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@ARTICLE{Bhatia:845779,
author = {Bhatia, Sanil and Diedrich, Daniela and Frieg, Benedikt and
Ahlert, Heinz and Stein, Stefan and Bopp, Bertan and Lang,
Franziska and Zang, Tao and Kröger, Tobias and Ernst,
Thomas and Kögler, Gesine and Krieg, Andreas and Lüdeke,
Steffen and Kunkel, Hana and Rodrigues Moita, Ana J. and
Kassack, Matthias U. and Marquardt, Viktoria and Opitz,
Friederike V. and Oldenburg, Marina and Remke, Marc and
Babor, Florian and Grez, Manuel and Hochhaus, Andreas and
Borkhardt, Arndt and Groth, Georg and Nagel-Steger, Luitgard
and Jose, Joachim and Kurz, Thomas and Gohlke, Holger and
Hansen, Finn K. and Hauer, Julia},
title = {{T}argeting {HSP}90 dimerization via the {C}-terminus is
effective in imatinib resistant {CML} and lacks heat shock
response},
journal = {Blood},
volume = {132},
number = {3},
issn = {1528-0020},
address = {Stanford, Calif.},
publisher = {HighWire Press},
reportid = {FZJ-2018-02988},
pages = {307-320},
year = {2018},
abstract = {Heat shock protein 90 (HSP90) stabilizes many client
proteins including BCR-ABL1 oncoprotein. BCR-ABL1 is the
hallmark of CML in which treatment-free remission (TFR) is
limited with clinical and economic consequences. Thus, there
is an urgent need for novel therapeutics, which synergize
with current treatment approaches. Several inhibitors
targeting the N-terminal domain (NTD) of HSP90 are under
investigation; however, side effects such as induction of
heat shock response (HSR) and toxicity have so far precluded
their FDA approval. We have developed a novel inhibitor
(referred to as aminoxyrone) of HSP90 function by targeting
HSP90 dimerization via the C-terminal domain (CTD). This was
achieved by structure-based molecular design, chemical
synthesis, and functional pre-clinical in vitro and in vivo
validation using CML cell lines and patient-derived CML
cells. Aminoxyrone (AX) is a promising potential candidate,
which induces apoptosis in leukemic stem cells (LSCs)
fraction (CD34+CD38-) as well as the leukemic bulk
(CD34+CD38+) of primary CML and in TKI-resistant cells.
Furthermore, BCR-ABL1 oncoprotein and related pro-oncogenic
cellular responses are downregulated and targeting HSP90
C-terminus by AX does not induce HSR in vitro and in vivo.
We also probed the potential of AX in other therapy
refractory leukemia such as BCR-ABL1+ BCP-ALL, FLT3-ITD+ AML
and Ph-like BCP-ALL. Therefore, AX is the first peptidometic
C-terminal HSP90 inhibitor with the potential to increase
TFR in TKI sensitive and refractory CML patients and also
offers a novel therapeutic option for patients with other
therapy-refractory leukemia, due to its low toxicity profile
and lack of HSR.},
cin = {JSC / NIC / ICS-6},
ddc = {610},
cid = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
I:(DE-Juel1)ICS-6-20110106},
pnm = {511 - Computational Science and Mathematical Methods
(POF3-511) / 561 - Biological Key Regulators and Small
Chemical Compounds (POF3-561) / 316 - Infections and cancer
(POF3-316) / Forschergruppe Gohlke $(hkf7_20170501)$},
pid = {G:(DE-HGF)POF3-511 / G:(DE-HGF)POF3-561 /
G:(DE-HGF)POF3-316 / $G:(DE-Juel1)hkf7_20170501$},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:29724897},
UT = {WOS:000439131800011},
doi = {10.1182/blood-2017-10-810986},
url = {https://juser.fz-juelich.de/record/845779},
}