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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
Author(s) -
Martin-Sanz Paloma,
Hopewell Roger,
Brindley David N.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80752-8
Subject(s) - cytosol , microsome , phosphatidate , biochemistry , chromosomal translocation , acyl coa , chemistry , biology , enzyme , phospholipid , membrane , phosphatidic acid , gene
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.