Lysophospholipid Acyltransferases Mediate Phosphatidylcholine Diversification to Achieve the Physical Properties Required In Vivo
作者: Takeshi HarayamaMiki EtoHideo ShindouYoshihiro KitaEiji OtsuboDaisuke HishikawaSatoshi IshiiKenji SakimuraMasayoshi MishinaTakao Shimizu
作者单位: 1Department of Lipid Signaling, Research Institute, National Center for Global Health and Medicine, Shinjuku, Tokyo 162-8655, Japan
2Department of Lipidomics, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan
3Advanced Medical Research Department, Research Division, Mitsubishi Tanabe Pharma Corporation, Yokohama, Kanagawa 227-0033, Japan
4Department of Immunology, Graduate School of Medicine, Akita University, Akita 010-8543, Japan
5Department of Cellular Neurobiology, Brain Research Institute, Niigata University, Niigata 951-8585, Japan
6Brain Science Laboratory, The Research Organization of Science and Technology, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan
刊名: Cell Metabolism, 2014, Vol.20 (2), pp.295-305
来源数据库: Elsevier Journal
DOI: 10.1016/j.cmet.2014.05.019
原始语种摘要: Summary(#br)The acyl-chain composition of the major mammalian phospholipid phosphatidylcholine (PC) is distinct in various tissues. Although it was classically suggested that PC diversity is acquired through acyl-chain remodeling, the mechanisms and biological relevance of acyl-chain diversity remain unclear. Here, we show that differences in the substrate selectivity of lysophospholipid acyltransferases regulate tissue PC acyl-chain composition through contribution of both the de novo and remodeling pathways, depending on the fatty acid species. Unexpectedly, while dipalmitoyl-PC (DPPC) is enriched through the remodeling pathway, several polyunsaturated PC molecules accumulate during the de novo pathway. We confirmed this concept for DPPC in pulmonary surfactant and showed that the...
全文获取路径: Elsevier  (合作)
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影响因子:14.619 (2012)

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