Steroid Sulfatase Inhibitors: Their Potential in the Therapy of Breast Cancer

ISSN: 1875-5992 (Online)
ISSN: 1871-5206 (Print)

Volume 17, 14 Issues, 2017

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Anti-Cancer Agents in Medicinal Chemistry

Formerly: Current Medicinal Chemistry - Anti-Cancer Agents

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  • 27th of 59 in Chemistry, Medicinal

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Michelle Prudhomme
Institut de Chimie de Clermont-Ferrand
Université Clermont Auvergne

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Steroid Sulfatase Inhibitors: Their Potential in the Therapy of Breast Cancer

Anti-Cancer Agents in Medicinal Chemistry, 5(5): 507-528.

Author(s): P. Nussbaumer and A Billich.

Affiliation: Novartis Institutes for Bio-Medical Research, Brunnerstrasse 59, A-1235 Vienna, Austria.


Steroid sulfatase (STS) is the only well characterized enzyme in human cells that is capable to desulfate estrone 3-sulfate (E1S) and dehydroepiandrosterone sulfate (DHEAS) as a first step in the conversion of these precursors to active hormones. STS has been found to be highly expressed in estrogen-dependent breast tumors in post-menopausal women and is regarded as a crucial component of the local estrogen production that is required for tumor growth and survival. Inhibitors of STS are expected to block the intra-tumoral estrogen synthesis and, therefore, are considered as potential new therapeutic agents for the treatment of estrogen-dependent cancers of the breast and the endometrium. In this review, we give an overview on the current status in the field of medicinal chemistry of STS inhibitors. Newer developments comprise potent aryl sulfamate-based irreversible inhibitors, and several types of reversible inhibitors. Other directions include compounds with dual mode of action, such as compounds that block both STS and aromatase, or act as STS inhibitors and antiproliferative or antiangiogenic agents at the same time. In particular, these agents featuring an extended mode of action hold promise to be included in the armamentarium to fight endocrine-dependent cancer.


arylsulfatase, breast cancer, desulfation, steroid sulfatase, steroid sulfate, sulfamate.

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Article Details

Volume: 5
Issue Number: 5
First Page: 507
Last Page: 528
Page Count: 22
DOI: 10.2174/1568011054866955
Price: $58
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