Document Detail

Member of the membrane-bound O-acyltransferase (MBOAT) family encodes a lysophospholipid acyltransferase with broad substrate specificity.
MedLine Citation:
PMID:  18782225     Owner:  NLM     Status:  MEDLINE    
Glycerophospholipids in biological membranes are metabolically active and participate in a series of deacylation-reacylation reactions, which may lead to accumulation of polyunsaturated fatty acids (PUFAs) at the sn-2 position of the glycerol backbone. The reacylation reaction is believed to be catalyzed by acyl-coenzyme A (acyl-CoA):lysophospholipid acyltransferase. Very recently, we have shown that Caenorhabditis elegans mboa-7, which belongs to the membrane-bound O-acyltransferase (MBOAT) family, encodes lysophosphatidylinositol (LPI)-specific acyltransferase (LPIAT). In this study, we found that knockdown of another member of the MBOAT family in C. elegans, named mboa-6, reduced incorporation of exogenous PUFAs into phosphatidylcholine (PC), phosphatidylserine (PS) and phosphatidylethanolamine (PE) in C. elegans. Knockdown of a human mboa-6 homologue, referred to as MBOAT5, also impaired the incorporation of PUFAs into PC, PS and PE in HeLa cells. In in vitro assays, lysoPC (LPC), lysoPS (LPS) and lysoPE (LPE) acyltransferase activities using [(14)C]arachidonoyl-CoA were significantly reduced in the microsomes of MBOAT5 knockdown cells. Conversely, over-expression of MBOAT5 in human embryonic kidney (HEK) 293 cells resulted in great increases in LPC, LPS and LPE acyltransferase activities but not in LPIAT or lysophosphatidic acid (LPA) acyltransferase (LPAAT) activities. These results indicate that human MBOAT5 is a lysophospholipid acyltransferase acting preferentially on LPC, LPS and LPE.
Shinji Matsuda; Takao Inoue; Hyeon-Cheol Lee; Nozomu Kono; Fumiharu Tanaka; Keiko Gengyo-Ando; Shohei Mitani; Hiroyuki Arai
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Genes to cells : devoted to molecular & cellular mechanisms     Volume:  13     ISSN:  1365-2443     ISO Abbreviation:  Genes Cells     Publication Date:  2008 Aug 
Date Detail:
Created Date:  2008-09-10     Completed Date:  2008-10-23     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9607379     Medline TA:  Genes Cells     Country:  England    
Other Details:
Languages:  eng     Pagination:  879-88     Citation Subset:  IM    
Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan.
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MeSH Terms
1-Acylglycerophosphocholine O-Acyltransferase / chemistry*,  genetics,  metabolism*
Amino Acid Sequence
Caenorhabditis elegans / enzymology*
Lysophosphatidylcholines / metabolism
Lysophospholipids / metabolism
Molecular Sequence Data
Sequence Alignment
Substrate Specificity
Reg. No./Substance:
0/Lysophosphatidylcholines; 0/Lysophospholipids; 0/lysophosphatidylethanolamine; 0/lysophosphatidylserine; EC O-Acyltransferase

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