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Special Issue "Molecular Research on Neurodegenerative Diseases 2.0"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: 10 April 2020.

Special Issue Editors

Prof. Dr. Cesar Borlongan
E-Mail Website
Guest Editor
Department of Neurosurgery, MDC 78, University of South Florida College Medicine, Tampa, FL 33612, USA
Interests: stem cell therapy; stroke, neonatal hypoxic-ischemic injury; Parkinson's disease; traumatic brain injury; translational research
Special Issues and Collections in MDPI journals
Dr. Eleonora Napoli
E-Mail Website
Guest Editor
Department of Molecular Sciences, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, USA

Special Issue Information

Dear Colleagues,

This Special Issue is a continuation of our previous Special Issue "Molecular Research on Neurodegenerative Diseases" (https://www.mdpi.com/journal/ijms/special_issues/neurodegenerative_dis).

Many neurological disorders have been characterized by neurodegenerative processes, with key molecular signaling pathways participating in the cascade of cell death events. Even brain diseases, traditionally considered as acute central nervous system injury, such as stroke and traumatic brain injury, have now been recognized as presenting with major pathological components, known as hallmarks of chronic neurodegeneration. Among the many molecular signatures of neurodegeneration, specific molecules associated with inflammation and mitochondrial dysfunction have been implicated as pivotal checkpoints in the propagation of cell death mechanisms, yet also indicated as equally involved as robust targets for anchoring cell survival therapeutics. This Special Issue is dedicated to the recent research progress in deciphering molecular pathways mediating cell death and cell survival in neurodegeneration and its treatment. The goal is to provide an in-depth understanding of the underlying central role of neurodegeneration in brain diseases, and to exploit such knowledge in the development of novel molecule-based therapies against neurodegenerative disorders.

Prof. Dr. Cesar Borlongan
Dr. Eleonora Napoli
Guest Editors

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 papers will be 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

  • neurological disorders
  • stroke
  • traumatic brain injury
  • neurodegeneration
  • Parkinson's disease
  • molecular pathways

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Published Papers (3 papers)

