Molecular cloning and expression of the C-terminal domain of mouse NTE-related esterase.

Mol Cell Biochem

Key Laboratory of Molecular Biology, College of Bio-information, Chongqing University of Posts and Telecommunications, Chongqing 400065, PR China.

Published: December 2007

AI Article Synopsis

  • NTE-related esterase (NRE) is similar to the neuropathy target esterase (NTE) and its function has been largely unexplored until now.
  • Research successfully cloned and expressed the mouse NRE gene, demonstrating that it exhibits esterase activity in mammalian cells, particularly localized in the cytoplasm.
  • Gene expression analysis revealed that NRE is more prevalent in the brain and testis compared to other tissues, providing new insights into its distribution and confirming its functional activity.

Article Abstract

NTE-related esterase (NRE), conserved in mouse, rat and human, was a member of patatin-like phospholipases (PLPLA) with high homology to neuropathy target esterase (NTE). Little has been known about the characteristics of NRE and NRE functional esterase activity has yet not been defined. The C-terminal gene sequence of mouse NRE (mNREC) encoding 923-1,326 amino acid containing the patatin domain was first cloned and then expressed tagged with enhanced green fluorescence protein (EGFP) in mammalian cells. The results showed that mNREC had NTE esterase activity in mammalian cells. Overexpression of mNREC did not affect the esterase activity sensitive to paraoxon or resistant to both paraoxon and mipafox. mNREC was distributed in the cytoplasm in contrast to the distribution of human NTE esterase domain. The expression analysis of NRE gene in adult mouse tissues by semi-quantitative reverse transcription-polymerase chain reaction (RT-PCR) showed that there were higher levels of NRE mRNA in the brain and testis than in the liver and kidney, which was about 50% and 35% of that in the brain. These results firstly showed the tissue distribution of NRE gene in adult mouse and defined that NRE had functional esterase activity.

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Source
http://dx.doi.org/10.1007/s11010-007-9550-2DOI Listing

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