What question did this study set out to answer?

To identify and characterize the functional and clinical consequences of a novel mutation in the lipoprotein lipase gene in a family presenting with dyslipidemia.

February 1, 1994Journal of Lipid ResearchOpen Access

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.

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To identify and characterize the functional and clinical consequences of a novel mutation in the lipoprotein lipase gene in a family presenting with dyslipidemia.
Sequenced exon 5 of the lipoprotein lipase (LPL) gene in a 50-year-old female proband and her two daughters.
Transfected COS cells with a mutant cDNA construct carrying the His183 to Gln substitution to assess enzyme secretion and catalytic activity in vitro.
Expression of the mutant cDNA construct in COS cells resulted in the secretion of an inactive LPL protein, demonstrating complete loss of catalytic activity.
Heterozygosity for the His183 to Gln mutation presented in the proband with variable and severe hypertriglyceridemia, obesity, hypertension, coronary heart disease, and non-insulin-dependent diabetes mellitus, whereas heterozygous daughters had milder hypertriglyceridemia and obesity.

Structured PICO

Population

A Finnish family (n=3; a 50-year-old female proband and her two daughters aged 24 and 19) presenting with variable hypertriglyceridemia and obesity, alongside an in vitro model using COS cells.

Outcome

Identification of LPL gene mutation and assessment of its functional catalytic activity.surrogate

Heterozygosity for a functional defect of LPL (His183-->Gln mutation) results in inactive enzyme protein and may contribute to the metabolic dyslipidemic syndrome.

Limitations

Assessment of a causative link between the mutation and hyperlipidemia awaits further studies

Discussion

No takes yet. Share an insight, caveat, or question.

Implication

May link novel LPL mutation to inactive enzyme and dyslipidemia; hypothesis-generating for metabolic syndrome role, needs validation.

Cite This Study

Tenkanen et al. (1994) studied this question.

synapsesocial.com/papers/6a82c140a7c6f3cae68addf0 https://doi.org/10.1016/s0022-2275(20)41210-6

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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.

Key Points

Structured PICO

Limitations

Discussion

Implication

Cite This Study

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.

Key Points

Structured PICO

Limitations

Discussion

Implication

Cite This Study

Also Consider

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