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Mitochondria as a Cellular Hub in Neurological Disorders 2.0
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Mitochondria as a Cellular Hub in Neurological Disorders 2.0

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

Deadline for manuscript submissions: 30 April 2024 | Viewed by 6126

Special Issue Editor

Dr. Anna Atlante

E-Mail Website
Guest Editor
Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM)-CNR, Via G. Amendola122/O, 70126 Bari, Italy
Interests: mitochondrial bioenergetics; oxidative phosphorylation; mitochondrial dysfunction; metabolic regulation; oxidative stress; apoptosis; Alzheimer’s disease; cystic fibrosis
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Research on mitochondrial function, an indicator of cell health, continues to be fervid.

Mitochondria receive great attention because they emerge as hubs on which cell survival or cell death is ultimately determined. Without ATP from the cell’s powerhouse, cell survival is endangered in neurological disorders, including Alzheimer's disease, Parkinson's disease, Huntington's disease, multiple sclerosis, epilepsy, stroke, and others. All of these diseases that significantly change the lives of millions of people are characterized by structural, biochemical, or electrical abnormalities in the brain, spinal cord, or other nerves, affecting memory and the ability to perform daily activities.

Morphologic, biochemical, and molecular genetic studies posit that mitochondria constitute a convergence point for these neurological disorders.

The aim of this Special Issue of the International Journal of Molecular Sciences entitled “Mitochondria as a Cellular Hub in Neurological Disorders 2.0” is to underline the advances and the most recent discoveries in all fields of science that deal with the role of mitochondria in neurological disorders.

Original full research articles, as well as review articles from research groups all over the world, are welcome in order to disseminate scientific knowledge on this interesting topic.

Dr. Anna Atlante
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • mitochondria
  • bioenergetics
  • ROS production
  • mitochondrial DNA
  • neurodegeneration
  • neurotoxicity
  • apoptosis
  • Alzheimer’s disease
  • Parkinson’s disease
  • Huntington's disease
  • multiple sclerosis
  • epilepsy
  • stroke

Related Special Issue

Published Papers (5 papers)

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Research

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19 pages, 18348 KiB  
Article
Cultured Rat Hippocampal Neurons Exposed to the Mitochondrial Uncoupler Carbonyl Cyanide Chlorophenylhydrazone Undergo a Rapid, Presenilin-Dependent Change in Neuronal Properties
by Liliia Kushnireva, Menahem Segal and Eduard Korkotian
Int. J. Mol. Sci. 2024, 25(1), 578; https://doi.org/10.3390/ijms25010578 - 01 Jan 2024
Viewed by 949
Abstract
Presenilin 1 (PS1) is a transmembrane proteolytic subunit of γ-secretase that cleaves amyloid precursor proteins. Mutations in PS1 (mPS1) are associated with early-onset familial Alzheimer’s disease (AD). The link between mutated PS1, mitochondrial calcium regulation, and AD has been studied extensively in [...] Read more.
Presenilin 1 (PS1) is a transmembrane proteolytic subunit of γ-secretase that cleaves amyloid precursor proteins. Mutations in PS1 (mPS1) are associated with early-onset familial Alzheimer’s disease (AD). The link between mutated PS1, mitochondrial calcium regulation, and AD has been studied extensively in different test systems. Despite the wide-ranging role of mPS1 in AD, there is a paucity of information on the link between PS1 and neuronal cell death, a hallmark of AD. In the present study, we employed the selective mitochondrial uncoupler carbonyl cyanide chlorophenylhydrazone (CCCP) and compared the reactivity of mPS1-transfected cultured rat hippocampal neurons with PS1 and control neurons in a situation of impaired mitochondrial functions. CCCP causes a slow rise in cytosolic and mitochondrial calcium in all three groups of neurons, with the mPS1 neurons demonstrating a faster rise. Consequently, mPS1 neurons were depolarized by CCCP and measured with TMRM, a mitochondrial voltage indicator, more than the other two groups. Morphologically, CCCP produced more filopodia in mPS1 neurons than in the other two groups, which were similarly affected by the drug. Finally, mPS1 transfected neurons tended to die from prolonged exposure to CCCP sooner than the other groups, indicating an increase in vulnerability associated with a lower ability to regulate excess cytosolic calcium. Full article
(This article belongs to the Special Issue Mitochondria as a Cellular Hub in Neurological Disorders 2.0)
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Review

