Expression and activity of paraoxonase 1 in human cataractous lens tissue |
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| Authors: | Zehra Hashim Amber Ilyas Ammara Saleem Asmat Salim Shamshad Zarina |
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| Institution: | 1. University of Groningen, University Medical Center Groningen, Department of Cardiology, Groningen, The Netherlands;2. Eindhoven University of Technology, Department of Mathematics and Computer Science, Eindhoven, The Netherlands;3. University of Groningen, University Medical Center Groningen, Department of Nephrology, Groningen, The Netherlands;1. Cardiology Clinic, Department of Cardiac, Thoracic and Vascular Sciences, University of Padua, Padua, Italy;2. Department of Cardiology, S. Bortolo Hospital, Vicenza, Italy;3. Cardiovascular Interventional Unit, Cardiology Department, S. Anna Hospital, Como, Italy;4. Cardiology Division, San Giacomo Hospital, Castelfranco Veneto, Italy;5. Cardiovascular Department, Ospedali Riuniti di Bergamo, Bergamo, Italy;6. Cardiovascular Department, S. Maria dei Battuti Regional Hospital, Treviso, Italy;7. Cardiovascular Department, Ospedale dell''Angelo, Mestre, Italy;8. Conegliano Hospital, Conegliano, Italy;9. Catheterization Laboratory Cardiology Department, S. Chiara Hospital, Trento, Italy;10. SOC di Cardiologia, Azienda Ospedaliero-Universitaria S. Maria della Misericordia, Udine, Italy;11. Cardiovascular Department, Mirano Public Hospital, Mirano, Italy |
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| Abstract: | Paraoxonase 1 (PON1) is a high-density lipoprotein-associated enzyme that is believed to be involved in the protection against oxidative stress. There is evidence that paraoxonase activity is reduced in patients with diabetes and cataract. In the current study, we analyzed mRNA expression of PON1 as well as other members of the paraoxonase family, PON2 and PON3, in human cataractous lens samples. Our results indicate that only PON1 is expressed at the gene and protein levels in human lens tissues. We quantified MDA levels and measured PON1 (paraoxonase/arylesterase) enzymatic activities in subjects suffering from cataract due to aging and diabetes. Decreased PON1 activity was more pronounced in diabetic patients (p < 0.001) compared to senile subjects, which may be due to glycation and increased oxidative insult. To examine the structural alterations that occur in response to glycation, we constructed a three-dimensional model of PON1 and its glycated variant. Glycation at Lys70 and Lys75 is predicted to cause hindrance in binding of substrate to the active site of the enzyme. |
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