Editorial: Mitochondrial therapy in neurodegeneration.
Ontology highlight
ABSTRACT:
SUBMITTER: Kalani A
PROVIDER: S-EPMC9969188 | biostudies-literature | 2023
REPOSITORIES: biostudies-literature
Publications
Editorial: Mitochondrial therapy in neurodegeneration.
Kalani Anuradha A Chaturvedi Pankaj P Brunetti Dario D Kalani Komal K
Frontiers in pharmacology 20230201
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Project description:This paper analyses the Editorial Board (EB) distribution of Occupational Therapy journals from a gender perspective. The "Occupational Therapy" field in the Scimago Journal and Country Rank (SJR) and the "Occupational Therapy" term in the title search of the Journal Citation Report (JCR) were used to find the Occupational Therapy-specific journals. The following indicators were calculated: Editorial Board Member (EBM) gender distribution by journal, publisher, subject speciality, country, and journal quartile. Thirty-seven journals were located, including 667 individuals, 206 males (31%) and 461 females (69%). Referring to the EB positions, most members (557) were EB members, 70 were listed as Associate Editors, and 20 as Editorial Leaders. The results show that the proportion of women in the EB's of Occupational Therapy journals represents a majority. Regarding the distribution by gender of the EBMs, six journals had a female proportion below the cut-off point revealed in this study (69%). Four did not reach parity, with female representation below 50%. Additionally, the balance among the EBMs is significantly underrepresented compared to the percentage of female Occupational Therapy practitioners.
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Project description:Aberrant localization of proteins to mitochondria disturbs mitochondrial function and contributes to the pathogenesis of Huntington's disease (HD). However, the crucial factors and the molecular mechanisms remain elusive. Here, we found that heat shock transcription factor 1 (HSF1) accumulates in the mitochondria of HD cell models, a YAC128 mouse model, and human striatal organoids derived from HD induced pluripotent stem cells (iPSCs). Overexpression of mitochondria-targeting HSF1 (mtHSF1) in the striatum causes neurodegeneration and HD-like behavior in mice. Mechanistically, mtHSF1 facilitates mitochondrial fission by activating dynamin-related protein 1 (Drp1) phosphorylation at S616. Moreover, mtHSF1 suppresses single-stranded DNA-binding protein 1 (SSBP1) oligomer formation, which results in mitochondrial DNA (mtDNA) deletion. The suppression of HSF1 mitochondrial localization by DH1, a unique peptide inhibitor, abolishes HSF1-induced mitochondrial abnormalities and ameliorates deficits in an HD animal model and human striatal organoids. Altogether, our findings describe an unsuspected role of HSF1 in contributing to mitochondrial dysfunction, which may provide a promising therapeutic target for HD.
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Project description:Aberrant localization of proteins to mitochondria disturbs mitochondrial function and contributes to the pathogenesis of Huntington's disease (HD). However, the crucial factors and the molecular mechanisms remain elusive. Here, we found that heat shock transcription factor 1 (HSF1) accumulates in the mitochondria of HD cell models, a YAC128 mouse model, and human striatal organoids derived from HD induced pluripotent stem cells (iPSCs). Overexpression of mitochondria-targeting HSF1 (mtHSF1) in the striatum causes neurodegeneration and HD-like behavior in mice. Mechanistically, mtHSF1 facilitates mitochondrial fission by activating dynamin-related protein 1 (Drp1) phosphorylation at S616. Moreover, mtHSF1 suppresses single-stranded DNA binding protein 1 (SSBP1) oligomer formation, which results in mitochondrial DNA (mtDNA) deletion. Suppression of HSF1 mitochondrial localization by DH1, a unique peptide inhibitor, abolishes HSF1-induced mitochondrial abnormalities and ameliorates deficits in an HD animal model and human striatal organoids. Altogether, our findings describe an unsuspected role of HSF1 in contributing to mitochondrial dysfunction, which may provide a promising therapeutic target for HD.
| S-SCDT-10_15252-EMMM_202215851 | biostudies-other