Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
9.0
4.9
Journals
IJMS
Special Issues
Molecular Mechanisms and Novel Therapeutic Approaches for Alzheimer’s Disease
ijms-logo
Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Molecular Mechanisms and Novel Therapeutic Approaches for Alzheimer’s Disease

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: closed (10 September 2024) | Viewed by 6734

Special Issue Editor

Dr. Wioletta Rozpędek-Kamińska

E-Mail Website
Guest Editor
Department of Clinical Chemistry and Biochemistry, Medical University of Lodz, 92-215 Lodz, Poland
Interests: polymers; restorative dentistry; bioactive dental materials; cell culture; apoptosis; cell signaling; western blot analysis; PCR; molecular cell biology; cancer biology; gene expression; electrophoresis; tissue culture

Special Issue Information

Dear Colleagues,

We are pleased to invite you to contribute to our Special Issue of the International Journal of Molecular Sciences (IJMS), entitled “Molecular Mechanisms and Novel Therapeutic Approaches for Alzheimer’s Disease”. This Special Issue will cover a selection of recent research topics and current review articles, reporting the latest updates on Alzheimer’s disease treatment. Alzheimer’s disease (AD) occurs as a result of neurodegenerative processes and it is characterized by the aggregation of misfolded and unfolded proteins among the neurons of the brain tissue, which is closely connected with a significant loss of neurons. Interestingly, it has been reported that AD pathogenesis and progression are strictly associated with common perturbation on the molecular level through the incorrect activation of selected molecular pathways. We welcome papers that address the molecular and cellular mechanisms underlying the pathogenesis of AD, molecular targets in AD, as well as novel therapeutic approaches for AD. This Special Issue is now open for submissions. If you are interested in contributing your work, please send a short abstract or tentative title to the Guest Editor or Editorial Office.

Dr. Wioletta Rozpędek-Kamińska
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

  • Alzheimer’s disease
  • dementia
  • amyloid-beta
  • amyloid aggregation
  • protein misfolding
  • Alzheimer’s disease signaling pathways
  • drug discovery
  • neuroprotection
  • Alzheimer’s disease treatment
  • neuroprotective strategies

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (3 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

16 pages, 6777 KiB  
Article
IGF-1 and Glucocorticoid Receptors Are Potential Target Proteins for the NGF-Mimic Effect of β-Cyclocitral from Lavandula angustifolia Mill. in PC12 Cells
by Chenyue An, Lijuan Gao, Lan Xiang and Jianhua Qi
Int. J. Mol. Sci. 2024, 25(18), 9763; https://doi.org/10.3390/ijms25189763 - 10 Sep 2024
Cited by 2 | Viewed by 1250
Abstract
In the present study, the PC12 cells as a bioassay system were used to screen the small molecules with nerve growth factor (NGF)- mimic effect from Lavandula angustifolia Mill. The β-Cyclocitral (β-cyc) as an active compound was discovered, and its [...] Read more.
In the present study, the PC12 cells as a bioassay system were used to screen the small molecules with nerve growth factor (NGF)- mimic effect from Lavandula angustifolia Mill. The β-Cyclocitral (β-cyc) as an active compound was discovered, and its chemical structure was also determined. Furthermore, we focused on the bioactive and action mechanism of this compound to do an intensive study with specific protein inhibitors and Western blotting analysis. The β-cyc had novel NGF-mimic and NGF-enhancer effects on PC12 cells, while the insulin-like growth factor-1 receptor (IGF-1R)/phosphatidylinositol 3 kinase, (PI3K)/serine/threonine-protein kinase (AKT), and glucocorticoid receptor (GR)/phospholipase C (PLC)/protein kinase C (PKC) signaling pathways were involved in the bioactivity of β-cyc. In addition, the important role of the rat sarcoma (Ras)/protooncogene serine-threonine protein kinase (Raf) signaling pathway was observed, although it was independent of tyrosine kinase (Trk) receptors. Moreover, the non-label target protein discovery techniques, such as the cellular thermal shift assay (CETSA) and drug affinity responsive target stability (DARTS), were utilized to make predictions of its target protein. The stability of IGF-R and GR, proteins for temperature and protease, was dose-dependently increased after treatment of β-cyc compared with control groups, respectively. These findings indicated that β-cyc promoted the neuron differentiation of PC12 cells via targeting IGF-1R and GR and modification of downstream signaling pathways. Full article
(This article belongs to the Special Issue Molecular Mechanisms and Novel Therapeutic Approaches for Alzheimer’s Disease)
►▼ Show Figures

