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      Molecular Variant of the Human Paraoxonase/Arylesterase Gene Is Associated with Central Retinal Vein Occlusion in the Japanese Population

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          Central retinal vein occlusion (CRVO) is a complex trait caused by a number of local and systemic factors. Among the latter, atherosclerosis has been attributed a major pathogenic role. Recently, the paraoxonase/arylesterase (PONA) enzyme has been implicated in the pathogenesis of atherosclerosis. There is a 10- to 40-fold variability in the activity of this enzyme among individuals. This variability is due to the presence of an A/G polymorphism in the coding region of the gene. The A and G alleles code for glutamine (A genotype) and arginine (B genotype), respectively. We determined the PONA genotypes and alleles in 42 patients with CRVO and in 45 control subjects of the Japanese population. The distribution of AA, AB and BB genotypes were 9.6, 45.2 and 45.2%, respectively, in the patients and 26.7, 53.3 and 20.0% in the control subjects, respectively (p < 0.05). The A allele frequency was 0.32 in patients and 0.53 in controls (p < 0.01). In conclusion, molecular variants of the PONA gene are involved in the predisposition to CRVO. Further studies are needed to characterize the molecular mechanism by which the PONA enzyme is involved in atherosclerosis.

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          Is paraoxonase related to atherosclerosis.

          Human serum paraoxonase is responsible for the hydrolysis of organophosphate anticholinesterases, however, whether the enzyme has a physiological role other than the detoxication of insecticides and nerve gases has remained uncertain. Recently, evidence has begun to accumulate of a relationship between the serum activity of paraoxonase and atherosclerosis. Paraoxonase may a fundamental role in lipoprotein metabolism, preventing oxidative changes to low-density lipoprotein which render the particle atherogenic.
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            Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification.

            Human and rabbit paraoxonases/arylesterases were purified to homogeneity by chromatographic and gel electrophoretic/isofocusing procedures coupled with activity stains. N-terminal and peptide sequence analysis suggested retention of the secretion signal sequence and allowed design of oligonucleotide probes. The probes were used to isolate a 1294-bp rabbit paraoxonase cDNA clone, which, in turn, was used to isolate three human cDNA clones. Comparison of rabbit and human protein and cDNA sequences indicated a high degree of sequence conservation (approximately 85% identity) and verified that paraoxonase retains its signal sequence (except for the N-terminal Met). The rabbit cDNA encodes a protein of 359 amino acids and the human a protein of 355 amino acids. In situ hybridization demonstrated, as expected, that the paraoxonase gene maps to the long arm of human chromosome 7. Arginine at position 192 specifies high activity paraoxonase and glutamine low activity human paraoxonase. Variation in protein levels explains the variation of enzyme activity observed within a genetic class. Toxicity studies showed that raising rat plasma paraoxonase levels by i.v. administration of partially purified rabbit paraoxonase protected animals against cholinesterase inhibition by paraoxon and chlorpyrifos oxon. Protection correlated with the relative rates of hydrolysis of these two compounds.

              Author and article information

              S. Karger AG
              August 1998
              18 June 1998
              : 212
              : 4
              : 257-259
              Department of Ophthalmology, Yamagata University School of Medicine, Yamagata, Japan
              27303 Ophthalmologica 1998;212:257–259
              © 1998 S. Karger AG, Basel

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              Pages: 3
              Original Paper · Travail original · Originalarbeit


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