title: Long-chain fatty acids and their acyl-CoA esters cause the translocation of phosphatidate phosphohydrolase from the cytosolic to the microsomal fraction of rat liver.
abstract: A translocation of phosphatidate phosphohydrolase from the cytosolic to the microsomal fraction was promoted in cell-free extracts of rat liver by oleate and palmitate and their CoA esters. Oleate was more potent in this respect than palmitate and the CoA esters were more effective than the unesterified acids. Octanoate, octanoyl-CoA and CoA did not cause the translocation. It is proposed that the interaction of phosphatidate phosphohydrolase with the membranes that synthesize glycerolipids causes it to become metabolically active. This enables the liver to increase its capacity for triacylglycerol synthesis in response to an increased supply of fatty acids.
mesh_terms: D000214:Acyl Coenzyme A / Q000494:pharmacology*; D000818:Animals; D001692:Biological Transport; D003600:Cytosol / Q000201:enzymology; D005230:Fatty Acids, Nonesterified / Q000494:pharmacology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008862:Microsomes, Liver / Q000378:metabolism*; D010711:Phosphatidate Phosphatase / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D051381:Rats; D013329:Structure-Activity Relationship
chemical_list: D000214:Acyl Coenzyme A; D005230:Fatty Acids, Nonesterified; D010744:Phosphoric Monoester Hydrolases; D010711:Phosphatidate Phosphatase