Sulphation Catalyzed by the Human Cytosolic Sulphotransferases: Chemical Defense or Molecular Terrorism?

    Michael W.H. Coughtrie
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    TLDR Human enzymes can detoxify harmful substances but might also increase their cancer risk.
    The document from 1996 examines the functions of human cytosolic sulphotransferases (STs), which are involved in detoxifying xenobiotics and metabolizing endogenous compounds. It explains that STs can convert toxic substances into less harmful forms for excretion, but they can also increase the toxicity and carcinogenic potential of certain compounds. The paper discusses the enzymology of STs, their substrate specificities, and the influence of genetic and environmental factors on their activity. It notes the role of oestrogen sulphotransferase in the endometrium and its regulation by the menstrual cycle and progesterone, as well as the necessity of sulphation for the activation of minoxidil, a hair growth medication. The review emphasizes the need for further research to fully understand the complex roles of STs in health and disease, including their contribution to chemical carcinogenesis and the variability in individual responses due to genetic differences in ST expression.
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