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J. Biol. Chem., Vol. 283, Issue 9, 5908-5917, February 29, 2008

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Identification of an Insulin-regulated Lysophospholipase with Homology to Neuropathy Target Esterase^*

From the Institute of Molecular Biosciences, University of Graz 8010, Graz, Austria

Neuropathy target esterase (NTE) is a member of the family of patatin domain-containing proteins and exhibits phospholipase activity in brain and cultured cells. NTE was originally identified as target enzyme for organophosphorus compounds that cause a delayed paralyzing syndrome with degeneration of nerve axons. Here we show that the structurally related murine protein NTE-related esterase (NRE) is a potent lysophospholipase. The enzyme efficiently hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid. No lipase activity was observed when triacylglycerols, cholesteryl esters, retinyl esters, phosphatidylcholine, or monoacylglycerol were used as substrates. Although NTE is predominantly expressed in the nervous system, we found the highest NRE mRNA levels in testes, skeletal muscle, cardiac muscle, and adipose tissue. Induction of NRE mRNA concentrations in these tissues during fasting suggested a nutritional regulation of enzyme expression and, in accordance with this observation, insulin reduced NRE mRNA levels in a dose-dependent manner in 3T3-L1 adipocytes. A green fluorescent protein-NRE fusion protein colocalized to the endoplasmic reticulum and lipid droplets. Thus, NRE is a previously unrecognized ER- and lipid droplet-associated lysophospholipase. Regulation of enzyme expression by the nutritional status and insulin suggests a role of NRE in the catabolism of lipid precursors and/or mediators that affect energy metabolism in mammals.

Received for publication, November 26, 2007

^* This work was supported in part by the Grant "GOLD-Genomics of Lipid-associated Disorders," which is part of the Austrian Genome project "GEN-AU Genome Research in Austria" funded by the Austrian Ministry of Science and Research and by the Austrian Science Foundation (FWF) Grants W901-B05 DK (Molecular Enzymology) and F30 SFB-LIPOTOX. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Inst. of Molecular Biosciences, University of Graz, Heinrichstrasse 31, A-8010 Graz, Austria. Tel.: 43-316-380-1901; Fax: 43-316-380-9016; E-mail: rudolf.zechner{at}uni-graz.at.

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