dependent diabetes mellitus. The daughters, aged 24 and 19 years, were also obese but had milder hypertriglyceridemia. In conclusion, we have identified a novel LPL mutation that results in the synthesis of an inactive enzyme protein. Although the assessment of a causative link between the mutation and hyperlipidemia awaits further studies, our data suggest that heterozygosity for a functional defect of LPL should be considered in patients presenting with the metabolic dyslipidemic syndrome, "syndrome-X."
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0022-2275
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
35
|
| pubmed:geneSymbol |
LPL
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
220-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8169525-Amino Acids,
pubmed-meshheading:8169525-Base Sequence,
pubmed-meshheading:8169525-Cells, Cultured,
pubmed-meshheading:8169525-DNA, Complementary,
pubmed-meshheading:8169525-DNA Mutational Analysis,
pubmed-meshheading:8169525-Exons,
pubmed-meshheading:8169525-Female,
pubmed-meshheading:8169525-Gene Expression,
pubmed-meshheading:8169525-Heterozygote,
pubmed-meshheading:8169525-Humans,
pubmed-meshheading:8169525-Hypertriglyceridemia,
pubmed-meshheading:8169525-Lipids,
pubmed-meshheading:8169525-Lipoprotein Lipase,
pubmed-meshheading:8169525-Lipoproteins,
pubmed-meshheading:8169525-Middle Aged,
pubmed-meshheading:8169525-Molecular Sequence Data,
pubmed-meshheading:8169525-Mutation,
pubmed-meshheading:8169525-Polymerase Chain Reaction,
pubmed-meshheading:8169525-Polymorphism, Genetic
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
A novel amino acid substitution (His183-->Gln) in exon 5 of the lipoprotein lipase gene results in loss of catalytic activity: phenotypic expression of the mutant gene in a heterozygous state.
|
| pubmed:affiliation |
National Public Health Institute, University of Helsinki, Finland.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|