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The protein encoded by PNPLA3 is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes. Additionally we are shipping PNPLA3 Antibodies (91) and PNPLA3 Kits (12) and many more products for this protein.
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Human PNPLA3 Protein expressed in Wheat germ - ABIN1315587
Winberg, Motlagh, Stenkula, Holm, Jones: Adiponutrin: a multimeric plasma protein. in Biochemical and biophysical research communications 2014
The PNPLA3 148 I/M or M/M variants and CD4 (show CD4 Proteins)(+) cell count were the only independent predictors of severe steatosis in patients with hepatitis C virus non-3 genotypes.
the PNPLA3 rs738409 was determined to be associated with hepatocellular carcinoma development in a cohort of Japanese patients with type 2 diabetes mellitus
PNPLA3 p.I148M variant represents the most important prosteatotic genetic risk factor. NAFLD carriers of this variant should be followed up carefully, with elastography being ideally suited for this purpose.
The PNPLA3 p.I148M variant is associated with non-alcoholic fatty liver disease.
based on data from the HALT-C trial, the PNPLA3 CG/GG SNP at rs738409 is associated with fibrosis progression but not development of Hepatocellular Carcinoma in patients with Hepatitis C Virus Infection
transmembrane 6 superfamily 2 C/T or T/T variants in conjunction with patatin-like phospho-lipase (show LIPG Proteins) domain-containing protein 3 (show HSPB3 Proteins) G/G variants may be potential genetic risk factors for developing HCC (show FAM126A Proteins) in alcohol-related cirrhosis.
Steatosis severity was independently associated with PNPLA3 rs738409 in large cohort of patients with genotype 1 Chronic hepatitis C.
I148M variant in PNPLA3 reduces central adiposity and metabolic disease risks while increasing Nonalcoholic fatty liver disease.
PNPLA3 148M Carriers with Inflammatory Bowel Diseases Have Higher Susceptibility to Hepatic Steatosis and Higher Liver Enzymes.
PNPLA3 rs738409 polymorphism was associated with the severity of liver fibrosis in patients coinfected with HIV and hepatitis C virus.
Neither ablation nor overexpression of wild-type PNPLA3 affects liver fat content in mice, whereas hepatic overexpression of the human 148M transgene causes steatosis.
PNPLA3 plays a role in remodeling TAG in lipid droplets, as they accumulate in response to food intake
adiponutrin/PNPLA3 is regulated by two key factors of the glycolytic and lipogenic pathways, raising the question of its implication in the metabolism of carbohydrates and lipids
data argue against a role for Pnpla3 loss-of-function in fatty liver disease or metabolic syndrome in mice.
Loss of Pnpla3 does not cause fatty liver, liver enzyme elevation, or insulin (show INS Proteins) resistance in mice.
Microarray-based gene profiling showed that the expression level of PNPLA3 in hepatocytes is correlated with that of genes associated with the lipogenic pathway such as ME1 (show ME1 Proteins), SPOT14 (show THRSP Proteins), and SCD1 (show SCD Proteins).
data suggest that murine ATGL (show PNPLA2 Proteins) but not adiponutrin contributes to net adipocyte lipolysis and that ATGL (show PNPLA2 Proteins) and adiponutrin are oppositely regulated by insulin (show INS Proteins) both in vitro and in vivo
The protein encoded by this gene is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes. The encoded protein, which appears to be membrane bound, may be involved in the balance of energy usage/storage in adipocytes.
, calcium-independent phospholipase A2-epsilon
, patatin-like phospholipase domain-containing protein 3