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13 pages, 726 KiB  
Review
OMA1-Mediated Mitochondrial Dynamics Balance Organellar Homeostasis Upstream of Cellular Stress Responses
by Robert Gilkerson, Harpreet Kaur, Omar Carrillo and Isaiah Ramos
Int. J. Mol. Sci. 2024, 25(8), 4566; https://doi.org/10.3390/ijms25084566 - 22 Apr 2024
Viewed by 303
Abstract
In response to cellular metabolic and signaling cues, the mitochondrial network employs distinct sets of membrane-shaping factors to dynamically modulate organellar structures through a balance of fission and fusion. While these organellar dynamics mediate mitochondrial structure/function homeostasis, they also directly impact critical cell-wide [...] Read more.
In response to cellular metabolic and signaling cues, the mitochondrial network employs distinct sets of membrane-shaping factors to dynamically modulate organellar structures through a balance of fission and fusion. While these organellar dynamics mediate mitochondrial structure/function homeostasis, they also directly impact critical cell-wide signaling pathways such as apoptosis, autophagy, and the integrated stress response (ISR). Mitochondrial fission is driven by the recruitment of the cytosolic dynamin-related protein-1 (DRP1), while fusion is carried out by mitofusins 1 and 2 (in the outer membrane) and optic atrophy-1 (OPA1) in the inner membrane. This dynamic balance is highly sensitive to cellular stress; when the transmembrane potential across the inner membrane (Δψm) is lost, fusion-active OPA1 is cleaved by the overlapping activity with m-AAA protease-1 (OMA1 metalloprotease, disrupting mitochondrial fusion and leaving dynamin-related protein-1 (DRP1)-mediated fission unopposed, thus causing the collapse of the mitochondrial network to a fragmented state. OMA1 is a unique regulator of stress-sensitive homeostatic mitochondrial balance, acting as a key upstream sensor capable of priming the cell for apoptosis, autophagy, or ISR signaling cascades. Recent evidence indicates that higher-order macromolecular associations within the mitochondrial inner membrane allow these specialized domains to mediate crucial organellar functionalities. Full article
(This article belongs to the Special Issue Mitochondria as a Cellular Hub in Neurological Disorders 2.0)
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33 pages, 6131 KiB  
Review
Variants in Human ATP Synthase Mitochondrial Genes: Biochemical Dysfunctions, Associated Diseases, and Therapies
by Valentina Del Dotto, Francesco Musiani, Alessandra Baracca and Giancarlo Solaini
Int. J. Mol. Sci. 2024, 25(4), 2239; https://doi.org/10.3390/ijms25042239 - 13 Feb 2024
Cited by 1 | Viewed by 1117
Abstract
Mitochondrial ATP synthase (Complex V) catalyzes the last step of oxidative phosphorylation and provides most of the energy (ATP) required by human cells. The mitochondrial genes MT-ATP6 and MT-ATP8 encode two subunits of the multi-subunit Complex V. Since the discovery of the first [...] Read more.
Mitochondrial ATP synthase (Complex V) catalyzes the last step of oxidative phosphorylation and provides most of the energy (ATP) required by human cells. The mitochondrial genes MT-ATP6 and MT-ATP8 encode two subunits of the multi-subunit Complex V. Since the discovery of the first MT-ATP6 variant in the year 1990 as the cause of Neuropathy, Ataxia, and Retinitis Pigmentosa (NARP) syndrome, a large and continuously increasing number of inborn variants in the MT-ATP6 and MT-ATP8 genes have been identified as pathogenic. Variants in these genes correlate with various clinical phenotypes, which include several neurodegenerative and multisystemic disorders. In the present review, we report the pathogenic variants in mitochondrial ATP synthase genes and highlight the molecular mechanisms underlying ATP synthase deficiency that promote biochemical dysfunctions. We discuss the possible structural changes induced by the most common variants found in patients by considering the recent cryo-electron microscopy structure of human ATP synthase. Finally, we provide the state-of-the-art of all therapeutic proposals reported in the literature, including drug interventions targeting mitochondrial dysfunctions, allotopic gene expression- and nuclease-based strategies, and discuss their potential translation into clinical trials. Full article
(This article belongs to the Special Issue Mitochondria as a Cellular Hub in Neurological Disorders 2.0)
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29 pages, 4150 KiB  
Review
Mitochondrial Complex I and β-Amyloid Peptide Interplay in Alzheimer’s Disease: A Critical Review of New and Old Little Regarded Findings
by Anna Atlante and Daniela Valenti
Int. J. Mol. Sci. 2023, 24(21), 15951; https://doi.org/10.3390/ijms242115951 - 03 Nov 2023
Viewed by 1634
Abstract
Alzheimer’s disease (AD) is the most common neurodegenerative disorder and the main cause of dementia which is characterized by a progressive cognitive decline that severely interferes with daily activities of personal life. At a pathological level, it is characterized by the accumulation of [...] Read more.
Alzheimer’s disease (AD) is the most common neurodegenerative disorder and the main cause of dementia which is characterized by a progressive cognitive decline that severely interferes with daily activities of personal life. At a pathological level, it is characterized by the accumulation of abnormal protein structures in the brain—β-amyloid (Aβ) plaques and Tau tangles—which interfere with communication between neurons and lead to their dysfunction and death. In recent years, research on AD has highlighted the critical involvement of mitochondria—the primary energy suppliers for our cells—in the onset and progression of the disease, since mitochondrial bioenergetic deficits precede the beginning of the disease and mitochondria are very sensitive to Aβ toxicity. On the other hand, if it is true that the accumulation of Aβ in the mitochondria leads to mitochondrial malfunctions, it is otherwise proven that mitochondrial dysfunction, through the generation of reactive oxygen species, causes an increase in Aβ production, by initiating a vicious cycle: there is therefore a bidirectional relationship between Aβ aggregation and mitochondrial dysfunction. Here, we focus on the latest news—but also on neglected evidence from the past—concerning the interplay between dysfunctional mitochondrial complex I, oxidative stress, and Aβ, in order to understand how their interplay is implicated in the pathogenesis of the disease. Full article
(This article belongs to the Special Issue Mitochondria as a Cellular Hub in Neurological Disorders 2.0)
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Other

