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PNPLA2 encodes an enzyme which catalyzes the first step in the hydrolysis of triglycerides in adipose tissue. Additionally we are shipping Patatin-Like phospholipase Domain Containing 2 Antibodies (175) and Patatin-Like phospholipase Domain Containing 2 Kits (40) and many more products for this protein.
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Human PNPLA2 Protein expressed in Wheat germ - ABIN1315583
Tavian, Missaglia, Redaelli, Pennisi, Invernici, Wessalowski, Maiwald, Arca, Coleman: Contribution of novel ATGL missense mutations to the clinical phenotype of NLSD-M: a strikingly low amount of lipase activity may preserve cardiac function. in Human molecular genetics 2012
the ATGL gene plays an important role in triglyceride lipolysis in GMECs; ATGL may be involved in lipid metabolism during lactation
Although we found evidence for moderate association between PNPLA2 tagSNPs and anthropometric and metabolic parameters in our cohort, no evidence for association between polymorphisms in the PNPLA2 gene and the presence and severity of non-alcoholic fatty liver disease was identified.
Study reports the derivation of iPSCs from fibroblasts of two Neutral Lipid Storage Disease with Myopathy (NLSDM)patients carrying different ATGL mutations. These iPSCs exhibited defects in neutral lipid metabolism similar to those of NLSDM fibroblasts. NLSDM-iPSCs were able to undergo directed differentiation into cardiomyocytes.
Thus, ATGL in leucocytes may be an important biomarker for the diagnosis of TGCV and our assay may provide insights into pathophysiology and elucidate the underlying mechanism of TGCV and related disorders.
The ATGL gene was frequently deleted in various forms of human cancers and was associated with poor prognosis.
a Snail1 (show SNAI1 Proteins)-ATGL axis that regulates adipose lipolysis and fatty acid release, is reported.
ABHD5 (show ABHD5 Proteins) possesses a PNPLA2-independent function in regulating autophagy and tumorigenesis.
Oxidative stress decreased the levels of PNPLA2 transcripts with no effect on ALOX5 (show ALOX5 Proteins) expression. Exogenous additions of P1 peptide or overexpression of the PNPLA2 gene decreased both LTB4 (show PTGR1 Proteins) levels and death of RPE (show RPE Proteins) cells undergoing oxidative stress.
Results suggest that increased adipose triglyceride lipase (ATGL) expression is associated with increased adiposity and stromal proliferation in patients with pancreatic ductal adenocarcinoma (PDAC).
A missense mutation in PNPLA2 is the rare cause of severe dilated cardiomyopathy secondary to neutral lipid storage disease.
A novel deletion was identified in PNPLA2 protein from a patient with complete deficiency of adipose triglyceride lipase.
Loss of ATGL induces spontaneous development of pulmonary neoplasia in knockout mouse model.
ATGL acts as an important upstream signaling node that, via SIRT1 (show SIRT1 Proteins), increases autophagy/lipophagy as a means to promote hepatic lipid droplet catabolism.
CGI-58 (show ABHD5 Proteins) regulates hepatic neutral lipid storage and inflammation in the genetic absence of ATGL.
Enhanced lipolysis in response to mitochondrial uncoupling relies on a form of autophagy as lipid droplets are captured by endolysosomal vesicles which is HSL (show LIPE Proteins)/ATGL-independent.
The Atgl is down-regulated by the basal transcription factor Sp1 (show SP1 Proteins) in preadipocytes and that the magnitude of down-regulation depends on interactions between Sp1 (show SP1 Proteins) and peroxisome proliferator-activated receptor gamma (PPARgamma (show PPARG Proteins)).
TAG synthesis and levels of PUFA-TAGs were lowered by the diacylglycerol acyltransferase (DGAT)1 (show DGAT1 Proteins) inhibitor, T863. The lipase (show LIPG Proteins) inhibitor, Atglistatin, increased the levels of TAG in both WT and ATGL-deficient mouse Hepatic stellate cell (HSC (show FUT1 Proteins)). Both Atglistatin and T863 inhibited the induction of activation marker, alpha-smooth muscle actin (show ACTG2 Proteins), in rat HSCs, but not in mouse HSCs.
G0S2 (show G0S2 Proteins) protein but not mRNA levels were reduced in the adipose tissue of ATGL-deficient mice, corroborating the involvement of ATGL in the stabilization of G0S2 (show G0S2 Proteins)
Atgl deficiency induces podocyte apoptosis and leads to glomerular filtration barrier damage.
These data raise the possibility that ATGL deficiency could impair the renal fatty acid metabolism though inhibiting PPARalphaexpression, which may lead to lipid deposition and cell apoptosis of PCT (show UROD Proteins), and finally contribute to the renal fibrosis and dysfunction
Results identified functional polymorphisms providing new evidence of PNPLA2 as an important candidate gene for fat deposition and carcass traits in pigs.
Resveratrol activated sirtuin 1 (Sirt1 (show SIRT1 Proteins)) gene expression and increased adipose triglyceride lipase (ATGL) gene expression and glycerol release. Furthermore, this study found the opposite Sirt1 (show SIRT1 Proteins) regulation pattern for PPARgamma (show PPARG Proteins) to that of ATGL in adipocytes.
analysis of porcine adipose triglyceride lipase (PNPLA2) gene
JAK (show JAK3 Proteins)-STAT (show STAT1 Proteins) and MAPK (show MAPK1 Proteins) signaling pathways, as well as PPAR gamma (show PPARG Proteins) all played important roles in the ATGL expression mediated by leptin (show LEP Proteins)
patatin-like phospholipase domain containing 2 gene (PNPLA2) is assiged to chromosome 2 in pigs.
ATGL expression reacts to hormonal stimuli and plays a role in catecholamine-induced lipolysis in porcine adipose tissue.
Tissue distribution of ATGL gene expression was highest in fat and muscle (skeletal and cardiac) tissue, while protein expression was solely detectible in the adipose tissue.
This gene encodes an enzyme which catalyzes the first step in the hydrolysis of triglycerides in adipose tissue. Mutations in this gene are associated with neutral lipid storage disease with myopathy.
patatin-like phospholipase domain-containing protein 2
, patatin-like phospholipase domain containing 2
, adipose triglyceride lipase
, calcium-independent phospholipase A2
, patatin-like phospholipase domain containing protein 2
, pigment epithelium-derived factor
, transport-secretion protein 2.2
, triglyceride hydrolase
, transport-secretion protein