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Publications (10 of 30) Show all publications
Carvalho, G., Nguyen, T. V. H., Repolês, B. M., Forslund, J., Wijethunga, R., Ranjbarian, F., . . . Wanrooij, P. H. (2025). Activating AMPK improves pathological phenotypes due to mtDNA depletion. The FEBS Journal
Open this publication in new window or tab >>Activating AMPK improves pathological phenotypes due to mtDNA depletion
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2025 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658Article in journal (Refereed) Epub ahead of print
Abstract [en]

AMP-activated protein kinase (AMPK) is a master regulator of cellular energy homeostasis that also plays a role in preserving mitochondrial function and integrity. Upon a disturbance in the cellular energy state that increases AMP levels, AMPK activity promotes a switch from anabolic to catabolic metabolism to restore energy homeostasis. However, the level of severity of mitochondrial dysfunction required to trigger AMPK activation is currently unclear, as is whether stimulation of AMPK using specific agonists can improve the cellular phenotype following mitochondrial dysfunction. Using a cellular model of mitochondrial disease characterized by progressive mitochondrial DNA (mtDNA) depletion and deteriorating mitochondrial metabolism, we show that mitochondria-associated AMPK becomes activated early in the course of the advancing mitochondrial dysfunction, before any quantifiable decrease in the ATP/(AMP + ADP) ratio or respiratory chain activity. Moreover, stimulation of AMPK activity using the specific small-molecule agonist A-769662 alleviated the mitochondrial phenotypes caused by the mtDNA depletion and restored normal mitochondrial membrane potential. Notably, the agonist treatment was able to partially restore mtDNA levels in cells with severe mtDNA depletion, while it had no impact on mtDNA levels of control cells. The beneficial impact of the agonist on mitochondrial membrane potential was also observed in cells from patients suffering from mtDNA depletion. These findings improve our understanding of the effects of specific small-molecule activators of AMPK on mitochondrial and cellular function and suggest a potential application for these compounds in disease states involving mtDNA depletion.

Place, publisher, year, edition, pages
John Wiley & Sons, 2025
Keywords
AMP-activated protein kinase, AMPK, mitochondrial DNA depletion, polymerase ɣ
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-235386 (URN)10.1111/febs.70006 (DOI)001415309200001 ()39918244 (PubMedID)2-s2.0-85217025089 (Scopus ID)
Funder
Swedish Research Council, 2019-01874Swedish Cancer Society, 19 0022 JIAKnut and Alice Wallenberg Foundation, 2021-0053Swedish Society for Medical Research (SSMF), S17-0023Åke Wiberg Foundation, M20-0132Swedish Cancer Society, 22 2381 Pj
Available from: 2025-02-19 Created: 2025-02-19 Last updated: 2025-02-19
Abrahamsson, A., Berner, A., Golebiewska-Pikula, J., Chaudhari, N., Keskitalo, E., Lindgren, C., . . . Chorell, E. (2025). Linker design principles for the precision targeting of oncogenic G-quadruplex DNA with G4-ligand-conjugated oligonucleotides. Bioconjugate chemistry, 36(4), 724-736
Open this publication in new window or tab >>Linker design principles for the precision targeting of oncogenic G-quadruplex DNA with G4-ligand-conjugated oligonucleotides
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2025 (English)In: Bioconjugate chemistry, ISSN 1043-1802, E-ISSN 1520-4812, Vol. 36, no 4, p. 724-736Article in journal (Refereed) Published
Abstract [en]

