posted on 2016-01-06, 00:00authored byA. Silva, J. Wang, S. Lomahan, T.- A. Tran, L. Grenlin, A. Suganami, Y. Tamura, N. Ikegaki
OSU-03012, a 3-phosphoinositide-dependent
kinase-1 (PDK1) inhibitor, destabilizes MYCN and MYC
proteins in neuroblastoma cells. However, AKT phosphorylation
is barely detectable in neuroblastoma cells under normal
culture conditions whether treated with OSU-03012 or not.
This observation suggests that PDK1 is not the main target of
OSU-03012 to destabilize MYC and MYCN in neuroblastoma
cells. In the present study, we explored one of the possible
mechanisms by which OSU-03012 destabilizes MYC and
MYCN. Since Aurora kinase A is reported to phosphorylate
GSK3β, leading to its inactivation, we hypothesized that one
of the targets of OSU-03012 is Aurora kinase A. Comparative
analysis of OSU-03012 and VX-680, a potent and specific
inhibitor of Aurora kinases, showed that both inhibitors
destabilized MYC and MYCN and were significantly growth
suppressive to neuroblastoma cell lines. In silico molecular
docking analysis further showed that the calculated interaction
energy between Aurora kinase A and OSU-03012 was
-109.901 kcal/mol, which was lower than that (-89.273 kcal/mol)
between Aurora kinase A and FXG, an Aurora kinase-specific
inhibitor. Finally, an in vitro Aurora kinase A inhibition assay
using a recombinant Aurora kinase A showed that OSU-03012
significantly inhibited Aurora kinase A, although it was weaker
in potency than that of VX-680. Thus, OSU-03012 has a likelihood
of binding to and inhibiting Aurora kinase A in vivo.
These results suggest that OSU-03012 affects multiple cellular
targets, including Aurora kinase A, to exhibit its growth
suppressive and MYC and MYCN-destabilizing effects on
neuroblastoma and other cancer cells.
Funding
The present study was supported by the NIH grant CA127571
and a grant from the St. Baldrick's Foundation.