Paraoxonase (PON) is a class of aromatic alcohols that are synthesized by the liver and bind to high-density lipoproteins. It was discovered as early as 1953 and was named paraoxonase because it hydrolyzes the neurotoxic insecticide paraoxon. It is currently found that the mammalian paraoxonase gene family has three members: PON1, PON2 and PON3, which have structural homology and similar enzymatic activities. These three genes have a high degree of structural homology with approximately 65% and 70% identity at the amino acid level and the nucleotide level, respectively. Paraoxonase 1 (PON1) located on chromosome 7q21.3. is a hydrolyzed esterase synthesized in the liver. It is tight binding to apolipoprotein A1 in serum is based on the extremely hydrophobic N-terminus, a key enzyme in clopidogrel metabolism, involved in the regulation of PON1 transcription and translation. Studies have confirmed that PON1 can promote the hydrolysis of lipid peroxides, prevent LDL from being oxidatively modified, and thus prevent cerebral atherosclerosis. PON1 not only reduces oxidative stress but also is involved in the development and progression of various cancers. Studies have suggested that PON1 polymorphism may be associated with the risk of breast cancer. PON1 expression and genotype distribution vary widely among different populations. There are two common functional single nucleotide polymorphisms in the coding region of the PON1 gene, which are polymorphisms of LSSM and Q192R loci. Low activity of PON1 has been a risk factor for gastric cancer, systemic lupus erythematosus and cardiovascular disease.

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