G-quadruplex (G4) DNA structures are noncanonical secondary structures found in key regulatory regions of the genome, including oncogenic promoters and telomeres. Small molecules, known as G4 ligands, capable of stabilizing G4s hold promise as chemical probes and therapeutic agents. Nevertheless, achieving precise specificity for individual G4 structures within the human genome remains a significant challenge. To address this, we expand upon G4-ligand-conjugated oligonucleotides (GL-Os), a modular platform combining the stabilizing properties of G4-ligands with the sequence specificity of guide DNA oligonucleotides. Central to this strategy is the linker that bridges the G4 ligand and the guide oligonucleotide. In this study, we develop multiple conjugation strategies for the GL-Os that enabled a systematic investigation of the linker in both chemical composition and length, enabling a thorough assessment of their impact on targeting oncogenic G4 DNA. Biophysical, biochemical, and computational evaluations revealed GL-Os with optimized linkers that exhibited enhanced binding to target G4s, even under thermal or structural stress. Notably, longer linkers broadened the range of targetable sequences without introducing steric hindrance, thereby enhancing the platform’s applicability across diverse genomic contexts. These findings establish GL-Os as a robust and versatile tool for the selective targeting of individual G4s. By facilitating precise investigations of G4 biology, this work provides a foundation for advancing G4-targeted therapeutic strategies and exploring their role in disease contexts.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2025
National Category
Biochemistry
Identifiers
urn:nbn:se:umu:diva-237287 (URN)10.1021/acs.bioconjchem.5c00008 (DOI)001448909600001 ()40112195 (PubMedID)2-s2.0-105000394779 (Scopus ID)
Funder
Swedish Research Council, VR-MH 2023-02160Swedish Research Council, VR-NT 2021-04805The Kempe Foundations, JCK-3159The Kempe Foundations, SMK21-0059Knut and Alice Wallenberg FoundationSwedish Cancer Society, 23 2793 PjSwedish Research Council, VR-MH 2023-02160Swedish Research Council, VR-NT 2021-04805The Kempe Foundations, JCK-3159The Kempe Foundations, SMK21-0059Knut and Alice Wallenberg FoundationSwedish Cancer Society, 23 2793 Pj
Available from: 2025-04-07 Created: 2025-04-07 Last updated: 2025-05-28Bibliographically approved
Aasumets, K., Hangas, A., Fragkoulis, G., Bader, C. P. J., Erdinc, D., Wanrooij, S., . . . Pohjoismäki, J. L. O. (2025). MRE11-independent effects of Mirin on mitochondrial DNA integrity and cellular immune responses. Molecular Biology of the Cell, 36(2), Article ID ar11.
Open this publication in new window or tab >>MRE11-independent effects of Mirin on mitochondrial DNA integrity and cellular immune responses
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2025 (English)In: Molecular Biology of the Cell, ISSN 1059-1524, E-ISSN 1939-4586, Vol. 36, no 2, article id ar11Article in journal (Refereed) Published
Abstract [en]

Mirin, a chemical inhibitor of MRE11, has been recently reported to suppress immune response triggered by mitochondrial DNA (mtDNA) breakage and release during replication stalling. We show that while Mirin reduces mitochondrial replication fork breakage in mitochondrial 3´-exonuclease MGME1 deficient cells, this effect occurs independently of MRE11. We also discovered that Mirin directly inhibits cellular immune responses, as shown by its suppression of STAT1 phosphorylation in Poly (I:C)-treated cells. Furthermore, Mirin also altered mtDNA supercoiling and accumulation of hemicatenated replication termination intermediates-hallmarks of topoisomerase dysfunction-while mitigating topological changes induced by the overexpression of mitochondrial TOP3A, including TOP3A-dependent strand breakage at the noncoding region of mtDNA. Although Mirin does not seem to inhibit TOP3A activity in vitro, our findings demonstrate its MRE11-independent effects in cells and give insight into the mechanisms of the maintenance of mtDNA integrity.

Place, publisher, year, edition, pages
American Society for Cell Biology (ASCB), 2025
National Category
Cell Biology Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-235673 (URN)10.1091/mbc.E24-01-0002 (DOI)39705374 (PubMedID)2-s2.0-85217518889 (Scopus ID)
Funder
Academy of Finland, 325015Academy of Finland, 338227Academy of Finland, 332458
Available from: 2025-03-04 Created: 2025-03-04 Last updated: 2025-04-01Bibliographically approved
Matsuda, S., Nakayama, M., Do, Y., Ishiuchi, T., Yagi, M., Wanrooij, S., . . . Yasukawa, T. (2025). TEFM facilitates transition from RNA synthesis to DNA synthesis at H-strand replication origin of mtDNA. Communications Biology, 8(1), Article ID 202.
Open this publication in new window or tab >>TEFM facilitates transition from RNA synthesis to DNA synthesis at H-strand replication origin of mtDNA
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2025 (English)In: Communications Biology, E-ISSN 2399-3642, Vol. 8, no 1, article id 202Article in journal (Refereed) Published
Abstract [en]

