Glutathione S transferase and multidrug resistance.docVIP

Glutathione S transferase and multidrug resistance.doc

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Glutathione S transferase and multidrug resistance

 PAGE \* MERGEFORMAT 30 Glutathione S transferase and multidrug resistance Keywords: glutathione S  transferase ; tumor Tumor resistance to chemotherapeutic drugs is one of the factors leading to treatment failure [1,2]. Resistant cancer cells could be divided into intrinsic drug resistance (intrinsic drug resistance) and acquired drug resistance (acquired drug resistance) into two categories, namely, the presence of primary drug resistance in certain tumors, known as intrinsic drug resistance; secondary to chemotherapy resistance, known as acquired drug resistance. According to drug-resistant spectrum can be divided into the original drug resistance (primary drug resistence, PDR) and multi-drug resistance (multidrug resistance, MDR). PDR is only induced by the original drug resistant, while for other drugs do not produce cross-resistance. Multi-drug resistance is defined as a drug-induced, while the other structures and mechanisms of a variety of different cross-resistance to anticancer drugs. In recent years, chemotherapy resistance mechanisms and how to overcome its resistance to become the focus of the study. Domestic and international studies have shown that drug-resistance related to reduced intracellular drug concentration, drug target changes and metabolic detoxification, DNA damage and repair capabilities to enhance a variety of mechanisms, with a variety of resistance-related genes [3]. In which glutathione  S  transferase (glutathione S  transferase, GST) and the closely related multidrug resistance, is now on its structure, functions and related research are reviewed. A reduced glutathione and glutathione  S  transferase π in structure and function of Glutathione is the body of a high content of the three thiol-containing peptides, glutamate by γ    cysteine-glycine structure, its main function is to protect the destruction of thiol oxidants on protection of sulfhydryl-containing membrane protein and thiol-co

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