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A special issue of Current Issues in Molecular Biology (ISSN 1467-3045). This special issue belongs to the section "Molecular Medicine".

Deadline for manuscript submissions: 31 March 2025 | Viewed by 8976

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Dr. Dumitru A. Iacobas

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Personalized Genomics Laboratory, Undergraduate Medical Academy, Prairie View A&M University, Prairie View, TX 77446, USA
Interests: cancer therapy; cancer biomarker; neurogenomics; systems biology; intercellular communication; neurotransmission
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Dear Colleagues，

This Special Issue, “Molecules at Play in Neurological Diseases 2024”, presents a meticulous examination of the molecular mechanisms underpinning diverse neurological disorders. This compilation of articles showcases pioneering research elucidating the roles of specific molecules in the etiology and progression of these conditions.

Contributions to this Special Issue span a spectrum of topics, encompassing the influence of neurotransmitters, neuropeptides, and neurotrophic factors on cerebral function and dysfunction. Researchers delve into the intricate interplay of genetic and epigenetic elements in neurological disorders, illuminating potential therapeutic targets.

Furthermore, this Special Issue underscores the latest advancements in neuroimaging modalities and their utility in diagnosing and monitoring neurological diseases. Insights into the evolution of innovative therapeutic approaches, such as gene therapy and pharmacological interventions, are also detailed.

In summary, "Molecules at Play in Neurological Diseases 2024" offers a comprehensive portrayal of the molecular landscape of neurological disorders. This body of work provides invaluable insights that may pave the way for the development of more efficacious treatments in the future.

Dr. Dumitru Iacobas
Guest Editor

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Keywords

neurological diseases
neurotransmitters
neuropeptides
neurotrophic factors
genetic and epigenetic elements

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23 pages, 3822 KiB

Open AccessArticle

BDNF/Cyclin D1 Signaling System and Cognitive Performance After Perampanel and Lacosamide Treatment Singly or in Combination in an Experimental Model of Temporal Lobe Epilepsy

by Michaela Shishmanova-Doseva and Darina Barbutska

Curr. Issues Mol. Biol. 2024, 46(12), 14010-14032; https://doi.org/10.3390/cimb46120838 - 11 Dec 2024

Viewed by 892

Abstract

Epilepsy is a common brain function disorder. The present study aims to evaluate the long-term effect of perampanel (PRM) and lacosamide (LCM), administered singly in a high-dose or in a low-dose combination of both, on comorbid anxiety, cognitive impairment, BDNF, and Cyclin D1 hippocampal expression in an experimental model of temporal lobe epilepsy with lithium–pilocarpine. PRM (3 mg/kg, p.o.)/LCM (30 mg/kg, p.o.) or PRM+LCM (0.5 mg/kg + 3 mg/kg, p.o.) treatments were administered three hours after the lithium–pilocarpine-induced status epilepticus and continued for up to ten weeks in adult Wistar rats. Our study demonstrated that perampanel and lacosamide administered singly in high doses improved epilepsy-associated cognitive impairment through ameliorating anxiety and facilitating passive learning and memory, with spatial and recognition memory measured in the elevated plus maze, step-through, Y-maze, and object recognition tests, respectively. In addition, the combination of both drugs in low doses demonstrated similar anxiolytic and cognitive-improving effects compared to the singly administered drugs. Moreover, the three experimental groups enhanced the hippocampal expression of the neurotrophic factor BDNF and mitigated the increased levels of the apoptotic factor Cyclin D1. These beneficial effects could be essential mechanisms through which administered anticonvulsants preserve neuronal survival and homeostasis in the CNS and especially in the hippocampus. Full article

(This article belongs to the Special Issue Molecules at Play in Neurological Diseases)

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17 pages, 3291 KiB

Open AccessArticle

Assessment of the Concentration of Transforming Growth Factor Beta 1–3 in Degenerated Intervertebral Discs of the Lumbosacral Region of the Spine

by Rafał Staszkiewicz, Dorian Gładysz, Dawid Sobański, Filip Bolechała, Edward Golec, Małgorzata Sobańska, Damian Strojny, Artur Turek and Beniamin Oskar Grabarek

Curr. Issues Mol. Biol. 2024, 46(11), 12813-12829; https://doi.org/10.3390/cimb46110763 - 11 Nov 2024

