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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 (179) and Patatin-Like phospholipase Domain Containing 2 Proteins (9) and many more products for this protein.
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the ATGL gene plays an important role in triglyceride lipolysis in GMECs; ATGL may be involved in lipid metabolism during lactation
Oxidative stress decreased the levels of PNPLA2 transcripts with no effect on ALOX5 expression. Exogenous additions of P1 peptide or overexpression of the PNPLA2 gene decreased both LTB4 levels and death of RPE 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.
Rab32 (show RAB32 ELISA Kits) controls intracellular lipid accumulation through inducing lipolysis via enhancing ATGL expression indirectly.
Data indicate that a tumor suppressor mechanism by which G0/G1 switch gene 2 product (G0S2) directly inhibits activity of a key intracellular adipose triglyceride lipase (ATGL).
Authors show that rat ATGL, coactivated by rat CGI-58 (show ABHD5 ELISA Kits), efficiently hydrolyzes triglycerides and retinyl ester.
PNPLA2 mutations were associated with an extended phenotype, including brain involvement in cases of neutral lipid-storage disease with myopathy.
Distinct cardiac phenotype between two homozygotes born in a village with accumulation of a genetic deficiency of adipose triglyceride lipase.
ANGPTL8 is a stress-response protein that down-regulates expression of ATGL.
The Atgl is down-regulated by the basal transcription factor Sp1 (show SP1 ELISA Kits) in preadipocytes and that the magnitude of down-regulation depends on interactions between Sp1 (show SP1 ELISA Kits) and peroxisome proliferator-activated receptor gamma (PPARgamma (show PPARG ELISA Kits)).
TAG synthesis and levels of PUFA-TAGs were lowered by the diacylglycerol acyltransferase (DGAT)1 (show DGAT1 ELISA Kits) inhibitor, T863. The lipase (show LIPG ELISA Kits) inhibitor, Atglistatin, increased the levels of TAG in both WT and ATGL-deficient mouse Hepatic stellate cell (HSC (show FUT1 ELISA Kits)). Both Atglistatin and T863 inhibited the induction of activation marker, alpha-smooth muscle actin (show ACTG2 ELISA Kits), in rat HSCs, but not in mouse HSCs.
G0S2 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
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 ELISA Kits), and finally contribute to the renal fibrosis and dysfunction
Markers of mitochondrial content and respiration were increased in adipose tissue from ATGL knockout mice.
ase (show ARSE ELISA Kits). Similar changes of GPNMB and G0S2 expression were present in a human liposarcoma database. These results show that a previously-unknown, fully penetrant epistatic interaction between Pnpla2 and Lipe (show LIPE ELISA Kits) can cause liposarcoma in mice. DAKO mice provide a promising model for studying early premalignant changes that lead to late-onset malignant disease.
Activities of adipose triglyceride lipase (ATGL), hormone sensitive lipolitic enzyme (HSL (show LIPE ELISA Kits)) and monoacylglycerol lipase (MGL (show MGLL ELISA Kits)) were significantly higher (51 %, 38 %, 49 %) in the DE group than the HF group (p < 0.05). MGL (show CLEC10A ELISA Kits), there were no differences between the CO group, HF group, and DC group, with the DE group (70 %) being significantly higher (p < 0.05).
ATGL activity is required for UCP1 (show UCP1 ELISA Kits) activation in intact adipocytes. (Review)
ATGL-dependent lipolysis plays a critical role in mediating diverse effects of FoxO (show FOXO3 ELISA Kits) proteins in the liver, including effects on gluconeogenic, glycolytic, and lipogenic gene expression and metabolism.
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 ELISA Kits)) gene expression and increased adipose triglyceride lipase (ATGL) gene expression and glycerol release. Furthermore, this study found the opposite Sirt1 (show SIRT1 ELISA Kits) regulation pattern for PPARgamma (show PPARG ELISA Kits) to that of ATGL in adipocytes.
analysis of porcine adipose triglyceride lipase (PNPLA2) gene
JAK (show JAK3 ELISA Kits)-STAT (show STAT1 ELISA Kits) and MAPK (show MAPK1 ELISA Kits) signaling pathways, as well as PPAR gamma (show PPARG ELISA Kits) all played important roles in the ATGL expression mediated by leptin (show LEP ELISA Kits)
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