Transcription of human mitochondrial DNA (mtDNA) begins from specific transcription promoters. In strand-asynchronous mtDNA replication, transcripts from the light-strand promoter serve as primers for leading-strand synthesis at the origin of the H-strand replication (OH). A 7S DNA strand, a presumed aborted replication product, is also synthesized from OH. Transition from RNA synthesis to DNA synthesis at OH is crucial for balancing replication with transcription, yet the mechanism remains unclear. Herein, we examine the role of mitochondrial transcription elongation factor (TEFM) in this process. TEFM knockout results in decreased 7S DNA, strand-asynchronous replication intermediates, and mtDNA copy number, all of which are concordant with downregulation of RNA-to-DNA transition at OH. Conversely, levels of tRNAs encoded near transcription promoters increase, indicating enhanced transcription initiation frequency. Taken together, we propose that, in addition to conferring processivity to the mitochondrial RNA polymerase, TEFM plays a crucial role in maintaining the balance between mitochondrial transcription and replication.

Place, publisher, year, edition, pages
Springer Nature, 2025
National Category
Biochemistry Molecular Biology Cell Biology
Identifiers
urn:nbn:se:umu:diva-235988 (URN)10.1038/s42003-025-07645-4 (DOI)001416636900001 ()39922921 (PubMedID)2-s2.0-85218242660 (Scopus ID)
Available from: 2025-03-18 Created: 2025-03-18 Last updated: 2025-03-18Bibliographically approved
Forslund, J. M. .., Nguyen, T. V. H., Parkash, V., Berner, A., Goffart, S., Pohjoismäki, J. L. .., . . . Wanrooij, S. (2025). The POLγ Y951N patient mutation disrupts the switch between DNA synthesis and proofreading, triggering mitochondrial DNA instability. Proceedings of the National Academy of Sciences of the United States of America, 122(16), Article ID e2417477122.
Open this publication in new window or tab >>The POLγ Y951N patient mutation disrupts the switch between DNA synthesis and proofreading, triggering mitochondrial DNA instability
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2025 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 122, no 16, article id e2417477122Article in journal (Refereed) Published
Abstract [en]

Mitochondrial DNA (mtDNA) stability, essential for cellular energy production, relies on DNA polymerase gamma (POLγ). Here, we show that the POLγ Y951N disease-causing mutation induces replication stalling and severe mtDNA depletion. However, unlike other POLγ disease-causing mutations, Y951N does not directly impair exonuclease activity and only mildly affects polymerase activity. Instead, we found that Y951N compromises the enzyme’s ability to efficiently toggle between DNA synthesis and degradation, and is thus a patient-derived mutation with impaired polymerase-exonuclease switching. These findings provide insights into the intramolecular switch when POLγ proofreads the newly synthesized DNA strand and reveal a new mechanism for causing mitochondrial DNA instability.

Place, publisher, year, edition, pages
Proceedings of the National Academy of Sciences (PNAS), 2025
Keywords
DNA polymerases, mitochondria, mitochondrial disease, mtDNA, mtDNA replication
National Category
Medical Genetics and Genomics
Identifiers
urn:nbn:se:umu:diva-238484 (URN)10.1073/pnas.2417477122 (DOI)40238457 (PubMedID)2-s2.0-105003483574 (Scopus ID)
Funder
Swedish Research Council, 2019-01874Swedish Cancer Society, 19 0022 JIASwedish Cancer Society, 22 2381 PjKnut and Alice Wallenberg Foundation, KAW 2021.0053Swedish Society of Medicine, S17-0023Swedish Research Council, 2021-01104Swedish Cancer Society, 23 2999 Pj
Available from: 2025-05-07 Created: 2025-05-07 Last updated: 2025-05-07Bibliographically approved
Andréasson, M., Donzel, M., Abrahamsson, A., Berner, A., Doimo, M., Quiroga, A., . . . Chorell, E. (2024). Exploring the dispersion and electrostatic components in arene-arene interactions between ligands and G4 DNA to develop G4-ligands. Journal of Medicinal Chemistry, 67(3), 2202-2219
Open this publication in new window or tab >>Exploring the dispersion and electrostatic components in arene-arene interactions between ligands and G4 DNA to develop G4-ligands
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2024 (English)In: Journal of Medicinal Chemistry, ISSN 0022-2623, E-ISSN 1520-4804, Vol. 67, no 3, p. 2202-2219Article in journal (Refereed) Published
Abstract [en]

