Rezvan Yazdian-Robati - Department of Biotechnology, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
Atena Pourtaji - Department of Pharmacodynamy and Toxicology, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
Marzieh Rashedinia - Department of Toxicology and pharmacology, School of Pharmacy, international branch, Shiraz University of Medical Sciences, Shiraz, Iran
Hossein Hosseinzadeh - Pharmaceutical Research Center, Department of Pharmacology and Toxicology, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
Maryam Ghorbani - Department of Pharmacology and Toxicology, School of Pharmacy, Baqiyatallah University of Medical Sciences, Tehran, Iran
BiBi Marjan Razavi - Targeted Drug Delivery Research Center, Department of Pharmacology and Toxicology, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
Mohammad Ramezani - Pharmaceutical Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
Khalil Abnous - Pharmaceutical Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran

Objective(s):Small ubiquitin-like modifiers (SUMOs) are a family of ubiquitin-related, proteins that are involved in a wide variety of signaling pathways. SUMOylation, as a vital post translational modification, regulate protein function in manycellular processes. Diazinon (DZN), an organophosphate insecticide, causses oxidative stress and subsequently programmed cell death in different tissues. The aim of this study was to evaluate the role and pattern of SUMO modificationas a defense mechanism against stress oxidative, in the heart tissuesof the DZN treated rats. Materials and Methods: Diazinon (۱۵ mg/kg/day), corn oil (control) were administered via gavageto male Wistar rats for four weeks. SUMO۱ antibody was covalently crosslinked to protein A/G agarose. heart tissue lysate were added to agarosebeads,After isolation of target proteins(SUMO۱- protein)SDS-PAGE gel electrophoresis was performed. Protein bands were identified using MALDI-TOF/TOF and MASCOT). Fold change of (DZN/Ctrl) separated proteins was evaluated using UVband software (UVITEC, UK). Results:Our result showed that subacute exposure to DZN increased SUMOylationoffour key proteins involved in the metabolic process including; Acyl-CoA dehydrogenase, creatine kinase, glyceraldehyde-۳-phosphate dehydrogenase and ATP synthase, in the heart tissue of animals .A probability value of  less than ۰.۰۵ was considered significant (P<۰.۰۵). Conclusion: It seems that protein SUMOylation provides a safeguard mechanism against DZN Toxicity.

Diazinon, MALDI-TOF/TOF, SUMOlation, SUMO۱