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Research

Open AccessArticle
Sequential Transcriptome Changes in the Penumbra after Ischemic Stroke
Int. J. Mol. Sci. 2019, 20(24), 6349; https://doi.org/10.3390/ijms20246349 - 16 Dec 2019
Abstract
To investigate the changes in the expression of specific genes that occur during the acute-to-chronic post-stroke phase, we identified differentially expressed genes (DEGs) between naive cortical tissues and peri-infarct tissues at 1, 4, and 8 weeks after photothrombotic stroke. The profiles of DEGs [...] Read more.
To investigate the changes in the expression of specific genes that occur during the acute-to-chronic post-stroke phase, we identified differentially expressed genes (DEGs) between naive cortical tissues and peri-infarct tissues at 1, 4, and 8 weeks after photothrombotic stroke. The profiles of DEGs were subjected to the Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway and gene ontology analyses, followed by string analysis of the protein–protein interactions (PPI) of the products of these genes. We found 3771, 536, and 533 DEGs at 1, 4, and 8 weeks after stroke, respectively. A marked decrease in biological–process categories, such as brain development and memory, and a decrease in neurotransmitter synaptic and signaling pathways were observed 1 week after stroke. The PPI analysis showed the downregulation of Dlg4, Bdnf, Gria1, Rhoa, Mapk8, and glutamatergic receptors. An increase in biological–process categories, including cell population proliferation, cell adhesion, and inflammatory responses, was detected at 4 and 8 weeks post-stroke. The KEGG pathways of complement and coagulation cascades, phagosomes, antigen processing, and antigen presentation were also altered. CD44, C1, Fcgr2b, Spp1, and Cd74 occupied a prominent position in network analyses. These time-dependent changes in gene profiles reveal the unique pathophysiological characteristics of stroke and suggest new therapeutic targets for this disease. Full article
(This article belongs to the Special Issue Molecular Research on Neurodegenerative Diseases 2.0)
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Open AccessArticle
Zinc Binding to Tau Influences Aggregation Kinetics and Oligomer Distribution
Int. J. Mol. Sci. 2019, 20(23), 5979; https://doi.org/10.3390/ijms20235979 - 27 Nov 2019
Cited by 1
Abstract
Metal ions are well known modulators of protein aggregation and are key players in Alzheimer’s Disease, being found to be associated to pathologic protein deposits in diseased brains. Therefore, understanding how metals influence amyloid aggregation is critical in establishing molecular mechanisms that underlie [...] Read more.
Metal ions are well known modulators of protein aggregation and are key players in Alzheimer’s Disease, being found to be associated to pathologic protein deposits in diseased brains. Therefore, understanding how metals influence amyloid aggregation is critical in establishing molecular mechanisms that underlie disease onset and progression. Here, we report data on the interaction of full-length human Tau protein with calcium and zinc ions, evidencing that Tau self-assembly is differently regulated, depending on the type of bound metal ion. We established that Tau binds 4 Zn2+ and 1 Ca2+ per monomer while using native mass spectrometry analysis, without inducing order or substantial conformational changes in the intrinsically disordered Tau, as determined by structural analysis using circular dichroism and Attenuated Total Reflectance-Fourier Transform Infrared (ATR-FTIR) spectroscopies. However, Tau aggregation is found to proceed differently in the calcium- and -zinc bound forms. While the rate of aggregation, as determined from thioflavin-T (ThT) fluorescence kinetics, is highly increased in both cases, the reaction proceeds via different mechanisms, as evidenced by the absence of the lag phase in the reaction of zinc-bound Tau. Monitoring Tau aggregation using native mass spectrometry indeed evidenced a distinct distribution of Tau conformers along the reaction, as confirmed by dynamic light scattering analysis. We propose that such differences arise from zinc binding at distinct locations within the Tau sequence that prompt both the rapid formation of seeding oligomers through interactions at high affinity sites within the repeat domains, as well as amorphous aggregation, through low affinity interactions with residues elsewhere in the sequence, including at the fuzzy coat domain. Full article
(This article belongs to the Special Issue Molecular Research on Neurodegenerative Diseases 2.0)
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Open AccessArticle
Reduced Cholinergic Activity in the Hippocampus of Hippocampal Cholinergic Neurostimulating Peptide Precursor Protein Knockout Mice
Int. J. Mol. Sci. 2019, 20(21), 5367; https://doi.org/10.3390/ijms20215367 - 28 Oct 2019
Abstract
The cholinergic efferent network from the medial septal nucleus to the hippocampus has an important role in learning and memory processes. This cholinergic projection can generate theta oscillations in the hippocampus to efficiently encode novel information. Hippocampal cholinergic neurostimulating peptide (HCNP) induces acetylcholine [...] Read more.
The cholinergic efferent network from the medial septal nucleus to the hippocampus has an important role in learning and memory processes. This cholinergic projection can generate theta oscillations in the hippocampus to efficiently encode novel information. Hippocampal cholinergic neurostimulating peptide (HCNP) induces acetylcholine synthesis in medial septal nuclei. HCNP is processed from the N-terminal region of a 186 amino acid, 21 kD HCNP precursor protein called HCNP-pp (also known as Raf kinase inhibitory protein (RKIP) and phosphatidylethanolamine-binding protein 1 (PEBP1)). In this study, we generated HCNP-pp knockout (KO) mice and assessed their cholinergic septo-hippocampal projection, local field potentials in CA1, and behavioral phenotypes. No significant behavioral phenotype was observed in HCNP-pp KO mice. However, theta power in the CA1 of HCNP-pp KO mice was significantly reduced because of fewer cholineacetyltransferase-positive axons in the CA1 stratum oriens. These observations indicated disruption of cholinergic activity in the septo-hippocampal network. Our study demonstrates that HCNP may be a cholinergic regulator in the septo-hippocampal network. Full article
(This article belongs to the Special Issue Molecular Research on Neurodegenerative Diseases 2.0)
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