fox-fordyce disease/glutathione

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Relation of glutathione S-transferase alpha and mu isoforms to response to therapy in human breast cancer.

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Glutathione S-transferase (GST) represents a multifunctional enzyme family consisting of four known cytosolic isoforms (alpha, mu, pi, and Phi) that detoxify a variety of xenobiotic chemicals and may confer resistance to both chemotherapeutic drugs and carcinogens in various experimental models.

Glutathione localisation in benign and malignant human breast lesions.

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Reduced glutathione (GSH) has been demonstrated in benign and malignant human breast lesions using a newly developed histofluorescence technique. GSH was present in every lesion and in each case was localised to the epithelium. A semi-quantitative assessment revealed a moderate amount of GSH in

Expression of glutathione S-transferase-pi in malignant skin tumors.

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GST-pi has been known to be markedly increased in human (pre) neoplasms of several organs. In this paper, the significance of immunohistochemical detection of GST-pi in human malignant tumors of the skin was studied. In specimens from 40 patients with various skin cancers, malignant melanoma,

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