Kırıkkale İlinde Spermophilus xanthoprymnus ve Meriones tristrami’de Glutatyon S-Transferaz-Alfa ve Glutatyon S-Transferaz-Pi Ekspresyon Düzeylerinin Yaşam Koşulları ve Doğal Habitat Farklılıkları Açısından İncelenmesi

Abstract

Glutathione S-transferase (GST) is a multifunctional enzyme that provides homeostasis by catalyzing the first step in the formation of the end product mercapturic acid in the detoxification metabolic pathway. Being found in mammals, insects, fish, birds, annelids, molluscs, and many microorganisms, GST takes part the elimination of toxic substances taken into body by consuming food, and their transport by binding non-substrate ligands (e.g. heme and bilirubin) with GSH. In addition, it can prevent reactive electrophilic compounds from harming the body by covalent bonding similar compounds to each other. These xenobiotic acceptors affected by GST include nitrogen halogen compounds, organophosphates, and polycyclic aromatic hydrocarbons. Xenobiotics are oxygenated by this enzyme system, the next mechanism of oxygenated products is more oxygenation, and these products become more easily soluble in water. In this study, Glutathione S-Transferase was detected in the liver tissue of Spermophilus xanthoprymnus and Meriones tristrami and its characteristic features were determined. For this purpose, the animals were anesthetized with sodium pentobarbital and their liver tissues were harvested. After necessary preparations were completed, the samples were analyzed by using immunohistochemical staining method and the expressions of GST isozymes were determined. As a result, glutathione s-transferase-alpha and glutathione s-transferase-pi expression levels were found to differ in Spermophilus xanthoprymnus and Meriones tristrami samples obtained from different localities of Kırıkkale province. Differences in GST enzyme expression in these species indicate that both species differ in their detoxification capacity and response to xenobiotics.