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GPAM encodes a mitochondrial enzyme which prefers saturated fatty acids as its substrate for the synthesis of glycerolipids. Additionally we are shipping Glycerol-3-Phosphate Acyltransferase, Mitochondrial Kits (5) and Glycerol-3-Phosphate Acyltransferase, Mitochondrial Proteins (4) and many more products for this protein.
Showing 10 out of 63 products:
Human Polyclonal GPAM Primary Antibody for EIA, WB - ABIN952583
Reiling, van Vliet-Ostaptchouk, van t Riet, van Haeften, Arp, Hansen, Kremer, Groenewoud, van Hove, Romijn, Smit, Nijpels, Heine, Uitterlinden, Pedersen, Slagboom, Maassen, Hofker, t Hart, Dekker: Genetic association analysis of 13 nuclear-encoded mitochondrial candidate genes with type II diabetes mellitus: the DAMAGE study. in European journal of human genetics : EJHG 2009
Show all 3 references for ABIN952583
Human Polyclonal GPAM Primary Antibody for ELISA, WB - ABIN566151
Li, Sugiyama, Yokoyama, Jiang, Tanaka, Aoyama: Molecular mechanism of age-specific hepatic lipid accumulation in PPARalpha (+/-):LDLR (+/-) mice, an obese mouse model. in Lipids 2008
Show all 2 references for ABIN566151
Human Polyclonal GPAM Primary Antibody for EIA, IHC (p) - ABIN499910
Coleman, Lee: Enzymes of triacylglycerol synthesis and their regulation. in Progress in lipid research 2003
GPAT1, but not GPAT4 (show AGPAT6 Antibodies), 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 Antibodies) of the Gpam promoter inhibited recruitment of the lipogenic transcription factor SREBP-1c (show SREBF1 Antibodies), whereas in the adult, decreased DNA methylation (show HELLS Antibodies) resulted in active chromatin conformation, allowing recruitment of SREBP-1c (show SREBF1 Antibodies).
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 Antibodies) 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 Antibodies) 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.
GPAT1 contributes significantly to cardiomyocyte triacylglycerol synthesis during lipogenic or high-fat diets and influences the incorporation of 20:4n6 into heart phospholipids.
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.
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