Premium
Acute Fasting Induces Expression of Acylglycerophosphate Acyltransferase (AGPAT) Enzymes in Murine Liver, Heart, and Brain
Author(s) -
Bradley Ryan M.,
Mardian Emily B.,
Moes Katherine A.,
Duncan Robin E.
Publication year - 2017
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/s11745-017-4251-4
Subject(s) - phosphatidic acid , lysophosphatidic acid , acyltransferases , acyltransferase , lipidology , clinical chemistry , medicine , endocrinology , enzyme , nefa , biochemistry , biology , chemistry , fatty acid , phospholipid , biosynthesis , receptor , membrane
During fasting, cells increase uptake of non‐esterified fatty acids (NEFA) and esterify excess into phosphatidic acid (PtdOH), the common precursor of both triacylglycerols and phospholipids, using acylglycerophosphate acyltransferases/lysophosphatidic acid acyltransferases (AGPAT/LPAAT). Knowledge of the regulation of AGPAT enzymes is important for understanding fasting adaptations. Total RNA was isolated from liver, heart, and whole brain tissue of C57BL/6J mice fed ad libitum, or fasted for 16 h. Following fasting, induction of Agpat2 , 3 , 4 , and 5 was observed in the liver, Agpat2 and 3 in heart tissue, and Agpat1 , 2 , and 3 in whole brain tissue. As a result, the relative abundance profile of the individual homologues within specific tissues was found to be significantly altered depending on the nutritive state of the animal. These data demonstrate tissue‐specific effects of fasting on the regulation of different Agpat that are implicated in supporting unique downstream glycerolipid synthesis pathways.