Background of the antigen
Members of the glutathione S-transferase (GST) family of proteins function in the detoxification of xenobiotics to protect cells against toxicant-induced damage. GSTs are differentially expressed in lung, liver and kidney tissue. Three isoforms, GSTA1-1, GSTA1-4 and GSTM1, localize to the mitochondria in addition to the cytoplasm. In normal and transformed cells, the oncoprotein Myb transcriptionally upregulates GSTM1. This isoform shows high specific activity for aflatoxin B1 epoxide conjugation, suggesting an important role for this interaction in the defense against both chemical and oxidative stress. The C-terminal domain of GSTA1 may form a component of the hydrophobic substrate-binding site, but in contrast appears not to be directly involved in GSH binding and is not absolutely essential for catalytic activity.