Figure 1

11 pages, 3015 KiB  
Article
Involvement of Endolysosomes and Aurora Kinase A in the Regulation of Amyloid β Protein Levels in Neurons
by Zahra Afghah, Nabab Khan, Gaurav Datta, Peter W. Halcrow, Jonathan D. Geiger and Xuesong Chen
Int. J. Mol. Sci. 2024, 25(11), 6200; https://doi.org/10.3390/ijms25116200 - 4 Jun 2024
Viewed by 1369
Abstract
Aurora kinase A (AURKA) is a serine/threonine-protein kinase that regulates microtubule organization during neuron migration and neurite formation. Decreased activity of AURKA was found in Alzheimer’s disease (AD) brain samples, but little is known about the role of AURKA in AD pathogenesis. Here, [...] Read more.
Aurora kinase A (AURKA) is a serine/threonine-protein kinase that regulates microtubule organization during neuron migration and neurite formation. Decreased activity of AURKA was found in Alzheimer’s disease (AD) brain samples, but little is known about the role of AURKA in AD pathogenesis. Here, we demonstrate that AURKA is expressed in primary cultured rat neurons, neurons from adult mouse brains, and neurons in postmortem human AD brains. AURKA phosphorylation, which positively correlates with its activity, is reduced in human AD brains. In SH-SY5Y cells, pharmacological activation of AURKA increased AURKA phosphorylation, acidified endolysosomes, decreased the activity of amyloid beta protein (Aβ) generating enzyme β-site amyloid precursor protein cleaving enzyme (BACE-1), increased the activity of the Aβ degrading enzyme cathepsin D, and decreased the intracellular and secreted levels of Aβ. Conversely, pharmacological inhibition of AURKA decreased AURKA phosphorylation, de-acidified endolysosomes, decreased the activity of cathepsin D, and increased intracellular and secreted levels of Aβ. Thus, reduced AURKA activity in AD may contribute to the development of intraneuronal accumulations of Aβ and extracellular amyloid plaque formation. Full article
(This article belongs to the Special Issue Molecular Mechanisms and Novel Therapeutic Approaches for Alzheimer’s Disease)
►▼ Show Figures

Figure 1

Review

Jump to: Research

23 pages, 1078 KiB  
Review
Potential Mechanisms of Tunneling Nanotube Formation and Their Role in Pathology Spread in Alzheimer’s Disease and Other Proteinopathies
by Szymon Kotarba, Marta Kozłowska, Małgorzata Scios, Kamil Saramowicz, Julia Barczuk, Zuzanna Granek, Natalia Siwecka, Wojciech Wiese, Michał Golberg, Grzegorz Galita, Grzegorz Sychowski, Ireneusz Majsterek and Wioletta Rozpędek-Kamińska
Int. J. Mol. Sci. 2024, 25(19), 10797; https://doi.org/10.3390/ijms251910797 - 8 Oct 2024
Cited by 2 | Viewed by 3196
Abstract
Alzheimer’s disease (AD) is the most common type of dementia worldwide. The etiopathogenesis of this disease remains unknown. Currently, several hypotheses attempt to explain its cause, with the most well-studied being the cholinergic, beta-amyloid (Aβ), and Tau hypotheses. Lately, there has been increasing [...] Read more.
Alzheimer’s disease (AD) is the most common type of dementia worldwide. The etiopathogenesis of this disease remains unknown. Currently, several hypotheses attempt to explain its cause, with the most well-studied being the cholinergic, beta-amyloid (Aβ), and Tau hypotheses. Lately, there has been increasing interest in the role of immunological factors and other proteins such as alpha-synuclein (α-syn) and transactive response DNA-binding protein of 43 kDa (TDP-43). Recent studies emphasize the role of tunneling nanotubes (TNTs) in the spread of pathological proteins within the brains of AD patients. TNTs are small membrane protrusions composed of F-actin that connect non-adjacent cells. Conditions such as pathogen infections, oxidative stress, inflammation, and misfolded protein accumulation lead to the formation of TNTs. These structures have been shown to transport pathological proteins such as Aβ, Tau, α-syn, and TDP-43 between central nervous system (CNS) cells, as confirmed by in vitro studies. Besides their role in spreading pathology, TNTs may also have protective functions. Neurons burdened with α-syn can transfer protein aggregates to glial cells and receive healthy mitochondria, thereby reducing cellular stress associated with α-syn accumulation. Current AD treatments focus on alleviating symptoms, and clinical trials with Aβ-lowering drugs have proven ineffective. Therefore, intensifying research on TNTs could bring scientists closer to a better understanding of AD and the development of effective therapies. Full article
(This article belongs to the Special Issue Molecular Mechanisms and Novel Therapeutic Approaches for Alzheimer’s Disease)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-3
Back to TopTop