HL60 promyeloid cells express both classes of oestrogen receptor (ERα and ERβ). We show that hydrolysis of oestrone sulphate by steroid sulphatase is a major source of oestrone in HL60 cells, and that most of the released oestrone is not metabolized further to 17β-oestradiol. Treatment of HL60 cells with retinoids or 1α,25-dihydroxyvitamin D3 increased steroid sulphatase mRNA and activity in parallel with the induction of CD11b, an early marker of myeloid differentiation that is expressed before the differentiating cells stop proliferating. Use of agonists and antagonists against retinoid receptor-α and retinoid receptor-X revealed that both classes of retinoid receptor can drive steroid sulphatase up-regulation. Steroid sulphatase activity fluctuates during the cell cycle, being highest around the transition from G1 to S phase. During the differentiation of HL60 cells induced by all-trans-retinoic acid or 1α,25-dihydroxyvitamin D3, there is increased conversion of 17β-oestradiol into oestrone by an oxidative 17β-hydroxysteroid dehydrogenase. Treatment of Caco-2 colon adenocarcinoma cells with all-trans-retinoic acid or 1α,25-dihydroxyvitamin D3 also increases 17β-oestradiol oxidation to oestrone. An increase in local oestrone production therefore occurs in multiple cell types following treatment with retinoids and 1α,25-dihydroxyvitamin D3. The possible involvement of locally produced oestrogenic steroids in regulating the proliferation and differentiation of myeloid cells is discussed.
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April 2001
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Research Article|
April 06 2001
Up-regulation of steroid sulphatase activity in HL60 promyelocytic cells by retinoids and 1α,25-dihydroxyvitamin D3
Philip J. HUGHES;
Philip J. HUGHES
1
*LRF Differentiation Programme, Division of Immunity and Infection, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.,
1To whom correspondence should be addressed (e-mail [email protected]).
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Lucy E. TWIST;
Lucy E. TWIST
†School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Jennifer DURHAM;
Jennifer DURHAM
*LRF Differentiation Programme, Division of Immunity and Infection, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.,
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M. Ansar CHOUDHRY;
M. Ansar CHOUDHRY
*LRF Differentiation Programme, Division of Immunity and Infection, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.,
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Mark DRAYSON;
Mark DRAYSON
*LRF Differentiation Programme, Division of Immunity and Infection, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.,
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Roshantha CHANDRARATNA;
Roshantha CHANDRARATNA
‡Retinoid Research, Allergan Inc., Irvine, CA 92612, U.S.A.
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Robert H. MICHELL;
Robert H. MICHELL
*LRF Differentiation Programme, Division of Immunity and Infection, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.,
†School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Christopher J. KIRK;
Christopher J. KIRK
†School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Geoffrey BROWN
Geoffrey BROWN
*LRF Differentiation Programme, Division of Immunity and Infection, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.,
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Publisher: Portland Press Ltd
Received:
July 21 2000
Revision Received:
December 15 2000
Accepted:
February 02 2001
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 2001
2001
Biochem J (2001) 355 (2): 361–371.
Article history
Received:
July 21 2000
Revision Received:
December 15 2000
Accepted:
February 02 2001
Citation
Philip J. HUGHES, Lucy E. TWIST, Jennifer DURHAM, M. Ansar CHOUDHRY, Mark DRAYSON, Roshantha CHANDRARATNA, Robert H. MICHELL, Christopher J. KIRK, Geoffrey BROWN; Up-regulation of steroid sulphatase activity in HL60 promyelocytic cells by retinoids and 1α,25-dihydroxyvitamin D3. Biochem J 15 April 2001; 355 (2): 361–371. doi: https://doi.org/10.1042/bj3550361
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