| Published Version Download ( PDF | 4MB) | License: Creative Commons Attribution 4.0 |
Mdm2 targeting via PROteolysis TArgeting Chimeras (PROTAC) is efficient in p53 wildtype, p53-mutated, and abemaciclib-resistant estrogen receptor-positive cell lines and superior to mdm2 inhibition
Article
Goerg, Alina, Piendl, Gerhard, Albert, Veruschka, Ortmann, Olaf
, Wege, Anja Kathrin
and Brockhoff, Gero
(2025)
Mdm2 targeting via PROteolysis TArgeting Chimeras (PROTAC) is efficient in p53 wildtype, p53-mutated, and abemaciclib-resistant estrogen receptor-positive cell lines and superior to mdm2 inhibition.
BMC Cancer 25 (1).
DOI to cite this document: 10.5283/epub.76841
Abstract
Purpose The human double minute 2 homolog hdm2, alias mdm2, is the main negative-regulator of the tumor suppressor p53. In that capacity, mdm2 is a promising but not yet utilized molecular target for the treatment of breast cancer, however, its inhibition by small molecules is rather inappropriate. Instead, mdm2 degradation by PROteolysis TArgeting Chimeras (PROTAC) is expected to be highly ...
Purpose
The human double minute 2 homolog hdm2, alias mdm2, is the main negative-regulator of the tumor suppressor p53. In that capacity, mdm2 is a promising but not yet utilized molecular target for the treatment of breast cancer, however, its inhibition by small molecules is rather inappropriate. Instead, mdm2 degradation by PROteolysis TArgeting Chimeras (PROTAC) is expected to be highly specific, to exhibit pronounced efficiency and minimal side effects. Moreover, there is profound evidence that mdm2-specific PROTAC degraders are efficient even in tumor cells harboring p53 loss-of-function mutations.
Methods
We comparatively treated p53 wildtype / abemaciclib-sensitive and -resistant MCF-7, as well as p53-mutated T-47D estrogen receptor-positive breast cancer cells in-vitro with the mdm2 inhibitor AMG-232 and an mdm2 PROTAC degrader. The molecular signaling as a function of mdm2 inhibition and degradation was assessed and cell viability and cell cycle kinetics were monitored. In addition, potential PROTAC effects on the expression of immune-related markers MHC-I, MHC-II, PD-L1, PD-L2, and CD276 were determined.
Results
PROTAC treatment considerably attenuated cell proliferations and was superior to mdm2 inhibition in p53 wildtype and even in p53-mutated cells. Proliferation-associated pathways were significantly but differentially affected, including p73, retinoblastoma protein, and the transcription factor E2F1. MHC-I and CD276 were significantly downregulated.
Conclusion
The data reveal deeper insight into PROTAC-induced molecular mechanisms in luminal breast cancer cells with and without p53 mutations. The study provides the basis to evaluate the therapeutic applicability of anti-mdm2 PROTAC degraders in an appropriate preclinical in-vivo setting, for example in humanized tumor mice.
Alternative links to fulltext
Involved Institutions
Details
| Item type | Article | ||||
| Journal or Publication Title | BMC Cancer | ||||
| Publisher | Springer | ||||
| Open Access Type | DEAL (Springer Gold) | ||||
| Volume | 25 | ||||
| Number of Issue or Book Chapter | 1 | ||||
| Date | 1 June 2025 | ||||
| Date of publication | 12 Jun 2025 04:28 | ||||
| Institutions | Medicine > Lehrstuhl für Frauenheilkunde und Geburtshilfe (Schwerpunkt Frauenheilkunde) | ||||
| Identification Number |
| ||||
| Keywords | Luminal breast cancer, Estrogen receptor-positive breast cancer, mdm2, p53 mutation, Abemaciclib, PROTAC | ||||
| Dewey Decimal Classification | 600 Technology > 610 Medical sciences Medicine | ||||
| Status | Published | ||||
| Refereed | Yes, this version has been refereed | ||||
| Created at the University of Regensburg | Yes | ||||
| URN of the UB Regensburg | urn:nbn:de:bvb:355-epub-768419 | ||||
| Item ID | 76841 |
Download Statistics
Download Statistics