Viewed by 649

Abstract

The purpose of this study was to evaluate the feasibility of using the expression profile of transforming growth factor beta (TGF-β-1-3) to assess the progression of L/S spine degenerative disease. The study group consisted of 113 lumbosacral (L/S) intervertebral disc (IVD) degenerative disease patients from whom IVDs were collected during a microdiscectomy, whereas the control group consisted of 81 participants from whom IVDs were collected during a forensic autopsy or organ harvesting. Hematoxylin and eosin staining was performed to exclude degenerative changes in the IVDs collected from the control group. The molecular analysis consisted of reverse-transcription real-time quantitative polymerase chain reaction (RT-qPCR), an enzyme-linked immunosorbent assay (ELISA), Western blotting, and an immunohistochemical analysis (IHC). In degenerated IVDs, we noted an overexpression of all TGF-β-1-3 mRNA isoforms with the largest changes observed for TGF-β3 isoforms (fold change (FC) = 19.52 ± 2.87) and the smallest for TGF-β2 (FC = 2.26 ± 0.16). Changes in the transcriptional activity of TGF-β-1-3 were statistically significant (p < 0.05). Significantly higher concentrations of TGF-β1 (2797 ± 132 pg/mL vs. 276 ± 19 pg/mL; p < 0.05), TGF-β2 (1918 ± 176 pg/mL vs. 159 ± 17 pg/mL; p < 0.05), and TGF-β3 (2573 ± 102 pg/mL vs. 152 ± 11 pg/mL) were observed in degenerative IVDs compared with the control samples. Determining the concentration profiles of TGF-β1-3 appears to be a promising monitoring tool for the progression of degenerative disease as well as for evaluating its treatment or developing new treatment strategies with molecular targets. Full article

(This article belongs to the Special Issue Molecules at Play in Neurological Diseases)

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17 pages, 2660 KiB

Open AccessArticle

The ER Stress Induced in Human Neuroblastoma Cells Can Be Reverted by Lumacaftor, a CFTR Corrector

by Michela Pecoraro, Adele Serra, Maria Pascale and Silvia Franceschelli

Curr. Issues Mol. Biol. 2024, 46(9), 9342-9358; https://doi.org/10.3390/cimb46090553 - 24 Aug 2024

Viewed by 1204

Abstract

Most neurodegenerative diseases share a common etiopathogenesis, the accumulation of protein aggregates. An imbalance in homeostasis brought on by the buildup of misfolded proteins within the endoplasmic reticulum (ER) results in ER stress in the cell. Three distinct proteins found in the ER membrane—IRE1α, PERK, and ATF6—control the unfolded protein response (UPR), a signal transduction pathway that is triggered to restore normal physiological conditions. Buildup of misfolded proteins in ER lumen leads to a shunting of GRP78/BiP, thus triggering the UPR. PERK autophosphorylation leads to activation of ATF4, the transcription factor; finally, ATF6 activates the UPR’s target genes, including GRP78/Bip. Accordingly, the UPR is a cellular reaction to an ER stress state that, if left unchecked for an extended period, results in apoptosis and irreversible damage. The identification of caspase 4, which is in the ER and is selectively activated by apoptotic stimuli caused by reticular stress, further demonstrated the connection between reticular stress and programed cell death. Moreover, oxidative stress and ER stress are linked. Oxidative stress is brought on by elevated quantities of radical oxygen species, both mitochondrial and cytosolic, that are not under the enzymatic regulation of superoxide dismutases, whose levels fall with increasing stress. Here, we evaluated the activity of Vx-809 (Lumacaftor), a drug used in cystic fibrosis, in SH-SY5Y neuronal cells, in which an ER stress condition was induced by Thapsigargin, to verify whether the drug could improve protein folding, suggesting its possible therapeutic use in proteinopathies, such as neurodegenerative diseases (NDs). Our data show that Vx-809 is involved in the significant reduction in protein produced under ER stress, particularly in the levels of Bip, ATF4, and ATF6 by Western blotting analysis, the reduction in ROS in the cytosol and mitochondria, and the reduction in the activation of the apoptotic pathway, measured by flow cytofluorimetry analysis and in restoring calcium homeostasis. Full article

(This article belongs to the Special Issue Molecules at Play in Neurological Diseases)