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13 pages, 1586 KiB  
Opinion
How the ‘Aerobic/Anaerobic Glycolysis’ Meme Formed a ‘Habit of Mind’ Which Impedes Progress in the Field of Brain Energy Metabolism
by Avital Schurr
Int. J. Mol. Sci. 2024, 25(3), 1433; https://doi.org/10.3390/ijms25031433 - 24 Jan 2024
Viewed by 1628
Abstract
The division of glycolysis into two separate pathways, aerobic and anaerobic, depending on the presence or absence of oxygen, respectively, was formulated over eight decades ago. The former ends with pyruvate, while the latter ends with lactate. Today, this division is confusing and [...] Read more.
The division of glycolysis into two separate pathways, aerobic and anaerobic, depending on the presence or absence of oxygen, respectively, was formulated over eight decades ago. The former ends with pyruvate, while the latter ends with lactate. Today, this division is confusing and misleading as research over the past 35 years clearly has demonstrated that glycolysis ends with lactate not only in cancerous cells but also in healthy tissues and cells. The present essay offers a review of the history of said division and the more recent knowledge that has been gained about glycolysis and its end-product, lactate. Then, it presents arguments in an attempt to explain why separating glycolysis into aerobic and anaerobic pathways persists among scientists, clinicians and teachers alike, despite convincing evidence that such division is not only wrong scientifically but also hinders progress in the field of energy metabolism. Full article
(This article belongs to the Special Issue Mitochondria as a Cellular Hub in Neurological Disorders 2.0)
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