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Gardner Junior Faculty Research Fellowship"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Neurooncol"],"published-print":{"date-parts":[[2021,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec>\n                <jats:title>Introduction<\/jats:title>\n                <jats:p>A large subset of diffusely infiltrative gliomas contains a gain-of-function mutation in isocitrate dehydrogenase 1 or 2 (IDH1\/2<jats:sup>mut<\/jats:sup>) which produces 2-hydroxglutarate, an inhibitor of \u03b1-ketoglutarate-dependent DNA demethylases, thereby inducing widespread DNA and histone methylation. Because histone deacetylase (HDAC) enzymes are localized to methylated chromatin via methyl-binding domain proteins, IDH1\/2<jats:sup>mut<\/jats:sup> gliomas may be more dependent on HDAC activity, and therefore may be more sensitive to HDAC inhibitors.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Methods<\/jats:title>\n                <jats:p>Six cultured patient-derived glioma cell lines, IDH1<jats:sup>wt<\/jats:sup> (n\u2009=\u20093) and IDH1<jats:sup>mut<\/jats:sup> (n\u2009=\u20093), were treated with an FDA-approved HDAC inhibitor, panobinostat. Cellular cytotoxicity and proliferation assays were conducted by flow cytometry. Histone modifications and cell signaling pathways were assessed using immunoblot and\/or ELISA.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>IDH1<jats:sup>mut<\/jats:sup> gliomas exhibited marked upregulation of genes associated with the HDAC activity. Glioma cell cultures bearing IDH1<jats:sup>mut<\/jats:sup> were significantly more sensitive to the cytotoxic and antiproliferative effects of panobinostat, compared to IDH1<jats:sup>wt<\/jats:sup> glioma cells. Panobinostat caused a greater increase in acetylation of the histone residues H3K14, H3K18, and H3K27 in IDH1<jats:sup>mut<\/jats:sup> glioma cells. Another HDAC inhibitor, valproic acid, was also more effective against IDH1<jats:sup>mut<\/jats:sup> glioma cells.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusion<\/jats:title>\n                <jats:p>These data suggest that IDH1<jats:sup>mut<\/jats:sup> gliomas may be preferentially sensitive to HDAC inhibitors. Further, IDH1<jats:sup>mut<\/jats:sup> glioma cultures showed enhanced accumulation of acetylated histone residues in response to panobinostat treatment, suggesting a direct epigenetic mechanism for this sensitivity. This provides a rationale for further exploration of HDAC inhibitors against IDH1<jats:sup>mut<\/jats:sup> gliomas.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1007\/s11060-021-03829-0","type":"journal-article","created":{"date-parts":[[2021,8,23]],"date-time":"2021-08-23T12:03:27Z","timestamp":1629720207000},"page":"159-170","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["IDH1 mutant glioma is preferentially sensitive to the HDAC inhibitor panobinostat"],"prefix":"10.1007","volume":"154","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3834-2439","authenticated-orcid":false,"given":"Thomas K.","family":"Sears","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Craig M.","family":"Horbinski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin D.","family":"Woolard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,8,23]]},"reference":[{"key":"3829_CR1","doi-asserted-by":"publisher","first-page":"621","DOI":"10.1007\/s00401-013-1106-9","volume":"125","author":"C Horbinski","year":"2013","unstructured":"Horbinski C (2013) What do we know about IDH1\/2 mutations so far, and how do we use it? 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