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Figure 1
Schematic representation on the probable effect of Lumacaftor. Full article ">Figure 2
Vx-809 affects UPR activation. Cells were pretreated with 300 nM TG for 30 min or 2 or 4 h, to induce ER stress condition. Next, Vx-809 (2 µM) was added for 24 h. BiP (Panel (A)), ATF4 (Panel (C)), ATF6 (Panel (D)) and PERK/pPERK (Panel (E)) expressions in neuroblastoma cells were revealed by Western blotting analysis. Expression of actin or tubulin was employed as a loading control. Panel (B) illustrates the gel migration of the 452 bps unsplit fragment of XBP1 mRNA (XBP1 u) and the 426 bp split fragment (XBP1 s), achieved by RT-PCR. These results are presented as the average ± standard error of at least three separate, triplicate-performed studies. Data were processed according to the Mann–Whitney U-test. * p < 0.05, ** p < 0.005, and *** p < 0.001 vs. untreated cells; ° p < 0.05 and °° p < 0.005 vs. Vx-809-treated cells; # p < 0.05 vs. TG-treated cells. Full article ">Figure 2 Cont.
Vx-809 affects UPR activation. Cells were pretreated with 300 nM TG for 30 min or 2 or 4 h, to induce ER stress condition. Next, Vx-809 (2 µM) was added for 24 h. BiP (Panel (A)), ATF4 (Panel (C)), ATF6 (Panel (D)) and PERK/pPERK (Panel (E)) expressions in neuroblastoma cells were revealed by Western blotting analysis. Expression of actin or tubulin was employed as a loading control. Panel (B) illustrates the gel migration of the 452 bps unsplit fragment of XBP1 mRNA (XBP1 u) and the 426 bp split fragment (XBP1 s), achieved by RT-PCR. These results are presented as the average ± standard error of at least three separate, triplicate-performed studies. Data were processed according to the Mann–Whitney U-test. * p < 0.05, ** p < 0.005, and *** p < 0.001 vs. untreated cells; ° p < 0.05 and °° p < 0.005 vs. Vx-809-treated cells; # p < 0.05 vs. TG-treated cells. Full article ">Figure 3
Vx-809 hampers calcium signaling. Cells were pretreated with 300 nM TG for 30 min or 1 or 4 h, to induce ER stress. Following this, Vx-809 (2 µM) was added for 24 h. After ER stress, the Vx-809 effect was determined on the reticular calcium pool in cells in calcium-free media in the presence of 1 nM TG (panel (A)), and intracellular calcium concentration was quantified using 1 μM of ionomycin (panel (B)). The results show the mean ± S.E.M. of the delta (δ) increase in the fluorescence of the FURA 2 ratio (340/380 nm) from a minimum of three separate experiments, each carried out in duplicate. The findings are presented as the average ± standard error of duplicate data from a minimum of three separate and identical tests. The Mann–Whitney U test analysis was performed on the data. ** p < 0.005 and *** p < 0.001 vs. untreated cells; ° p < 0.05 vs. Vx-809-treated cells; # p < 0.05 and ### p < 0.001 vs. TG-treated cells. Full article ">Figure 4
Vx-809 mitigates the oxidative damage caused by Thapsigargin. To cause ER stress, cells were pretreated with 300 nM TG for 30 min, 1 h, or 4 h. The corrector Vx-809 (2 µM) was then administered for a whole day. The probe 2′,7′-dichlorofluorescein diacetate (H2DCF-DA) was used to measure the amount of ROS produced in SH-SY5Y cells (Panel (A)). The percentage of DCF-positive cells in at least three independent experiments, each conducted in duplicate, was used to express the mean ± SEM of ROS generation. Using the MitoSOX Red probe, flow cytometry analysis was used to measure the amount of superoxide produced by the mitochondria in cells (Panel (B)). The expression of mitochondrial superoxide generation was calculated as the mean ± standard error of the proportion of cells positive for MitoSOX in three separate tests, each carried out in duplicate. SODIII expressions (Panel (C)) on neuroblastoma cells were detected by a Western blotting assay. Actin protein expression was used as loading control. The Mann–Whitney U test was used to evaluate the data. ** p < 0.005 and *** p < 0.001 vs. untreated cells; ° p < 0.05 vs. Vx-809-treated cells; # p < 0.05 and ## p < 0.005 vs. TG-treated cells. Full article ">Figure 4 Cont.
Vx-809 mitigates the oxidative damage caused by Thapsigargin. To cause ER stress, cells were pretreated with 300 nM TG for 30 min, 1 h, or 4 h. The corrector Vx-809 (2 µM) was then administered for a whole day. The probe 2′,7′-dichlorofluorescein diacetate (H2DCF-DA) was used to measure the amount of ROS produced in SH-SY5Y cells (Panel (A)). The percentage of DCF-positive cells in at least three independent experiments, each conducted in duplicate, was used to express the mean ± SEM of ROS generation. Using the MitoSOX Red probe, flow cytometry analysis was used to measure the amount of superoxide produced by the mitochondria in cells (Panel (B)). The expression of mitochondrial superoxide generation was calculated as the mean ± standard error of the proportion of cells positive for MitoSOX in three separate tests, each carried out in duplicate. SODIII expressions (Panel (C)) on neuroblastoma cells were detected by a Western blotting assay. Actin protein expression was used as loading control. The Mann–Whitney U test was used to evaluate the data. ** p < 0.005 and *** p < 0.001 vs. untreated cells; ° p < 0.05 vs. Vx-809-treated cells; # p < 0.05 and ## p < 0.005 vs. TG-treated cells. Full article ">Figure 5
Vx-809 alters the process of apoptosis. Neuroblastoma cells were pretreated with 300 nM TG for 30 min, 2 h, or 4 h, to induce ER stress. Subsequently, 2 µM of the Vx-809 was administered for 24 h. After, the cells were stained by propidium iodide, and the fluorescence of individual nuclei was evaluated by flow cytometry (Panel (A)). The data are presented as the mean ± standard error of the percentage of hypodiploid nuclei from a minimum of three independent tests, each carried out in duplicate. The percentage of caspase 4 positive cells (Panel (B)) from at least three separate experiments, each carried out in duplicate, was given as mean ± S.E.M. The Mann–Whitney U test was utilized for data analysis. * p < 0.05, ** p < 0.05 and *** p < 0.001 vs. non-treated cells; ° p < 0.05 vs. Vx-809-treated cells; ## p < 0.005 and ### p < 0.001 vs. TG-treated cells. Full article ">

