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Resources » Paper

Shinji Matsuda et al. (2010) East Asia Worm Meeting "A member of the membrane-bound O-acyltransferase (MBOAT) family encodes a lysophospholipid acyltransferase with broad substrate specificity"

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  • Comments on Shinji Matsuda et al. (2010) East Asia Worm Meeting "A member of the membrane-bound O-acyltransferase (MBOAT) family encodes a lysophospholipid acyltransferase with broad substrate specificity" (0)

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    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00036602

    Shinji Matsuda, Takao Inoue, Keiko Gengyo-Ando, Shohei MItani, & Hiroyuki Arai (2010). A member of the membrane-bound O-acyltransferase (MBOAT) family encodes a lysophospholipid acyltransferase with broad substrate specificity presented in East Asia Worm Meeting. Unpublished information; cite only with author permission.

    Various kinds of fatty acids are distributed in membrane phospholipids in mammalian cells and tissues. In general, saturated fatty acids are esterified at the sn-1 position, whereas polyunsaturated fatty acids (PUFAs), such as arachidonic acid, are commonly found at the sn-2 position. It has long been assumed that lysophospholipid acyltransferases that catalyze the incorporation of PUFAs into lysophospholipids are responsible for the formation of phospholipid molecular species; however, these enzymes have not been isolated until recently because of their very fragile nature and small quantity in cells. Very recently, we have shown that C. 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 [14C]arachidonoyl-CoA were significantly reduced in the microsomes of MBOAT5 knockdown cells. Conversely, overexpression of MBOAT5 in 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. So far, the physiological significance of fatty acid molecular species in membrane phospholipids has not been elucidate. C. elegans genetics will open the door to reveal important new details about PUFAs in membrane phospholipids.


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