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PNPLA4 encodes a member of the patatin-like family of phospholipases. De plus, nous expédions PNPLA4 Protéines (3) et beaucoup plus de produits pour cette protéine.
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These results strongly suggest that PNPLA9, -6 and -4 play a key role in GPL turnover and homeostasis in human cells. A hypothetical model suggesting how these enzymes could recognize the relative concentration of the different GPLs is proposed
iPLA2epsilon (adiponutrin), iPLA2zeta (TTS-2.2), and iPLA2eta (GS2) are three novel TAG lipases/acylglycerol transacylases that likely participate in TAG hydrolysis and the acyl-CoA independent transacylation of acylglycerols
The GS2 gene (PNPLA4) encodes a keratinocyte retinyl ester hydrolase. The protein also catalyzes fatty acyl CoA-dependent and -independent retinol esterification, using triolein as substrate and generates diacylglyceride and free fatty acid.
we report the identity of an inhibitor, TIP47, which prevents retinylester hydrolysis catalyzed by GS2 lipase and hormone-sensitive lipase
GS2 promotes RE accumulation and may do so either as a catalyst or as a regulatory protein that enhances retinylesters formation catalyzed by other acyl transferases.
No association between genetic variants in PNPLA4 genes and childhood and adolescent obesity
This gene encodes a member of the patatin-like family of phospholipases. The encoded enzyme has both triacylglycerol lipase and transacylase activities and may be involved in adipocyte triglyceride homeostasis. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome Y.
patatin-like phospholipase domain-containing protein 4
, patatin-like phospholipase 4
, patatin-like phospholipase domain containing 4
, IPLA2 eta
, calcium independent phospholipases A2 eta