Please use this identifier to cite or link to this item: https://doi.org/10.1182/blood-2012-04-424275
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dc.titleTargeting transcription factor SALL4 in acute myeloid leukemia by interrupting its interaction with an epigenetic complex
dc.contributor.authorGao, C.
dc.contributor.authorDimitrov, T.
dc.contributor.authorYong, K.J.
dc.contributor.authorTatetsu, H.
dc.contributor.authorJeong, H.-W.
dc.contributor.authorLuo, H.R.
dc.contributor.authorBradner, J.E.
dc.contributor.authorTenen, D.G.
dc.contributor.authorChai, L.
dc.date.accessioned2016-07-08T09:27:21Z
dc.date.available2016-07-08T09:27:21Z
dc.date.issued2013-02-21
dc.identifier.citationGao, C., Dimitrov, T., Yong, K.J., Tatetsu, H., Jeong, H.-W., Luo, H.R., Bradner, J.E., Tenen, D.G., Chai, L. (2013-02-21). Targeting transcription factor SALL4 in acute myeloid leukemia by interrupting its interaction with an epigenetic complex. Blood 121 (8) : 1413-1421. ScholarBank@NUS Repository. https://doi.org/10.1182/blood-2012-04-424275
dc.identifier.issn00064971
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/125461
dc.description.abstractAn exciting recent approach to targeting transcription factors in cancer is to block formation of oncogenic complexes. We investigated whether interfering with the interaction of the transcription factor SALL4, which is critical for leukemic cell survival, and its epigenetic partner complex represents a novel therapeutic approach. The mechanism of SALL4 in promoting leukemogenesis is at least in part mediated by its repression of the tumor suppressor phosphatase and tensin homolog deleted on chromosome 10 (PTEN) through its interaction with a histone deacetylase (HDAC) complex. In this study, we demonstrate that a peptide can compete with SALL4 in interacting with the HDAC complex and reverse its effect on PTEN repression. Treating SALL4-expressing malignant cells with this peptide leads to cell death that can be rescued by a PTEN inhibitor. The antileukemic effect of this peptide can be confirmed on primary human leukemia cells in culture and in vivo, and is identical to that of down-regulation of SALL4 in these cells using an RNAi approach. In summary, our results demonstrate a novel peptide that can block the specific interaction between SALL4 and its epigenetic HDAC complex in regulating its target gene, PTEN. Furthermore, targeting SALL4 with this approach could be an innovative approach in treating leukemia. © 2013 by The American Society of Hematology.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1182/blood-2012-04-424275
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentMEDICINE
dc.description.doi10.1182/blood-2012-04-424275
dc.description.sourcetitleBlood
dc.description.volume121
dc.description.issue8
dc.description.page1413-1421
dc.description.codenBLOOA
dc.identifier.isiut000321750000026
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