Background:Acrylamide is a widespread substance with many areas of utilization. Acrylamide also forms a part of high-temperature-processed starchy foods. To date, numerous in vivo and in vitro studies have documented that acrylamide poses toxic effects on various organ systems.Aims:To determine the potential protective effect of L-cysteine on acrylamide-induced testicular toxicity.Study Design:Animal experimentation.Methods:We randomly divided 28 rats into four groups: control (0.9% saline), L-cysteine (150 mg/kg), acrylamide (40 mg/kg), and acrylamide+L-cysteine. After a 10-day intraperitoneal injection period, we euthanized the animals, recorded their body and testis weights, collected blood samples for serum testosterone measurement, and excised the testes for histopathological and morphometric evaluation. Immunohistochemical scoring of proliferating cell nuclear antigen and bax proteins was performed.Results:Acrylamide reduced body (p<0.01) and testis weights (p<0.05), seminiferous tubule diameter (p<0.001), and proliferating cell nuclear antigen expression (p<0.05) but increased bax protein expression (p<0.01) and the percentage of seminiferous tubules containing multinucleated giant cells (p<0.001). However, no significant change was observed in serum testosterone level of the experimental groups when compared with that of controls. L-cysteine administered with acrylamide decreased multinucleated giant cell number (p<0.001) and reversed the reduced proliferating cell nuclear antigen positivity (p<0.001) but showed no effect in restoring other parameters compared with the group treated with acrylamide alone.Conclusion:Considering the dose and duration employed, the present study concluded that L-cysteine partially protects testis against acrylamide-induced toxic effects.
Glutathione reductase [GR, E.C.1.8.1.7] catalyses NADPH dependent reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH). Thus, it is the crucial enzyme to maintain high [GSH]/[GSSG] ratio and physiological redox status in cells. Kidney and liver tissues were considered as a rich source of GR. In this study, rat kidney GR was purified and some of its properties were investigated. The enzyme was purified 2,356 fold with a yield of 16% by using heat-denaturation and Sephadex G25 gel filtration, 2',5'-ADP Agarose 4B, PBE94 column chromatographies. The purified enzyme had a specific activity (Vm) of 250 U/mg protein and the ratio of absorbances at wavelengths of A (273)/A (463,) A (280)/A (460), A (365)/A (460), and A (379)/A (463), were 7.1, 6.8, 1.2 and 1.0, respectively. Each mol of GR subunit bound 0.97 mol of FAD. NADH was used as a coenzyme by rat kidney GR but with a lower efficiency (32.7%) than NADPH. Its subunit molecular weight was estimated as 53 kDa. An optimum pH of 6.5 and optimum temperature of 65 degrees C were found for rat kidney GR. Its activation energy (Ea) and temperature coefficient (Q(10)) were calculated as 7.02 kcal/mol and 1.42, respectively. The Km((NADPH)) and kcat/Km ((NADPH)) values were found to be 15.3 +/- 1.4 microM and 1.68 x 10(7) M(-1) s(-1) for the concentration range of 10-200 microM NADPH and when GSSG is the variable substrate, the Km((GSSG)) and the kcat/Km((GSSG)) values of 53.1 +/- 3.4 microM and 4.85 x 10(6) M(-1) s(-1) were calculated for the concentration range of 20-1,200 microM GSSG.
Targeted therapies have come into prominence in the ongoing battle against non-small cell lung cancer (NSCLC) because of the shortcomings of traditional chemotherapy. In this context, indole-based small molecules, which were synthesized efficiently, were subjected to an in vitro colorimetric assay to evaluate their cyclooxygenase (COX) inhibitory profiles. Compounds 3b and 4a were found to be the most selective COX-1 inhibitors in this series with IC50 values of 8.90 µM and 10.00 µM, respectively. In vitro and in vivo assays were performed to evaluate their anti-NSCLC and anti-inflammatory action, respectively. 2-(1H-Indol-3-yl)-N′-(4-morpholinobenzylidene)acetohydrazide (3b) showed selective cytotoxic activity against A549 human lung adenocarcinoma cells through apoptosis induction and Akt inhibition. The in vivo experimental data revealed that compound 3b decreased the serum myeloperoxidase and nitric oxide levels, pointing out its anti-inflammatory action. Moreover, compound 3b diminished the serum aminotransferase (particularly aspartate aminotransferase) levels. Based on the in vitro and in vivo experimental data, compound 3b stands out as a lead anti-NSCLC agent endowed with in vivo anti-inflammatory action, acting as a dual COX-1 and Akt inhibitor.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.