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Poster Display & Cocktail

60P - ALDH1 isoform landscape in breast cancer: Advancing precision therapies with a potent ALDH1A3-selective inhibitor

Date

03 Mar 2025

Session

Poster Display & Cocktail

Presenters

Andrada Constantinescu

Citation

Annals of Oncology (2025) 10 (suppl_2): 1-8. 10.1016/esmoop/esmoop104219

Authors

A. Constantinescu1, R. Pequerul2, R. Rebollido-Rios3, X. Pares Casasampera4, G. Fournet5, G. Martin6, I. Ceylan7, J. Farres4, M. Perez8

Author affiliations

  • 1 Research And Development, Advanced BioDesign, 69800 - Saint-Priest/FR
  • 2 Bioquímica I Biologia Molecular, Faculty of Biosciences- Universitat Autonoma de Barcelona, Biochemistry and Molecular Biology, 08193 - Barcelona/ES
  • 3 Internal Medicine, University Hospital of Cologne, 50931 - Cologne/DE
  • 4 Bioquímica I Biologia Molecular, Facultat de Biociències, 08193 - Barcelona/ES
  • 5 , Institut De Chimie Et Biochimie Moléculaire Et Supramoléculaire, Université de Claude Bernard-Lyon1, 69100 - Villeurbanne/FR
  • 6 Research And Development, Advanced Biodesign, 69800 - Saint-Priest/FR
  • 7 Research & Development, ADVANCED BIODESIGN, 69800 - Lyon/FR
  • 8 Research & Development, Advanced Biodesign, 69800 - Saint-Priest/FR

Resources

This content is available to ESMO members and event participants.

Abstract 60P

Background

Triple-negative breast cancer (TNBC) is among the most aggressive and clinically challenging breast cancer subtypes, marked by high metastatic potential, poor prognosis and limited treatment options. This underscores the urgent need to identify novel molecular targets for effective therapies. Aldehyde dehydrogenase 1 (ALDH1) enzymatic activity is a hallmark of cancer stem cells (CSCs), strongly associated with drug resistance, tumor aggressiveness, and metastasis, making it an attractive therapeutic target. However, the distinct roles of ALDH1 isoforms, particularly ALDH1A1 and ALDH1A3, remain poorly understood, hindering the rational design of selective inhibitors.

Methods

This study integrates bulk RNA-seq data from 1,103 primary breast tumors, 50 breast cancer cell lines, and single-cell RNA-seq data from 26 patients to characterize ALDH1 isoform expression across molecular subtypes and the tumor microenvironment.

Results

ALDH1A3 was predominantly expressed in basal-like TNBC tumors, primarily by epithelial tumor cells, while ALDH1A1 was enriched in stromal components, including myeloid cells and cancer-associated fibroblasts, implicating this isoform in immune suppression and metastasis.

Building on this insight, we developed a novel ALDH1A3-selective inhibitor derived from DIMATE, an ALDH1A1 inhibitor currently in clinical trials for AML. Structure-activity relationship studies identified a lead compound with enhanced selectivity for ALDH1A3, sparing the critical ALDH2 and ALDH3. Functional assays revealed that this inhibitor selectively induced apoptosis in ALDH1A3-expressing basal-like TNBC cell lines. Furthermore, it suppressed metastasis by inhibiting IL-6/JAK2/STAT3 and tPA/Src/FAK signaling pathways, potentially via a regulatory mechanism involving modulation of retinoic acid production mediated by ALDH1 in both tumor cells and the microenvironment. Preclinical TNBC models demonstrated its efficacy in reducing tumor growth and preventing distant metastases.

Conclusions

This work establishes ALDH1A3 as a promising biomarker and therapeutic target in basal-like TNBC, offering a promising approach to address unmet clinical needs in aggressive TNBC.

Clinical trial identification

Editorial acknowledgement

Legal entity responsible for the study

Advanced BioDesign.

Funding

Advanced BioDesign.

Disclosure

G. Fournet: Financial Interests, Personal, Stocks/Shares: Advanced BioDesign. G. Martin, I. Ceylan, M. Perez: Financial Interests, Personal and Institutional, Member of Board of Directors: Advanced BioDesign. All other authors have declared no conflicts of interest.

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