Cloning of porcine GPIHBP1 gene and its tissue expression pattern and genetic effect on adipose traits.

Lipoprotein lipase (LPL) is a key enzyme in lipid metabolism and is transported by glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) from the interstitial spaces to the capillary lumen. Here, we cloned a cDNA and the genomic locus of the porcine GPIHBP1 gene, and investigated its tissue expression pattern and its genetic effects on adipose traits. Porcine GPIHBP1 exhibits a four-exon/three-intron structure, including a 543bp open reading frame that encodes 180 amino acids.

Tissue expression pattern and polymorphism of G0S2 gene in porcine.

Adipose triglyceride lipase (ATGL), catalyzing the initial step of hydrolysis of triacylglycerol (TAG) in adipocytes, has been known to be inhibited by G0/G1 switch protein 2 (G0S2). In this study, we determined tissue expression pattern and polymorphism of G0S2 gene in porcine. The results showed that the G0S2 transcript levels were very high in the liver and, to a lesser degree, in adipose tissues of greater omentum and suet fat; and low G0S2 transcript levels were observed in other tissues.

[New insights in regulation factors of lipoprotein lipase].

Lipoprotein lipase (LPL) is an essential enzyme in the lipid metabolism, and proper regulation of LPL is important for controlling the delivery of lipid nutrients to tissues. Recent studies have identified glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1(GPIHBP1) as the important regulation factor of LPL that serves as a binding platform for lipolysis on the vascular lumen and an endothelial cell transporter transporting LPL from the interstitial spaces to the capillary lumen. In addition, several other regulation factors of LPL have also been identified including microRNAs, SorLA (Sortilin-related receptor with A-type repeats), and apolipoproteins that are potentially important for regulating LPL activity.