16 pages, 4106 KiB

Open AccessArticle

Hypomyelination Leukodystrophy 16 (HLD16)-Associated Mutation p.Asp252Asn of TMEM106B Blunts Cell Morphological Differentiation

by Sui Sawaguchi, Miki Ishida, Yuki Miyamoto and Junji Yamauchi

Curr. Issues Mol. Biol. 2024, 46(8), 8088-8103; https://doi.org/10.3390/cimb46080478 - 27 Jul 2024

Viewed by 923

Abstract

Transmembrane protein 106B (TMEM106B), which is a type II transmembrane protein, is believed to be involved in intracellular dynamics and morphogenesis in the lysosome. TMEM106B is known to be a risk factor for frontotemporal lobar degeneration and has been recently identified as the receptor needed for the entry of SARS-CoV-2, independently of angiotensin-converting enzyme 2 (ACE2). A missense mutation, p.Asp252Asn, of TMEM106B is associated with hypomyelinating leukodystrophy 16 (HLD16), which is an oligodendroglial cell-related white matter disorder causing thin myelin sheaths or myelin deficiency in the central nervous system (CNS). However, it remains to be elucidated how the mutated TMEM106B affects oligodendroglial cells. Here, we show that the TMEM106B mutant protein fails to exhibit lysosome distribution in the FBD-102b cell line, an oligodendroglial precursor cell line undergoing differentiation. In contrast, wild-type TMEM106B was indeed localized in the lysosome. Cells harboring wild-type TMEM106B differentiated into ones with widespread membranes, whereas cells harboring mutated TMEM106B failed to differentiate. It is of note that the output of signaling through the lysosome-resident mechanistic target of rapamycin (mTOR) was greatly decreased in cells harboring mutated TMEM106B. Furthermore, treatment with hesperetin, a citrus flavonoid known as an activator of mTOR signaling, restored the molecular and cellular phenotypes induced by the TMEM106B mutant protein. These findings suggest the potential pathological mechanisms underlying HLD16 and their amelioration. Full article

(This article belongs to the Special Issue Molecules at Play in Neurological Diseases)

