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We Are Not Signatories of 1999] Category:EZLN Category:Zapatista Army of National LiberationGlutathione S-transferases (GST) are dimeric detoxification proteins that have the ability to remove glutathione (GSH) conjugates from the cell. In general, there are three classes of GST (alpha, mu and pi) and these are expressed in a tissue-specific manner. GSTA4 (alpha class) is highly expressed in the liver, whereas the mu and pi classes are preferentially expressed in the small intestine. Mice deficient in GSTA4 have a severe phenotype that resembles human metabolic syndrome with low blood pressure, hypoglycemia, hyperinsulinemia and glucose intolerance (Stacpoole, J. et al., 1998, Nature 393, 780). Mice deficient in GSTM1 are also resistant to alloxan induced diabetes, since the active drug is metabolized by the pi class GST and if the enzyme is absent the drug cannot be converted to its active form (de la Fuente, R. et al., 1995, Biochem. Biophys. Res. Comm. 211, 1537). It is thought that GSTs catalyse the formation of thioether adducts (S-glutathionylations) of protein thiol groups which are involved in a number of processes including: cytotoxicity, protein aggregation, protein degradation and post-translational modifications (Zaitseva, I. et al., 1998, Free Rad. Biol. Med. 23, 377). The relative importance of these pathways varies according to cell type. For example, in hepatocytes (a common site of expression for GSTA4) glutathione-S-transferase (GST) conjugates are formed and removed in the endoplasmic reticulum and can be retrieved in the plasma membrane where they are released from the cell via exocytosis (Raj, R. et al., 2004, J. Biol. Chem. 279, 18802). In contrast, in jejunal enterocytes (a common site of expression for GSTM1 and GSTM3) the glutathione-S-transferase (GST) conjugates are synthesized and retrieved in the cytoplasm, perhaps to be used for the synthesis of biosynthetic enzymes (Raj, R. et al., 2004, J. Biol.