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A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation resulting in pro-metastatic NF-κB signaling
P. Altea-Manzano, G. Doglioni, Y. Liu, AM. Cuadros, E. Nolan, J. Fernández-García, Q. Wu, M. Planque, KJ. Laue, F. Cidre-Aranaz, XZ. Liu, O. Marin-Bejar, J. Van Elsen, I. Vermeire, D. Broekaert, S. Demeyer, X. Spotbeen, J. Idkowiak, A. Montagne,...
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
Perzistentní odkaz
https://www.medvik.cz/link/bmc23003938
- MeSH
- acetylace MeSH
- acetylkoenzym A metabolismus MeSH
- karnitin-O-palmitoyltransferasa metabolismus MeSH
- lysinové acetyltransferasy * metabolismus MeSH
- myši MeSH
- NF-kappa B * metabolismus MeSH
- palmitany MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Metabolic rewiring is often considered an adaptive pressure limiting metastasis formation; however, some nutrients available at distant organs may inherently promote metastatic growth. We find that the lung and liver are lipid-rich environments. Moreover, we observe that pre-metastatic niche formation increases palmitate availability only in the lung, whereas a high-fat diet increases it in both organs. In line with this, targeting palmitate processing inhibits breast cancer-derived lung metastasis formation. Mechanistically, breast cancer cells use palmitate to synthesize acetyl-CoA in a carnitine palmitoyltransferase 1a-dependent manner. Concomitantly, lysine acetyltransferase 2a expression is promoted by palmitate, linking the available acetyl-CoA to the acetylation of the nuclear factor-kappaB subunit p65. Deletion of lysine acetyltransferase 2a or carnitine palmitoyltransferase 1a reduces metastasis formation in lean and high-fat diet mice, and lung and liver metastases from patients with breast cancer show coexpression of both proteins. In conclusion, palmitate-rich environments foster metastases growth by increasing p65 acetylation, resulting in a pro-metastatic nuclear factor-kappaB signaling.
Cancer Research UK Beatson Institute Glasgow UK
Department of Oncology KU Leuven Leuven Belgium
Department of Pathology University Hospitals Leuven KU Leuven Leuven Belgium
Hopp Children's Cancer Center Heidelberg Germany
Institute of Pathology Heidelberg University Hospital Heidelberg Germany
Laboratory for Angiogenesis and Vascular Metabolism VIB KU Leuven Leuven Belgium
Laboratory for Molecular Biology of Leukemia VIB KU Leuven Leuven Belgium
Laboratory for Molecular Cancer Biology VIB Center for Cancer Biology Leuven Belgium
Laboratory for Translational Breast Cancer Research Department of Oncology KU Leuven Leuven Belgium
Laboratory of Experimental Oncology Department of Oncology KU Leuven Leuven Belgium
Laboratory of Lipid Metabolism and Cancer Department of Oncology KU Leuven Leuven Belgium
Laboratory of Translational Genetics Department of Human Genetics KU Leuven Leuven Belgium
Laboratory of Translational Genetics VIB Center for Cancer Biology Leuven Belgium
Laboratory of Tumor Inflammation and Angiogenesis VIB Center for Cancer Biology Leuven Belgium
School of Cancer Sciences University of Glasgow Glasgow UK
SciLifeLab Department of Microbiology Tumor and Cell Biology Karolinska Institute Solna Sweden
The Francis Crick Institute London UK
Université Paris Cité NF kappaB Différenciation et Cancer Paris France
Citace poskytuje Crossref.org
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- $a Altea-Manzano, Patricia $u Laboratory of Cellular Metabolism and Metabolic Regulation, VIB-KU Leuven Center for Cancer Biology, Leuven, Belgium $u Laboratory of Cellular Metabolism and Metabolic Regulation, Department of Oncology, KU Leuven and Leuven Cancer Institute (LKI), Leuven, Belgium $1 https://orcid.org/0000000270752051
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- $a A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation resulting in pro-metastatic NF-κB signaling / $c P. Altea-Manzano, G. Doglioni, Y. Liu, AM. Cuadros, E. Nolan, J. Fernández-García, Q. Wu, M. Planque, KJ. Laue, F. Cidre-Aranaz, XZ. Liu, O. Marin-Bejar, J. Van Elsen, I. Vermeire, D. Broekaert, S. Demeyer, X. Spotbeen, J. Idkowiak, A. Montagne, M. Demicco, HF. Alkan, N. Rabas, C. Riera-Domingo, F. Richard, T. Geukens, M. De Schepper, S. Leduc, S. Hatse, Y. Lambrechts, EJ. Kay, S. Lilla, A. Alekseenko, V. Geldhof, B. Boeckx, C. de la Calle Arregui, G. Floris, JV. Swinnen, JC. Marine, D. Lambrechts, V. Pelechano, M. Mazzone, S. Zanivan, J. Cools, H. Wildiers, V. Baud, TGP. Grünewald, U. Ben-David, C. Desmedt, I. Malanchi, SM. Fendt
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- $a Metabolic rewiring is often considered an adaptive pressure limiting metastasis formation; however, some nutrients available at distant organs may inherently promote metastatic growth. We find that the lung and liver are lipid-rich environments. Moreover, we observe that pre-metastatic niche formation increases palmitate availability only in the lung, whereas a high-fat diet increases it in both organs. In line with this, targeting palmitate processing inhibits breast cancer-derived lung metastasis formation. Mechanistically, breast cancer cells use palmitate to synthesize acetyl-CoA in a carnitine palmitoyltransferase 1a-dependent manner. Concomitantly, lysine acetyltransferase 2a expression is promoted by palmitate, linking the available acetyl-CoA to the acetylation of the nuclear factor-kappaB subunit p65. Deletion of lysine acetyltransferase 2a or carnitine palmitoyltransferase 1a reduces metastasis formation in lean and high-fat diet mice, and lung and liver metastases from patients with breast cancer show coexpression of both proteins. In conclusion, palmitate-rich environments foster metastases growth by increasing p65 acetylation, resulting in a pro-metastatic nuclear factor-kappaB signaling.
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