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Figure 1
TMEM106B protein with the HLD16-associated D252N mutation is widely distributed throughout the cytoplasmic regions. (A) FBD-102b cells (surrounded by white dotted lines) were transfected with the plasmid encoding wild-type (WT) TMEM106B tagged with EGFP at its C-terminus or EGFP-tagged TMEM106B with the D252N mutation. Transfected cells were stained with DAPI for nuclear staining. Scan plots were created along the white dotted lines in the direction of the arrows in the images. (B) Graphs showing fluorescence intensities (F.I., arbitrary units) along the white dotted lines in the direction of the arrows are presented at the bottom of the representative fluorescence images. (C) Cells with abnormal, widely distributed structures were counted and statistically depicted (** p < 0.01; n = 10 fields). Full article ">Figure 2
Mutated TMEM106B is present in the lysosome. (A) Cells (surrounded by white dotted lines) were transfected with the plasmid encoding mutated TMEM106B (D252N). Transfected cells were stained with the respective antibodies against ER-specific KDEL, Golgi body-specific GM130, and lysosome-resident LAMP1. Scan plots were created along the white dotted lines in the direction of the arrows in the images. (B) Graphs showing fluorescence intensities (F.I., arbitrary units) along the white dotted lines in the direction of the arrows are presented at the bottom of the representative fluorescence images. (C) The respective merged percentages are depicted in bar graphs (n = 3 fields). Full article ">Figure 3
Cells harboring mutated TMEM106B show decreased cell differentiation abilities. (A) Cells harboring wild-type (WT) or mutated (D252N) TMEM106B were allowed to differentiate for 0 or 5 days. Cells surrounded with dotted red lines in the middle panels are magnified in the right panels. The cell surrounded by a white dotted line is a typically differentiated one with widespread membranes. (B) Differentiated cells are statistically depicted (** p < 0.01; n = 10 fields). (C) The lysates of cells at 5 days following the induction of differentiation were immunoblotted with the respective antibodies against differentiation markers PLP1 and MBP, cell lineage marker Sox10, and internal control actin. (D) Quantification of immunoreactive bands, using control immunoreactive bands as 100%, is depicted in the respective graphs of PLP1, MBP, Sox10, and actin (** p < 0.01; n = 3 blots). Full article ">Figure 4
Cells harboring mutated TMEM106B show decreased phosphorylation levels of ribosomal S6 and translational 4E-BP1 proteins. (A) The lysates of cells at 5 days following the induction of differentiation were immunoblotted with the respective antibodies against phosphorylated ribosomal S6 and translational 4E-BP1 proteins (pS6 and p4E-BP1). Total ribosomal S6 and translational 4E-BP1 protein (S6 and 4E-BP1) bands are also presented. (B) Quantification of immunoreactive bands, using control immunoreactive bands as 100%, is depicted in the respective graphs of pS6, S6, p4E-BP1, and 4E-BP1 (** p < 0.01; n = 3 blots). Full article ">Figure 5
Hesperetin recovers phenotypes of cells harboring mutated TMEM106B. (A) Cells harboring mutated TMEM106B were allowed to differentiate for 0 or 5 days in the presence or absence of 10 μm hesperetin (DMSO as the vehicle). Cells surrounded with dotted red lines in the middle panels are magnified in the right panels. The cell surrounded by a white dotted line is a typically differentiated one with widespread membranes. (B) Differentiated cells are statistically depicted (** p < 0.01; n = 10 fields). (C) The lysates of cells at 5 days following the induction of differentiation were immunoblotted with the respective antibodies against differentiation markers PLP1 and MBP, cell lineage marker Sox10, and internal control actin. (D) Quantification of immunoreactive bands, using hesperetin plus immunoreactive bands as 100%, is depicted in the respective graphs of PLP1, MBP, Sox10, and actin (** p < 0.01; n = 3 blots). Full article ">Figure 6
Hesperetin recovers decreased phosphorylation levels of ribosomal S6 and translational 4E-BP1 proteins in cells harboring mutated TMEM106B. (A) The lysates of cells at 5 days following the induction of differentiation in the presence or absence of hesperetin were immunoblotted with the respective antibodies against phosphorylated ribosomal S6 and translational 4E-BP1 proteins (pS6 and p4E-BP1). Total ribosomal S6 and translational 4E-BP1 protein (S6 and 4E-BP1) bands are also presented. (B) Quantification of immunoreactive bands, using hesperetin plus immunoreactive bands as 100%, is depicted in the respective graphs of pS6, S6, p4E-BP1, and 4E-BP1 (** p < 0.01; n = 3 blots). Full article ">

