Literature DB >> 28405875

Acute Fasting Induces Expression of Acylglycerophosphate Acyltransferase (AGPAT) Enzymes in Murine Liver, Heart, and Brain.

Ryan M Bradley1, Emily B Mardian1, Katherine A Moes1, Robin E Duncan2.   

Abstract

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.

Entities:  

Keywords:  Acylglycerophosphate acyltransferase (AGPAT)/lysophosphatidic acid acyltransferase (LPAAT); Fasting; Non-esterified fatty acids (NEFA); Phospholipid synthesis; Triacylglycerol (TAG)

Mesh:

Substances:

Year:  2017        PMID: 28405875     DOI: 10.1007/s11745-017-4251-4

Source DB:  PubMed          Journal:  Lipids        ISSN: 0024-4201            Impact factor:   1.880


  33 in total

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