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Steroid sulfatase : molecular biology, regulation, and inhibition


Reference:

Reed, M. J., Purohit, A., Woo, L. W. L., Newman, S. P. and Potter, B. V. L., 2005. Steroid sulfatase : molecular biology, regulation, and inhibition. Endocrine Reviews, 26 (2), pp. 171-202.

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Official URL:

http://dx.doi.org/10.1210/er.2004-0003

Abstract

Steroid sulfatase (STS) is responsible for the hydrolysis of aryl and alkyl steroid sulfates and therefore has a pivotal role in regulating the formation of biologically active steroids. The enzyme is widely distributed throughout the body, and its action is implicated in physiological processes and pathological conditions. The crystal structure of the enzyme has been resolved, but relatively little is known about what regulates its expression or activity. Research into the control and inhibition of this enzyme has been stimulated by its important role in supporting the growth of hormone-dependent tumors of the breast and prostate. STS is responsible for the hydrolysis of estrone sulfate and dehydroepiandrosterone sulfate to estrone and dehydroepiandrosterone, respectively, both of which can be converted to steroids with estrogenic properties (i.e., estradiol and androstenediol) that can stimulate tumor growth. STS expression is increased in breast tumors and has prognostic significance. The role of STS in supporting tumor growth prompted the development of potent STS inhibitors. Several steroidal and nonsteroidal STS inhibitors are now available, with the irreversible type of inhibitor having a phenol sulfamate ester as its active pharmacophore. One such inhibitor, 667 COUMATE, has now entered a phase I trial in postmenopausal women with breast cancer. The skin is also an important site of STS activity, and deficiency of this enzyme is associated with X-linked ichthyosis. STS may also be involved in regulating part of the immune response and some aspects of cognitive function. The development of potent STS inhibitors will allow investigation of the role of this enzyme in physiological and pathological processes.

Details

Item Type Articles
CreatorsReed, M. J., Purohit, A., Woo, L. W. L., Newman, S. P. and Potter, B. V. L.
DOI10.1210/er.2004-0003
DepartmentsFaculty of Science > Pharmacy & Pharmacology
Faculty of Engineering & Design > Mechanical Engineering
RefereedYes
StatusPublished
ID Code1992

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