G-Quadruplex (G4) DNA structures are important regulatory elements in central biological processes. Small molecules that selectively bind and stabilize G4 structures have therapeutic potential, and there are currently >1000 known G4 ligands. Despite this, only two G4 ligands ever made it to clinical trials. In this work, we synthesized several heterocyclic G4 ligands and studied their interactions with G4s (e.g., G4s from the c-MYC, c-KIT, and BCL-2 promoters) using biochemical assays. We further studied the effect of selected compounds on cell viability, the effect on the number of G4s in cells, and their pharmacokinetic properties. This identified potent G4 ligands with suitable properties and further revealed that the dispersion component in arene-arene interactions in combination with electron-deficient electrostatics is central for the ligand to bind with the G4 efficiently. The presented design strategy can be applied in the further development of G4-ligands with suitable properties to explore G4s as therapeutic targets.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2024
National Category
Medicinal Chemistry
Identifiers
urn:nbn:se:umu:diva-220319 (URN)10.1021/acs.jmedchem.3c02127 (DOI)001160609500001 ()38241609 (PubMedID)2-s2.0-85183093324 (Scopus ID)
Funder
The Kempe Foundations, JCK-3159The Kempe Foundations, SMK-1632Swedish Research Council, 2017-05235Swedish Research Council, 2021-04805Knut and Alice Wallenberg Foundation
Available from: 2024-02-13 Created: 2024-02-13 Last updated: 2025-04-24Bibliographically approved
Berner, A., Das, R. N., Bhuma, N., Golebiewska, J., Abrahamsson, A., Andréasson, M., . . . Chorell, E. (2024). G4-ligand-conjugated oligonucleotides mediate selective binding and stabilization of individual G4 DNA structures. Journal of the American Chemical Society, 146(10), 6926-6935
Open this publication in new window or tab >>G4-ligand-conjugated oligonucleotides mediate selective binding and stabilization of individual G4 DNA structures
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2024 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 146, no 10, p. 6926-6935Article in journal (Refereed) Published
Abstract [en]

G-quadruplex (G4) DNA structures are prevalent secondary DNA structures implicated in fundamental cellular functions, such as replication and transcription. Furthermore, G4 structures are directly correlated to human diseases such as cancer and have been highlighted as promising therapeutic targets for their ability to regulate disease-causing genes, e.g., oncogenes. Small molecules that bind and stabilize these structures are thus valuable from a therapeutic perspective and helpful in studying the biological functions of the G4 structures. However, there are hundreds of thousands of G4 DNA motifs in the human genome, and a long-standing problem in the field is how to achieve specificity among these different G4 structures. Here, we developed a strategy to selectively target an individual G4 DNA structure. The strategy is based on a ligand that binds and stabilizes G4s without selectivity, conjugated to a guide oligonucleotide, that specifically directs the G4-Ligand-conjugated oligo (GL-O) to the single target G4 structure. By employing various biophysical and biochemical techniques, we show that the developed method enables the targeting of a unique, specific G4 structure without impacting other off-target G4 formations. Considering the vast amount of G4s in the human genome, this represents a promising strategy to study the presence and functions of individual G4s but may also hold potential as a future therapeutic modality.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2024
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:umu:diva-222294 (URN)10.1021/jacs.3c14408 (DOI)001179314400001 ()38430200 (PubMedID)2-s2.0-85186374110 (Scopus ID)
Funder
The Kempe Foundations, JCK-3159The Kempe Foundations, SMK-1632The Kempe Foundations, SMK21-0059Swedish Research Council, 2017-05235Swedish Research Council, 2021-04805Swedish Research Council, 2018-0278Cancerforskningsfonden i Norrland, AMP19-968Knut and Alice Wallenberg Foundation, SMK21-0059
Available from: 2024-03-20 Created: 2024-03-20 Last updated: 2025-04-07Bibliographically approved
Manjunath, P., Stojkovic, G., Euro, L., Konovalova, S., Wanrooij, S., Koski, K. & Tyynismaa, H. (2024). Preferential binding of ADP-bound mitochondrial HSP70 to the nucleotide exchange factor GRPEL1 over GRPEL2. Protein Science, 33(11), Article ID e5190.
Open this publication in new window or tab >>Preferential binding of ADP-bound mitochondrial HSP70 to the nucleotide exchange factor GRPEL1 over GRPEL2
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2024 (English)In: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 33, no 11, article id e5190Article in journal (Refereed) Published
Abstract [en]

