Do iron chelators increase the antiproliferative effect of trichostatin A through a glucose-regulated protein 78 mediated mechanism?
 
Yazarlar (6)
Veli Kılınç
Public Health Laboratory, Türkiye
Abdülkerim Bedir
Ondokuz Mayis University, Medical School, Türkiye
Ali Okuyucu
Ondokuz Mayis University, Medical School, Türkiye
Osman Saliş
Ondokuz Mayis University, Medical School, Türkiye
Hasan Alaçam
Ondokuz Mayis University, Medical School, Türkiye
Doç. Dr. Sedat GÜLTEN Kastamonu Üniversitesi, Türkiye
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Tumor Biology
Dergi ISSN 1010-4283 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 06-2014
Kabul Tarihi Yayınlanma Tarihi 13-03-2014
Cilt / Sayı / Sayfa 35 / 6 / 5945–5951 DOI 10.1007/s13277-014-1788-1
Makale Linki http://dx.doi.org/10.1007/s13277-014-1788-1
UAK Araştırma Alanları
Tıbbi Biyokimya
Özet
Histone deacetylase (HDAC) inhibitors, such as trichostatin A (TSA), and iron chelators, including deferoxamine (DFO) and phenanthroline (PHEN), appear to have anticancer effects. We hypothesized that the HDAC inhibitors and iron chelators would be synergistic with their effect on breast cancer cell line MCF7, because the HDAC inhibitors increase glucose-regulated protein 78 (Grp78) and the iron chelators reduce its expression. Although the administration of TSA alone resulted in a dose-related decrease in the cell index, it did not have an antiproliferative effect except the 62.5 and 500 nM of TSA. However, all doses of TSA produced a cytotoxic effect from the initial hours when combined with 150 μM of DFO and 25 μM of PHEN. DFO and PHEN downregulated Grp78, Grp94, and MRP1 expressions and upregulated CHOP and HO-1 expressions. TSA upregulated all the genes in various rates when used …
Anahtar Kelimeler
CHOP | Deferoxamine | Grp78 | MCF-7 | Phenanthroline | Trichostatin A
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
Web of Science 2
Scopus 2
Google Scholar 3
Do iron chelators increase the antiproliferative effect of trichostatin A through a glucose-regulated protein 78 mediated mechanism?

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