18 pages, 310 KiB

Open AccessArticle

Serum Levels of Zinc, Albumin, Interleukin-6 and CRP in Patients with Unipolar and Bipolar Depression: Cross Sectional Study

by Tihana Bagarić, Alma Mihaljević-Peleš, Milena Skočić Hanžek, Maja Živković, Ana Kozmar and Dunja Rogić

Curr. Issues Mol. Biol. 2024, 46(5), 4533-4550; https://doi.org/10.3390/cimb46050275 - 9 May 2024

Viewed by 1150

Abstract

Unipolar (UD) and bipolar depression (BDD) show a high degree of similarity in clinical presentations, which complicates the differential diagnosis of these disorders. The aim of this study was to investigate the serum levels of interleukin 6 (IL-6), C-reactive protein (CRP), albumin (Alb), and zinc (Zn) in patients with UD, BDD, and healthy controls (HC). A total of 211 samples were collected: 131 patient samples (65 UD and 68 BDD) and 80 HC. The Montgomery–Asberg Depression Rating Scale (MADRS), along with the Hamilton Depression Rating Scale (HAMD-17), were administered to patient groups to evaluate symptoms. A cross-sectional study was performed to analyse the serum levels of IL-6, CRP, albumin, and zinc. The concentration of CRP was determined using the immunoturbidimetry method, zinc using the colorimetric method, and albumin using the colorimetric method with bromocresol green on the Alinity c device. IL-6 cytokine concentration in serum samples was ascertained using a commercial enzyme immunoassay, ELISA. We found no significant differences in serum concentrations of zinc, albumin, CRP, and IL-6 between the groups of patients with unipolar and bipolar depression. There was a significant statistical difference (p < 0.001) between serum levels of all investigated parameters in both groups of depressed patients in comparison with HC. Furthermore, correlations with specific items on HAMD-17; (namely, hypochondrias, work and activities, somatic symptoms-general, and weight loss) and on MADRS (concentration difficulties, lassitude) were observed in both patient groups. These findings confirm the presence of low-grade inflammation in depression, thus adding better insight into the inflammation hypothesis directed to explain the aetiology of depressive disorders. Our results do not indicate potential biomarkers for distinguishing between unipolar and bipolar depression. Full article

(This article belongs to the Special Issue Molecules at Play in Neurological Diseases)

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21 pages, 1746 KiB

Open AccessReview

Unlocking the Potential: Semaglutide’s Impact on Alzheimer’s and Parkinson’s Disease in Animal Models

by Andreea Daniela Meca, Ianis Kevyn Stefan Boboc, Liliana Mititelu-Tartau and Maria Bogdan

Curr. Issues Mol. Biol. 2024, 46(6), 5929-5949; https://doi.org/10.3390/cimb46060354 - 13 Jun 2024

Cited by 4 | Viewed by 3556

Abstract

Semaglutide (SEM), a glucagon-like peptide-1 receptor agonist, has garnered increasing interest for its potential therapeutic effects in neurodegenerative disorders such as Alzheimer’s disease (AD) and Parkinson’s disease (PD). This review provides a comprehensive description of SEM’s mechanism of action and its effects in preclinical studies of these debilitating conditions. In animal models of AD, SEM has proved beneficial effects on multiple pathological hallmarks of the disease. SEM administration has been associated with reductions in amyloid-beta plaque deposition and mitigation of neuroinflammation. Moreover, SEM treatment has been shown to ameliorate behavioral deficits related to anxiety and social interaction. SEM-treated animals exhibit improvements in spatial learning and memory retention tasks, as evidenced by enhanced performance in maze navigation tests and novel object recognition assays. Similarly, in animal models of PD, SEM has demonstrated promising neuroprotective effects through various mechanisms. These include modulation of neuroinflammation, enhancement of mitochondrial function, and promotion of neurogenesis. Additionally, SEM has been shown to improve motor function and ameliorate dopaminergic neuronal loss, offering the potential for disease-modifying treatment strategies. Overall, the accumulating evidence from preclinical studies suggests that SEM holds promise as a novel therapeutic approach for AD and PD. Further research is warranted to elucidate the underlying mechanisms of SEM’s neuroprotective effects and to translate these findings into clinical applications for the treatment of these devastating neurodegenerative disorders. Full article

(This article belongs to the Special Issue Molecules at Play in Neurological Diseases)

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