Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 427, Issue 2, Pages 336-342Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.09.057
Keywords
Histone demethylase LSD1; S100A7; Breast cancer cells; Estrogen-mediated transcriptional regulation
Categories
Funding
- Korea Research Foundation
- Korean Government [KRF-2008-313-C00723]
- National R&D Program for Cancer Control, Ministry for Health, Welfare and Family affairs, Republic of Korea [0920260]
- National Research Foundation of Korea (NRF)
- Korea government (MEST) [20110030773]
- Basic Science Research Program through the National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology [2010-0010639]
- Mid-career Researcher Program through NRF
- MEST [2009-0083772]
- Brain Korea21 (BK21) Program
- Korea Health Promotion Institute [0920260] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2011-0030773, 2010-0010639] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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S100A7, a member of S100 calcium binding protein family, is highly associated with breast cancer. However, the molecular mechanism of S100A7 regulation remains unclear. Here we show that long-term treatment with estradiol stimulated S100A7 expression in MCF7 breast cancer cells at both the transcriptional and translational levels. Both treatment with a histone demethylase LSD1 inhibitor and shRNA-based knockdown of LSD1 expression significantly decreased 17 beta-estradiol (E2)-induced S100A7 expression. These reduced E2-mediated S100A7 expression are rescued by the overexpressed wild-type LSD1 but not by its catalytically inactive mutant. Our data showed in vivo association of 1501 with S100A7 promoters, confirming the potential role of LSD1 in regulating S100A7 expression. S100A7 knockdown increased both normal cell growth and estrogen-induced cell proliferation, suggesting a negative influence by S100A7 on the growth of cancer cells. Together, our data suggest that estrogen-induced S100A7 expression mediated by the histone demethylase 1501 may downregulate breast cancer cell proliferation, implying a potential tumor suppressor-like function for S100A7. (C) 2012 Elsevier Inc. All rights reserved.
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