Prolidase gene

E2. Endo, F., Tanoue, A., Nakai, H Hata, A., Indo, Y., Titani, K., and Matsuda, I., Primary structure and gene localization of human prolidase. J. Biol. Chem. 264,4476-4481 (1989). 

Finally, in situ transient production of enzymes, if the need arises, will be possible by gene therapy in the future. Promising results have been published using short-induction gene vectors (adenoviral systems) for human PON-1 (Cowan et al., 2001 Bradshaw et al., 2005 Fu et al., 2005 Miyoshi et al., 2007 Guns et al., 2008 Duysen et al., 2011), human AChE (Li et al., 2006), hiunan BChE (Chilukuri et al., 2009 Parikh et al., 2011), mutated human BChE that displays high cocaine esterase (Gao et al., 2013), and human prolidase (Aleti et al., 2013). 

Costance, M., Biggemarm, L., Alamneh, Y., et al., 2012. Hydrolysis potential of recombinant human skin and kidney prolidase against diisopropylfluoro-phosphate and sarin by in vitro analysis. Toxicol. In Vitro 26,182-188. Cowan, J., Sinton, C.M., Varley, A.W., et al., 2001. Gene therapy to prevent organophosphate intoxication. Toxicol. Appl. Pharmacol. 173,1-6. 

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