Human nucleotide exchange factors GRPEL1 and GRPEL2 play pivotal roles in the ADP–ATP exchange within the protein folding cycle of mitochondrial HSP70 (mtHSP70), a crucial chaperone facilitating protein import into the mitochondrial matrix. Studies in human cells and mice have indicated that while GRPEL1 serves as an essential co-chaperone for mtHSP70, GRPEL2 has a role regulated by stress. However, the precise structural and biochemical mechanisms underlying the distinct functions of the GRPEL proteins have remained elusive. In our study, we present evidence revealing that ADP-bound mtHSP70 exhibits remarkably higher affinity for GRPEL1 compared to GRPEL2, with the latter experiencing a notable decrease in affinity upon ADP binding. Additionally, Pi assay showed that GRPEL1, but not GRPEL2, enhanced the ATPase activity of mtHSP70. Utilizing Alphafold modeling, we propose that the interaction between GRPEL1 and mtHSP70 can induce the opening of the nucleotide binding cleft of the chaperone, thereby facilitating the release of ADP, whereas GRPEL2 lacks this capability. Additionally, our findings suggest that the redox-regulated Cys87 residue in GRPEL2 does not play a role in dimerization but rather reduces its affinity for mtHSP70. Our findings on the structural and functional disparities between GRPEL1 and GRPEL2 may have implications for mitochondrial protein folding and import processes under varying cellular conditions.

Place, publisher, year, edition, pages
John Wiley & Sons, 2024
Keywords
Alphafold, co-chaperone, cysteines, GRPEL1, GRPEL2, interactions, mitochondria, mtHSP70, nucleotide exchange factor
National Category
Biochemistry Molecular Biology Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-231360 (URN)10.1002/pro.5190 (DOI)001368205600001 ()39445986 (PubMedID)2-s2.0-85207509829 (Scopus ID)
Available from: 2024-11-11 Created: 2024-11-11 Last updated: 2025-04-24Bibliographically approved
Doimo, M., Chaudhari, N., Abrahamsson, S., L'Hôte, V., Nguyen, T. V. H., Berner, A., . . . Wanrooij, S. (2023). Enhanced mitochondrial G-quadruplex formation impedes replication fork progression leading to mtDNA loss in human cells. Nucleic Acids Research, 51(14), 7392-7408
Open this publication in new window or tab >>Enhanced mitochondrial G-quadruplex formation impedes replication fork progression leading to mtDNA loss in human cells
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2023 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 51, no 14, p. 7392-7408Article in journal (Refereed) Published
Abstract [en]

