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FASEB J. 2016 Jul;30(7):2591-601. doi: 10.1096/fj.201500097R. Epub 2016 Apr 5.

Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell-derived neurons.

Author information

1
Division of Infections and Molecular Biology, Department of Health Promotion, Kyushu Dental University, Kitakyushu, Japan; Division of Oral and Maxillofacial Surgery, Department of Science of Physical Functions, Kyushu Dental University, Kitakyushu, Japan;
2
Department of Oral Functional Management, Kyushu Dental University, Kitakyushu, Japan; r09hikiji@fa.kyu-dent.ac.jp.
3
Division of Infections and Molecular Biology, Department of Health Promotion, Kyushu Dental University, Kitakyushu, Japan;
4
Department of Lipid Signaling, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan;
5
Department of Lipid Signaling, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan; Agency for Medical Research and Development-Core Research for Evolutionary Science and Technology (AMED-CREST), Tokyo, Japan; and.
6
Department of Lipid Signaling, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan; Department of Lipidomics, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
7
Division of Oral and Maxillofacial Surgery, Department of Science of Physical Functions, Kyushu Dental University, Kitakyushu, Japan;

Abstract

Glycerophospholipids, which are components of biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)-treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 cells. Voltage-dependent calcium channel activity was also suppressed in these cells transfected with LPEAT1/MBOAT1 siRNA. These results suggest that LPEAT1/MBOAT1 plays an important role in neurite outgrowth and function.-Tabe, S., Hikiji, H., Ariyoshi, W., Hashidate-Yoshida, T., Shindou, H., Okinaga, T., Shimizu, T., Tominaga, K., Nishihara, T. Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell-derived neurons.

KEYWORDS:

lysophospholipid; neuronal differentiation; oleoyl-CoA; phospholipid metabolism; remodeling pathway

PMID:
27048541
DOI:
10.1096/fj.201500097R
[Indexed for MEDLINE]

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