期刊
FASEB JOURNAL
卷 30, 期 7, 页码 2591-2601出版社
FEDERATION AMER SOC EXP BIOL
DOI: 10.1096/fj.201500097R
关键词
remodeling pathway; lysophospholipid; neuronal differentiation; phospholipid metabolism; oleoyl-CoA
资金
- Japan Society for the Promotion of Science (JSPS) (KAKENHI) [23390467, 24659841, 24229003, 26460380, 26870879]
- Agency for Medical Research and Development-Core Research for Evolutional Science and Technology (AMED-CREST)
- Shimadzu Corp.
- Ono Pharmaceutical Co., Ltd.
- Grants-in-Aid for Scientific Research [16H05545, 24659841, 26870879, 16K21651, 15K15696, 23390467, 15K11083, 15K15746] Funding Source: KAKEN
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.
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