Mitochondrial DNA (mtDNA) replication stalling is considered an initial step in the formation of mtDNA deletions that associate with genetic inherited disorders and aging. However, the molecular details of how stalled replication forks lead to mtDNA deletions accumulation are still unclear. Mitochondrial DNA deletion breakpoints preferentially occur at sequence motifs predicted to form G-quadruplexes (G4s), four-stranded nucleic acid structures that can fold in guanine-rich regions. Whether mtDNA G4s form in vivo and their potential implication for mtDNA instability is still under debate. In here, we developed new tools to map G4s in the mtDNA of living cells. We engineered a G4-binding protein targeted to the mitochondrial matrix of a human cell line and established the mtG4-ChIP method, enabling the determination of mtDNA G4s under different cellular conditions. Our results are indicative of transient mtDNA G4 formation in human cells. We demonstrate that mtDNA-specific replication stalling increases formation of G4s, particularly in the major arc. Moreover, elevated levels of G4 block the progression of the mtDNA replication fork and cause mtDNA loss. We conclude that stalling of the mtDNA replisome enhances mtDNA G4 occurrence, and that G4s not resolved in a timely manner can have a negative impact on mtDNA integrity.

Place, publisher, year, edition, pages
Oxford University Press, 2023
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-214069 (URN)10.1093/nar/gkad535 (DOI)001030190900001 ()37351621 (PubMedID)2-s2.0-85168980694 (Scopus ID)
Funder
Knut and Alice Wallenberg FoundationSwedish Research Council, VR-MH 2018-0278Swedish Research Council, VR-NT 2017-05235The Kempe Foundations, SMK-1632Wenner-Gren FoundationsEU, Horizon 2020, 751474Swedish Foundation for Strategic Research, RIF14-0081
Available from: 2023-09-05 Created: 2023-09-05 Last updated: 2025-04-07Bibliographically approved
Akhunzianov, A. A., Nesterova, A. I., Wanrooij, S., Filina, Y. V., Rizvanov, A. A. & Miftakhova, R. R. (2023). Unravelling the Therapeutic Potential of Antibiotics in Hypoxia in a Breast Cancer MCF-7 Cell Line Model. International Journal of Molecular Sciences, 24(14), Article ID 11540.
Open this publication in new window or tab >>Unravelling the Therapeutic Potential of Antibiotics in Hypoxia in a Breast Cancer MCF-7 Cell Line Model
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2023 (English)In: International Journal of Molecular Sciences, ISSN 1661-6596, E-ISSN 1422-0067, Vol. 24, no 14, article id 11540Article in journal (Refereed) Published
Abstract [en]

Antibiotics inhibit breast cancer stem cells (CSCs) by suppressing mitochondrial biogenesis. However, the effectiveness of antibiotics in clinical settings is inconsistent. This inconsistency raises the question of whether the tumor microenvironment, particularly hypoxia, plays a role in the response to antibiotics. Therefore, the goal of this study was to evaluate the effectiveness of five commonly used antibiotics for inhibiting CSCs under hypoxia using an MCF-7 cell line model. We assessed the number of CSCs through the mammosphere formation assay and aldehyde dehydrogenase (ALDH)-bright cell count. Additionally, we examined the impact of antibiotics on the mitochondrial stress response and membrane potential. Furthermore, we analyzed the levels of proteins associated with therapeutic resistance. There was no significant difference in the number of CSCs between cells cultured under normoxic and hypoxic conditions. However, hypoxia did affect the rate of CSC inhibition by antibiotics. Specifically, azithromycin was unable to inhibit sphere formation in hypoxia. Erythromycin and doxycycline did not reduce the ratio of ALDH-bright cells, despite decreasing the number of mammospheres. Furthermore, treatment with chloramphenicol, doxycycline, and tetracycline led to the overexpression of the breast cancer resistance protein. Our findings suggest that hypoxia may weaken the inhibitory effects of antibiotics on the breast cancer model.

Place, publisher, year, edition, pages
MDPI, 2023
Keywords
antibiotics, breast cancer, cancer stem cells, hypoxia, mitochondria
National Category
Cancer and Oncology Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-212713 (URN)10.3390/ijms241411540 (DOI)001038566100001 ()37511298 (PubMedID)2-s2.0-85165983164 (Scopus ID)
Available from: 2023-08-15 Created: 2023-08-15 Last updated: 2023-08-15Bibliographically approved
Projects
The role of mitochondrial DNA double strand break repair in human disease and normal aging. [2011-02419_VR]; Umeå UniversityThe mechanisms underlying mitochondrial DNA deletion formation in human disease. [2018-02781_VR]; Umeå University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-6126-4382

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