IFNγ protects motor neurons from oxidative stress via enhanced global protein synthesis in FUS‐associated amyotrophic lateral sclerosis
Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global protein synthesis, but the mechanism that drives this has not been established. Here, we used ALS6 patient‐derived induced pluripotent stem...
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| Published in | Brain pathology (Zurich, Switzerland) Vol. 34; no. 1; pp. e13206 - n/a |
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| Main Authors | , , , , , , , , , |
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John Wiley & Sons, Inc
01.01.2024
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| Abstract | Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global protein synthesis, but the mechanism that drives this has not been established. Here, we used ALS6 patient‐derived induced pluripotent stem cells (hIPSCs) to study the effect of the ALS6 FUSR521H mutation on the translation machinery in motor neurons (MNs). We find, in agreement with findings of others, that protein synthesis is decreased in FUSR521H MNs. Furthermore, FUSR521H MNs are more sensitive to oxidative stress and display reduced expression of TGF‐β and mTORC gene pathways when stressed. Finally, we show that IFNγ treatment reduces apoptosis of FUSR521H MNs exposed to oxidative stress and partially restores the translation rates in FUSR521H MNs. Overall, these findings suggest that a functional IFNγ response is important for FUS‐mediated protein synthesis, possibly by FUS nuclear translocation in ALS6.
FUS R521H motor neurons derived from IPSCs exhibit reduced viability, decreased protein synthesis, and diminished cytokine production when exposed to oxidative stress. Treatment with IFNy improves translation rates and mitigates apoptosis caused by oxidative injury. |
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| AbstractList | Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global protein synthesis, but the mechanism that drives this has not been established. Here, we used ALS6 patient‐derived induced pluripotent stem cells (hIPSCs) to study the effect of the ALS6 FUSR521H mutation on the translation machinery in motor neurons (MNs). We find, in agreement with findings of others, that protein synthesis is decreased in FUSR521H MNs. Furthermore, FUSR521H MNs are more sensitive to oxidative stress and display reduced expression of TGF‐β and mTORC gene pathways when stressed. Finally, we show that IFNγ treatment reduces apoptosis of FUSR521H MNs exposed to oxidative stress and partially restores the translation rates in FUSR521H MNs. Overall, these findings suggest that a functional IFNγ response is important for FUS‐mediated protein synthesis, possibly by FUS nuclear translocation in ALS6.
FUS R521H motor neurons derived from IPSCs exhibit reduced viability, decreased protein synthesis, and diminished cytokine production when exposed to oxidative stress. Treatment with IFNy improves translation rates and mitigates apoptosis caused by oxidative injury. Abstract Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global protein synthesis, but the mechanism that drives this has not been established. Here, we used ALS6 patient‐derived induced pluripotent stem cells (hIPSCs) to study the effect of the ALS6 FUS R521H mutation on the translation machinery in motor neurons (MNs). We find, in agreement with findings of others, that protein synthesis is decreased in FUS R521H MNs. Furthermore, FUS R521H MNs are more sensitive to oxidative stress and display reduced expression of TGF‐β and mTORC gene pathways when stressed. Finally, we show that IFN γ treatment reduces apoptosis of FUS R521H MNs exposed to oxidative stress and partially restores the translation rates in FUS R521H MNs. Overall, these findings suggest that a functional IFN γ response is important for FUS‐mediated protein synthesis, possibly by FUS nuclear translocation in ALS6. Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global protein synthesis, but the mechanism that drives this has not been established. Here, we used ALS6 patient-derived induced pluripotent stem cells (hIPSCs) to study the effect of the ALS6 FUS mutation on the translation machinery in motor neurons (MNs). We find, in agreement with findings of others, that protein synthesis is decreased in FUS MNs. Furthermore, FUS MNs are more sensitive to oxidative stress and display reduced expression of TGF-β and mTORC gene pathways when stressed. Finally, we show that IFNγ treatment reduces apoptosis of FUS MNs exposed to oxidative stress and partially restores the translation rates in FUS MNs. Overall, these findings suggest that a functional IFNγ response is important for FUS-mediated protein synthesis, possibly by FUS nuclear translocation in ALS6. Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global protein synthesis, but the mechanism that drives this has not been established. Here, we used ALS6 patient‐derived induced pluripotent stem cells (hIPSCs) to study the effect of the ALS6 FUS R521H mutation on the translation machinery in motor neurons (MNs). We find, in agreement with findings of others, that protein synthesis is decreased in FUS R521H MNs. Furthermore, FUS R521H MNs are more sensitive to oxidative stress and display reduced expression of TGF‐β and mTORC gene pathways when stressed. Finally, we show that IFN γ treatment reduces apoptosis of FUS R521H MNs exposed to oxidative stress and partially restores the translation rates in FUS R521H MNs. Overall, these findings suggest that a functional IFN γ response is important for FUS‐mediated protein synthesis, possibly by FUS nuclear translocation in ALS6. FUS R521H motor neurons derived from IPSCs exhibit reduced viability, decreased protein synthesis, and diminished cytokine production when exposed to oxidative stress. Treatment with IFNy improves translation rates and mitigates apoptosis caused by oxidative injury. Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global protein synthesis, but the mechanism that drives this has not been established. Here, we used ALS6 patient-derived induced pluripotent stem cells (hIPSCs) to study the effect of the ALS6 FUSR521H mutation on the translation machinery in motor neurons (MNs). We find, in agreement with findings of others, that protein synthesis is decreased in FUSR521H MNs. Furthermore, FUSR521H MNs are more sensitive to oxidative stress and display reduced expression of TGF-β and mTORC gene pathways when stressed. Finally, we show that IFNγ treatment reduces apoptosis of FUSR521H MNs exposed to oxidative stress and partially restores the translation rates in FUSR521H MNs. Overall, these findings suggest that a functional IFNγ response is important for FUS-mediated protein synthesis, possibly by FUS nuclear translocation in ALS6. |
| Author | Carvalho, Valdemir M. Oliveira, Danyllo Foijer, Floris Wardenaar, René Alves, Luciana M. Assoni, Amanda Faria Okamoto, Oswaldo Keith Guerrero, Erika N. Bakker, Petra L. Zatz, Mayana |
| AuthorAffiliation | 2 Instituto de Biociências Universidade de São Paulo São Paulo Brazil 1 European Research Institute for the Biology of Ageing (ERIBA) University of Groningen, University Medical Center Groningen Groningen The Netherlands 3 Department of Stem Cell Research Gorgas Memorial Institute for Health Studies Panama City Republic of Panama 4 Division of Research and Development Fleury Group São Paulo Brazil |
| AuthorAffiliation_xml | – name: 2 Instituto de Biociências Universidade de São Paulo São Paulo Brazil – name: 4 Division of Research and Development Fleury Group São Paulo Brazil – name: 1 European Research Institute for the Biology of Ageing (ERIBA) University of Groningen, University Medical Center Groningen Groningen The Netherlands – name: 3 Department of Stem Cell Research Gorgas Memorial Institute for Health Studies Panama City Republic of Panama |
| Author_xml | – sequence: 1 givenname: Amanda Faria surname: Assoni fullname: Assoni, Amanda Faria organization: Universidade de São Paulo – sequence: 2 givenname: Erika N. surname: Guerrero fullname: Guerrero, Erika N. organization: Gorgas Memorial Institute for Health Studies – sequence: 3 givenname: René surname: Wardenaar fullname: Wardenaar, René organization: University of Groningen, University Medical Center Groningen – sequence: 4 givenname: Danyllo surname: Oliveira fullname: Oliveira, Danyllo organization: Universidade de São Paulo – sequence: 5 givenname: Petra L. surname: Bakker fullname: Bakker, Petra L. organization: University of Groningen, University Medical Center Groningen – sequence: 6 givenname: Luciana M. surname: Alves fullname: Alves, Luciana M. organization: Universidade de São Paulo – sequence: 7 givenname: Valdemir M. orcidid: 0000-0002-9816-8615 surname: Carvalho fullname: Carvalho, Valdemir M. organization: Fleury Group – sequence: 8 givenname: Oswaldo Keith surname: Okamoto fullname: Okamoto, Oswaldo Keith organization: Universidade de São Paulo – sequence: 9 givenname: Mayana surname: Zatz fullname: Zatz, Mayana organization: Universidade de São Paulo – sequence: 10 givenname: Floris orcidid: 0000-0003-0989-3127 surname: Foijer fullname: Foijer, Floris email: f.foijer@umcg.nl organization: University of Groningen, University Medical Center Groningen |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37582053$$D View this record in MEDLINE/PubMed |
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| Snippet | Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to decreased global... Abstract Amyotrophic lateral sclerosis type 6 (ALS6) is a familial subtype of ALS linked to Fused in Sarcoma (FUS) gene mutation. FUS mutations lead to... |
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| SubjectTerms | Amyotrophic lateral sclerosis Amyotrophic Lateral Sclerosis - genetics Amyotrophic Lateral Sclerosis - metabolism Apoptosis Cytokines Cytoplasm FUS gene FUS protein Genes Humans Localization Motor neurons Motor Neurons - metabolism Mutation Neurons Nuclear transport Oxidative Stress Patients Pluripotency Point mutation Protein biosynthesis Protein synthesis Proteins RNA-Binding Protein FUS - genetics Sarcoma Stem cells Translation γ-Interferon |
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| Title | IFNγ protects motor neurons from oxidative stress via enhanced global protein synthesis in FUS‐associated amyotrophic lateral sclerosis |
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