Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.34 (lipoprotein lipase)
 7,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We report here the molecular cloning of a novel member of the triglyceride lipase family, a 2.4-kb cDNA encoding human lipase H (LIPH) and the mouse ortholog (Liph). The human LIPH cDNA encodes a 451-amino-acid protein with a lipase domain. Mouse Liph shows 85% amino acid identity and 75% nucleotide identity to human LIPH. Human LIPH exhibits 47% identity with phosphatidylserine-specific phospholipase A1 (PS-PLA1) and 46% identity with endothelial lipase (LIPG) and lipoprotein lipase (LPL). LIPH is localized on human chromosome 3q27-q28. Northern blot analysis revealed specific expression of LIPH mRNA in intestine, lung, and pancreas. Lipase H protein was also detected in human intestine. Lipase H is a secreted protein with an apparent molecular weight of 63 kDa. Although several lipid substrates were tested, the lipid substrate of LIPG was not identified. Like the other members of this gene family, LIPH may be involved in lipid and energy metabolism.
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PMID:Lipase H, a new member of the triglyceride lipase family synthesized by the intestine. 1221 96

The triglyceride lipase gene family, including lipoprotein lipase (LPL), hepatic triglyceride lipase (HTGL), carboxyl ester lipase (CEL), endothelial lipase (EL), Lipase H, hormone sensitive lipase (HSL) and adipose triglyceride lipase (ATGL), plays a critical role in lipid metabolism in mammals. In this study, we have identified and characterized the expression profile of these genes in the chicken, Gallus gallus. Chicken LPL and ATGL have been cloned, and HTGL, EL, Lipase H, and CEL sequences were found in the chicken genome database. The deduced amino acid sequences of HTGL, EL, Lipase H, and CEL were 66, 75, 63, and 65% identical with their respective human genes, suggesting conservation of important enzymatic functions. In contrast, a homologue of the HSL gene was not identified in the chicken genome. We performed RT-PCR using chicken liver, muscle, abdominal adipose tissue, or pancreas mRNA as the template, and all partial products were completely matched to the corresponding predicted sequences of triglyceride lipase gene members. Quantitation by qPCR of the transcript levels of these genes in 13 tissues indicates that the expression patterns diverge greatly between species. A particularly interesting pattern was observed in the distribution of EL and HTGL mRNA, which were highly expressed in kidney and ovary. This is the first report of HTGL, EL, Lipase H, and CEL in a pre-mammalian species and reveals novel details about specific features of the expression of these important molecules in lipid metabolism.
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PMID:Tissue distribution of lipase genes related to triglyceride metabolism in laying hens (Gallus gallus). 1981 11