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Vorinostat inhibits TP53. 16 / 17
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"LBH589 (100 nM) and SAHA (5 muM) depleted MDM2 and p53, and induced PTEN and acetyl H3 in all LPS lines."
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"XREF_BIBR, XREF_BIBR Similarly, SAHA, a histone deacetylase inhibitor, stimulates degradation of mutp53 by inhibiting HDAC6, a key positive regulator of HSP90."
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"15 described that HDAC inhibitor suberoylanilide hydroxamic acid, which shows limited clinical activity to solid tumors, reduces p53 activity in response to DNA damage."
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"SAHA downregulates mutp53 but not wtp53."
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"In the human cancer lines MDA-MB-231 (mutp53-R280K) and DLD1 (mutp53-S241F), SAHA induced a significant mutp53 degradation."
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"Additionally, vorinostat pre-treatment attenuated the stabilization of total p53 protein induced by epirubicin exposure."
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"Vorinostat pre-treatment significantly attenuated p53 stabilization in the presence of epirubicin (XREF_FIG)."
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"Vorinostat restores miR-150 and inhibits migration independently of p53 status."
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"Interestingly, the silencing of HDAC10 (XREF_SUPPLEMENTARY) resulted in the most efficient reduction of p53 (XREF_FIG), exhibiting a 25% decrease in protein expression, suggesting that the observed SAHA mediated reduction of HIF-1alpha and p53 is occurring through inhibition of different HDAC family members."
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"Altogether, it seemed that vorinostat repressed HIF1 and TP53 in DU 145, but had less effect in PC-3 and 22Rv1."
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"We found that SAHA or NaB, alone or in combination with camptothecin (CPT) treatment, inhibited accumulation of wild-type p53 protein in HCT116 cells (XREF_FIG)."
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"To test the above hypothesis that, like mutant p53, RUNX2 could contribute to SAHA resistance of p53 mutated pancreatic cancer cells, we sought to assess the possible impact of RUNX2 knockdown on SAHA mediated cell death and mutant p53 expression in MiaPaCa-2 cells."
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"In addition, HIF1A and TP53 protein were downregulated by vorinostat under normoxia and hypoxia in DU 145, but not in the others (XREF_FIG)."
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"We conclude that autophagy can be a relevant pathway for mutp53 degradation induced by SAHA, but its contribution to mutp53 destabilization and the consequences on cell death are likely context dependent."
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"This is due to degradation of mutp53 by SAHA, which is likely caused by hyperacetylation and inhibition of HSP90 through inactivation of HDAC6 by SAHA [XREF_BIBR]."
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"Taken together, these data imply that mechanistically SAHA causes mutp53 degradation by inducing functional reactivation of MDM2 and CHIP."