Abstract
Glutathione transferase P1-1 (GSTP1-1) is expressed in some human tissues and is abundant in mammalian erythrocytes (here termed e-GST). This enzyme is able to detoxify the cell from endogenous and exogenous toxic compounds by using glutathione (GSH) or by acting as a ligandin. This review collects studies that propose GSTP1-1 as a useful biomarker in different fields of application. The most relevant studies are focused on GSTP1-1 as a biosensor to detect blood toxicity in patients affected by kidney diseases. In fact, this detoxifying enzyme is over-expressed in erythrocytes when unusual amounts of toxins are present in the body. Here we review articles concerning the level of GST in chronic kidney disease patients, in maintenance hemodialysis patients and to assess dialysis adequacy. GST is also over-expressed in autoimmune disease like scleroderma, and in kidney transplant patients and it may be used to check the efficiency of transplanted kidneys. The involvement of GSTP in the oxidative stress and in other human pathologies like cancer, liver and neurodegenerative diseases, and psychiatric disorders is also reported. Promising applications of e-GST discussed in the present review are its use for monitoring human subjects living in polluted areas and mammals for veterinary purpose.
Highlights
Glutathione transferases (GSTs) represent a superfamily of multifunctional proteins expressed in almost all eukaryotic and prokaryotic cells, able to detoxify against endogenous and exogenous toxic compounds [1,2]
By means of negative cooperativity, when one subunit of the enzyme has bound dinitrosyl-diglutathionyl-iron complex (DNDGIC), the other free subunit becomes unable to bind a second molecule [24]. This mechanism preserves GSTP1-1 from complete inactivation when it is involved in the DNDGIC detoxification, maintaining its classical conjugating activity even when an excess of nitric oxide (NO) is produced in the cell
One of the most recent studies, in which Asian osteosarcoma patients were analyzed, suggested that the GSTP1 gene polymorphism is associated with an increased risk of osteosarcoma, whereas the other GSTs gene polymorphisms may not influence the development of this cancer [156]
Summary
Glutathione transferases (GSTs) represent a superfamily of multifunctional proteins expressed in almost all eukaryotic and prokaryotic cells, able to detoxify against endogenous and exogenous toxic compounds [1,2]. In mammalian organisms, they are grouped into three major families: cytosolic GSTs, mitochondrial GSTs, and microsomal GSTs [1]. Many different gene-independent classes represent the cytosolic GSTs; each group of GST isoenzymes presents similar sequences and structural properties. While the Alpha class collects A1-1, A2-2, A3-3, A4-4 isoenzymes, the Pi class only contains one enzyme, the GSTP1-1 [2] These enzymes were discovered years ago ago [3]. Compounds (H-site) (Figure 1) [4]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
