Effects of timolol treatment on pancreatic antioxidant enzymes in streptozotocin-induced diabetic rats: An experimental and computational study

• DOI: 10.2478/jomb-2018-0034
• Publication Date: 2018-10-29T09:34:01Z
• Authors: Nuriye Nuray Ulusu; Muslum Gok; Burak Erman; Belma Turan
• Keywords: 0301 basic medicine; Original Paper; diabetes; Chemistry; Biochemistry and molecular biology; Diabetes; camp; QD415-436; timolol; Biochemistry; 3. Good health; Chemistry; 03 medical and health sciences; cAMP; glucose-6-phosphate dehydrogenase; Timolol; Biochemistry and molecular biology; 6-phosphogluconate dehydrogenase; cAMP; Diabetes; Glucose-6-phosphate dehydrogenase; Timolol; 6-phosphogluconate dehydrogenase; Glucose-6-phosphate dehydrogenase

SummaryBackgroundThe study aimed to investigate whether timolol-treatment has a beneficial effect on pentose phosphate pathway enzyme activities such as glucose-6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGDH) enzyme activities and cAMP level in streptozotocin-induced diabetic rats in pancreatic tissuesMethodsDiabetes was induced by streptozotocin (STZ) in 3-month old male Wistar rats. The diabetic rats were treated with timolol (5 mg/kg body weight, for 12 weeks) while the control group received saline. Enzyme activities were determined in pancreas tissue. To support our results, we performedin silicocalculations, using Protein Data Bank structures.ResultsTimolol treatment of STZ-induced diabetic rats had no noteworthy effect on high blood-glucose levels. However, this treatment induced activities of G6PD and 6PGDH in diabetic rats. Timolol treatment significantly increased cAMP level in diabetic pancreatic tissue. We found that timolol cannot bind strongly to either G6PD or 6PGD, but there is a relatively higher binding affinity to adenylyl cyclase, responsible for cAMP production, serving as a regulatory signal via specific cAMP-binding proteins.ConclusionsOur data point out that timolol treatment has beneficial effects on the antioxidant defence mechanism enzymes in the pancreas of STZ-induced diabetic rats.