Q192R polymorphism

Cole, T.B., Walter, B.J., Shih, D.M., Tward, A.D., Lusis, A.J., Timchalk, C., Richter, R.J., Costa, L.G., Furlong, C.E. (2005). Toxicity of chlorpyrifos and chlorpyrifos oxon in a transgenic mouse model of the human paraoxonase (PONl) Q192R polymorphism. Pharmacogenet. Genom. 15 589-98. 

Although strong evidence indicate.s that PONl levels and, in some cas es, the Q192R polymorphism determine the efficiency with which an individual will detoxify a specific OP, further proof in human populations is still needed. In particular, studies are needed in which PONl status is correlated with the degree of expo.sure and with signs and symptoms of toxicity. 

Bayrak, A., Bayrak, T., Tokgozoglu, S.L., et al., 2012. Serum PONl activity but not Q192R polymorphism is related to the extent of atherosclerosis. J. Atheroscler. Thromb. 19, 367—384. 

The human paraoxonase-1 (PONl) is a 45kDa calcium-dependent enzyme bound to high-density lipoprotein (HDL) particles, in association with other apolipoproteins. PON 1 shows a genetic polymorphism the most prominent determines the Q192R allozyme, which can have a substantial impact on PONl activity against OPs and arylesters (Smo-len et al, 1991) (Table 70.1). The enzyme was shown to be involved in the protection against atherosclerosis (Shih... 

FIG. 2. Gene structure of PONI. Note the two polymorphisms in the coding region (Q192R and L5.5M) and the polymorphisms in the 5 promoter region. 

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