This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Glutathione transferases (GSTs) are a large superfamily of isoenzymes essential for the metabolism of many drugs and other exogenously ingested compounds that are potentially toxic to cells. The diverse substrate specificities of the isoenzymes together afford protection to many chemicals including common anti-cancer chemotherapeutic agents such as chlorambucil and adriamycin. Although beneficial under normal physiological circumstances, it has been observed that various cancer cell lines over-express the class pi isoenzyme (hGSTP1-1). The over-expression may underlie resistance against chemotherapy developed by many tumours. GSTs catalyse the addition of glutathione to the electrophilic centre of the receiving substrate. The reaction renders the substrate less toxic and prepares it for export by certain transmembrane proteins for further metabolism. Several GST classes such as hGSTP1-1 are also involved in substrate storage by means of non-catalytic binding of the substrate. In particular, hGSTP1-1 can function as a carrier of nitric oxide (NO), in such forms as N- nitrosoglutathione (GSNO) and dinitrosyldiglutathionyl iron complex (DNDGIC). In this view, a potential role of hGSTP1-1 in signalling or modulating functions of other proteins may be hypothesised. Structures of hGSTP1-1 bound with various compounds will enable an understanding of how hGSTP1-1 performs its functions and any future design of hGSTP1-1 inhibitors for chemotherapy.
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