AI Article Synopsis

  • The study identified the full-length cDNA of chicken neuropathy target esterase (cNTE), revealing its structure with a regulatory domain (cNTER) and a catalytic domain (cNEST).
  • Over-expression of cNTER did not exhibit NTE activity, while cNEST displayed this activity, indicating functional differences between the two regions.
  • Furthermore, cNTER accumulates in an endoplasmic reticulum-like pattern and is degraded through macroautophagy and proteasome pathways, unlike cNEST.

Article Abstract

Neuropathy target esterase (NTE) was proposed as the initial target during the process of organophosphate-induced delayed neuropathy (OPIDN) and adult hens are the animal model of OPIDN. However, little has been known about the sequence and characteristics of chicken NTE. Here, we firstly identified the full length cDNA of chicken NTE (cNTE), which contained an open reading frame of 3966 nucleotides encoding 1321 amino acids. Chicken NTE had two distinct regions, one was the regulatory domain (cNTER) and the other was the catalytic domain (cNEST). Over-expression of cNTER in mammalian cells did not show any NTE activity, whereas cNEST had NTE activity. Cells expressing cNTER tagged with green fluorescent protein (GFP) showed accumulation of cNTER-GFP in an endoplasmic reticulum-like localization pattern. In addition, macroautophagy and the proteasome pathways were found to be involved in the degradation of cNTER, but not cNEST. These results first showed that cNTE was an ER-anchored protein and degraded by macroautophagy as well as the proteasome.

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Source
http://dx.doi.org/10.1016/j.gene.2009.01.004DOI Listing

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