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New Advances in Mitochondria Biology

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (28 February 2025) | Viewed by 1832

Special Issue Editor


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Guest Editor
Department of Mitochondrial Physiology, No.75, Institute of Physiology of the Czech Academy of Sciences, 14220 Prague, Czech Republic
Interests: reactive oxygen species; mitochondria; oxidative stress; mitochondrial DNA; oxidative phosphorylation; free radicals; redox; glucose

Special Issue Information

Dear Colleagues,

Mitochondria have been under the scrutiny of scientists for over a century, yet new insights into their biology remain at least as fascinating as when their research began. This never-ending progress in understanding their function is largely driven by innovative methodological approaches. The advent of high-resolution microscopy and volume electron microscopy has enabled fascinating studies of mitochondrial dynamic ultrastructure, their interactions with other organelles, as well as the study of processes involved in mitochondrial quality maintenance. Likewise, research of bioenergetics and respiratory chain, often perceived as a more traditional branch in mitochondrial research, profits from methodological advances. A better knowledge of processes involved in the regulation of cellular bioenergetics and their spatial compartmentalization significantly improves our understanding of the complex role of mitochondria within both cellular and whole-organism physiology.

This Special Issue aims to collect original research articles and full review papers dealing with all aspects of mitochondrial biology. Contributions related to, but not limited to, mitochondrial morphology, cristae, mitochondrial nucleoids, interactions with other organelles, and quality maintenance are welcomed. Papers covering new aspects of mitochondrial bioenergetics will also be considered.

Dr. Andrea Dlasková
Guest Editor

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Keywords

  • mitochondria
  • cristae
  • cristae shaping proteins
  • nucleoids
  • mitochondrial membrane contact sites
  • mitochondrial quality control
  • bioenergetics

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Published Papers (1 paper)

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Research

15 pages, 2529 KB  
Article
EPA and DHA Enhance CACT Promoter Activity by GABP/NRF2
by Eleonora Stanca, Francesco Spedicato, Anna Maria Giudetti, Laura Giannotti, Benedetta Di Chiara Stanca, Fabrizio Damiano and Luisa Siculella
Int. J. Mol. Sci. 2024, 25(16), 9095; https://doi.org/10.3390/ijms25169095 - 22 Aug 2024
Viewed by 1142
Abstract
Carnitine-acylcarnitine translocase (CACT) is a nuclear-encoded mitochondrial carrier that catalyzes the transfer of long-chain fatty acids across the inner mitochondrial membrane for β-oxidation. In this study, we conducted a structural and functional characterization of the CACT promoter to investigate the molecular mechanism underlying [...] Read more.
Carnitine-acylcarnitine translocase (CACT) is a nuclear-encoded mitochondrial carrier that catalyzes the transfer of long-chain fatty acids across the inner mitochondrial membrane for β-oxidation. In this study, we conducted a structural and functional characterization of the CACT promoter to investigate the molecular mechanism underlying the transcriptional regulation of the CACT gene by n-3 PUFA, EPA and DHA. In hepatic BRL3A cells, EPA and DHA stimulate CACT mRNA and protein expression. Deletion promoter analysis using a luciferase reporter gene assay identified a n-3 PUFA response region extending from −202 to −29 bp. This region did not contain a response element for PPARα, a well-known PUFA-responsive nuclear receptor. Instead, bioinformatic analysis revealed two highly conserved GABP responsive elements within this region. Overexpression of GABPα and GABPβ subunits, but not PPARα, increased CACT promoter activity, more remarkably upon treatment with EPA and DHA. ChIP assays showed that n3-PUFA enhanced the binding of GABPα to the −202/−29 bp sequence. Furthermore, both EPA and DHA induced nuclear accumulation of GABPα. In conclusion, our findings indicate that the upregulation of CACT by n3-PUFA in hepatic cells is independent from PPARα and could be mediated by GABP activation. Full article
(This article belongs to the Special Issue New Advances in Mitochondria Biology)
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