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Human lipoprotein lipase complementary DNA sequence.

K L Wion, T G Kirchgessner, A J Lusis

Science (New York, N.Y.)

|March 27, 1987

Summary

Researchers have sequenced the human lipoprotein lipase (LPL) enzyme, a key player in lipid metabolism linked to obesity and atherosclerosis. This breakthrough provides the protein sequence and reveals LPL belongs to a lipase gene family.

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Area of Science:

Biochemistry
Molecular Biology
Genetics

Background:

Lipoprotein lipase (LPL) is a critical enzyme in lipid metabolism, hydrolyzing triglycerides to supply free fatty acids and influencing lipoprotein maturation.
LPL is implicated in the pathogenesis of obesity and atherosclerosis.
Previous challenges in purifying human LPL hindered the determination of its protein sequence.

Purpose of the Study:

To clone and sequence the complementary DNA (cDNA) encoding human lipoprotein lipase.
To elucidate the protein sequence of mature human LPL.
To investigate the relationship of human LPL to other lipases and its gene expression patterns.

Main Methods:

Complementary DNA (cDNA) cloning of human lipoprotein lipase.
DNA sequencing to determine the protein sequence.
Bioinformatic analysis to compare LPL with hepatic and pancreatic lipases.
Messenger RNA (mRNA) detection in various tissues using Northern blot or similar techniques.

Main Results:

The cDNA for human LPL was successfully cloned and sequenced, revealing a mature protein of 448 amino acids.
Sequence analysis indicated that human LPL, hepatic lipase, and pancreatic lipase share homology, suggesting membership in a gene family.
Two distinct species of LPL mRNA were identified in multiple tissues, resulting from alternative 3'-terminal polyadenylation sites.

Conclusions:

The determination of the human LPL sequence provides a foundational resource for further research into its function and regulation.
The findings establish a genetic link between LPL and other lipases, offering insights into lipase evolution and function.
The existence of alternative mRNA forms suggests complex post-transcriptional regulation of LPL expression in different tissues.

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