Physiological roles of glutathione in organism

Dominko, Kristina (2011) Physiological roles of glutathione in organism. Bachelor's thesis, Faculty of Science > Department of Biology.

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Abstract

Glutathione (γ-glutamylcysteinylglycine, GSH) is a tripeptid present in large levels in all mammalian tissues. It is synthetized within the cells of all organs, especially in the liver. The largest levels of GSH are present in cytosol, mitochondria and ER. GSH serves as antioxidant, detoxifying agent in a number of metabolism processes and it modulates cell events. There are two forms of GSH: reduced form (GSH) which can oxidize to disulphide (GSSG), GSH/GSSG ratio determines redox state of cells which is important factor in many processes. This review explaines roles of GSH as a regulator of cellular processes in a modulation of transcriptional factors and immune responses and, also, as a cofactor in proinflammatory mediators synthesis and NO-adduct formation. In conditions of oxidative stress, a decrease in GSH levels activates transcriptional factors NF-κB i AP-1 which then activate pro-inflammatory genes and cytokine genes expression. GSH has a double role in the immune system: it affects the decrease in cytokine synthesis which can enhance oxidative stress and, also, adequate levels of GSH are essential for T lymphocyte proliferation and successful immune response. In the synthesis of pro-inflammatory mediators, leukotrienes and prostaglandins, GSH serves as a cofactor in some of the steps catalyzed by special GSH-S transferase membrane-bound enzymes called MAPEG. NO can form an adduct with GSH forming S-nitrosoglutathione (GSNO) which by posttranslational modification through Sthiolation and S-glutathionilation can modify protein activity and additionally apoptosis inhibition or cell redox state.

Item Type: Thesis (Bachelor's thesis)
Supervisor: Đikić, Domagoj
Date: 2011
Number of Pages: 28
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 27 Oct 2014 10:21
Last Modified: 27 Oct 2014 10:21
URI: http://digre.pmf.unizg.hr/id/eprint/3170

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