Description
Inhibition of histone deacetylase (HDAC) enzymes by compounds such as trichostatin A can have wide ranging effects in cancer, cell differentiation, and other aspects of gene expression regulation. BML-210 is a small molecule inhibitor of HDAC with an IC
50 value of 30 μM when tested in HeLa cell nuclear extracts using 200 μM acetylated fluorometric substrate (substrate available in Cayman’s HDAC Activity and Inhibitor Screening Assay Kits -
Item Nos.
10011563 and
10011564).
Uses
N1-(2-Aminophenyl)-N8-phenyloctanediamide is a histone deacetylase (HDAC) inhibitor, an anti-cancer target for breast cancer therapeutic intervention.
Definition
ChEBI: A dicarboxylic acid diamide comprising suberic (octanedioic) acid coupled to aniline and 1,2-diaminobenzene.
Biochem/physiol Actions
BML-210 is a synthetic benzamide and is a potential tumor inhibitor. It is used as a therapeutic agent to treat promyelocytic leukemia. In human leukemia cell lines (NB4, HL-60, THP-1, and K562), BML-210 modulates histone deacetylase and promotes apoptosis. BML-210 favors frataxin expression in neurodegenerative disease Friedreich′s ataxia (FRDA). It interacts with myocyte enhancer factor-2 (MEF2) via hydrogen-bonding and prevents histone deacetylase 4 (HDAC4) binding.
in vivo
BML-210 (20 mg/kg; IP; three times per week for two weeks) notably suppresses the tumour growth and weight. BML-210 has no effect on tumour growth and weight in the immune-deficient nude (Nu/J) mice[3].
| Animal Model: | Female C57BL/6 mice with mouse breast cancer EO771 cells[3] |
| Dosage: | 20 mg/kg |
| Administration: | IP; three times per week for two weeks |
| Result: | Notably suppressed the tumour growth and weight.
|
References
[1] JURATE SAVICKIENE . The novel histone deacetylase inhibitor BML-210 exerts growth inhibitory, proapoptotic and differentiation stimulating effects on the human leukemia cell lines[J]. European journal of pharmacology, 2006, 549 1: Pages 9-18. DOI:
10.1016/j.ejphar.2006.08.010[2] DAVID HERMAN. Histone deacetylase inhibitors reverse gene silencing in Friedreich”s ataxia[J]. Nature chemical biology, 2006, 2 10: 551-558. DOI:
10.1038/nchembio815
