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Silencing of GPAT1 by gpat1 siRNA transfection reduced glucosamine-mediated anti-apoptosis in mouse embryonic stem cells and reduced mammalian target of rapamycin (show FRAP1 Proteins) phosphorylation.
GPAT1, but not GPAT4 (show AGPAT6 Proteins), is required to incorporate de novo synthesized fatty acids into TAG and to divert them away from oxidation.
GPAT1 deletion is capable of reducing the number of new T cells produced via alterations in membrane receptor function.
In the neonatal liver, DNA methylation (show HELLS Proteins) of the Gpam promoter inhibited recruitment of the lipogenic transcription factor SREBP-1c (show SREBF1 Proteins), whereas in the adult, decreased DNA methylation (show HELLS Proteins) resulted in active chromatin conformation, allowing recruitment of SREBP-1c (show SREBF1 Proteins).
It was hypothesized that GPAT isoform GPAT1 might influence liver susceptibility to tumorigenesis. Data show that alterations in the formation of complex lipids catalyzed by Gpat1 reduce susceptibility to DEN-induced liver tumorigenesis.
Sterol regulatory element binding protein 1 mediated induction of hepatic steatosis in obese mice requires Gpat1.
Data confirm the role of mitochondrial glycerol-3-phosphate acyltransferase (GPAT) in the synthesis of triacylglycerol, in the fatty acid content of triacylglycerol and cholesterol esters, and in the positioning of specific fatty acids in phospholipids.
mtGPAT1 is essential for normal acyl-CoA (show GNPAT Proteins) metabolism, and that the absence of hepatic mtGPAT1 results in the partitioning of fatty acids away from triacylglycerol synthesis and toward oxidation and ketogenesis
Increased hepatic mtGPAT activity associated with obesity and insulin (show INS Proteins) resistance MAY contribute to increased TAG biosynthesis and inhibition of fatty acid oxidation, responses that would promote hepatic steatosis and dyslipidemia.
Gpat1-/- liver exhibits increased oxidative stress and sensitivity of the mitochondrial permeability transition pore, and a balanced increase in apoptosis and proliferation.
High GPAM expression is associated with Ovarian Carcinoma.
two transcriptional initiation sites and two promoters (promoter I and II) required for expression of the human GPAT1 (hGPAT1) gene were identified.
Results suggest that GPAM is expressed in human breast cancer with associated changes in the cellular metabolism, in particular an increased synthesis of phospholipids, the major structural component of cellular membranes.
Result showed that the knockdown of GPAM expression significantly reduced the synthesis of triglycerides and expression of lipid metabolism-related gene in bovine embryonic fibroblast cells (p<0.05), and the over-expression of GPAM could significantly increased the levels of triglyceride and expression of lipid metabolism-related gene (p<0.05).
Expression pattern differs with those of non-ruminant animals where liver is one of the tissues with higher mRNA expression level. (Glycerol-3-phosphate acyltransferase mitochondrial)
This gene encodes a mitochondrial enzyme which prefers saturated fatty acids as its substrate for the synthesis of glycerolipids. This metabolic pathway's first step is catalyzed by the encoded enzyme. Two forms for this enzyme exist, one in the mitochondria and one in the endoplasmic reticulum. Two alternatively spliced transcript variants have been described for this gene.
mitochondrial glycerol 3-phosphate acyltransferase
, glycerol-3-phosphate acyltransferase, mitochondrial
, glycerol-3-phosphate acyltransferase 1, mitochondrial
, glycerol 3-phosphate acyltransferase, mitochondrial
, mitochondrial glycerol phosphate acyltransferase