Showing posts with label neurodegenerative diseases. Show all posts
Showing posts with label neurodegenerative diseases. Show all posts

Sunday, April 12, 2026

Cannabidiol (CBD) further confirmed to reverse brain damage in mouse model of Alzheimer's disease

Good news!

"... The non-psychoactive compound derived from the Cannabis sativa plant, called cannabidiol (CBD), was recently found to show promise for protecting brain cells from damage.

Compared to Δ9-tetrahydrocannabinol (THC), the compound in cannabis that elicits feelings of euphoria and alters a user's mental state, CBD is safer and could thus be easier to introduce in clinical settings. ...

Du and her colleagues studied a mouse model of AD known as triple-transgenic AD mice. These are genetically modified mice whose synapses become progressively damaged, following the formation of Tau protein tangles and the accumulation of Aβ. These mice exhibit characteristics that resemble those observed in patients with AD, such as memory loss and anxiety-like behaviors.

First, the researchers treated the mice with CBD six days per week for a total period of 45 days. After this treatment period, they observed the mice's behavior and examined their brains.

Interestingly, they found that the mice's memory had improved after treatment and their anxiety levels appeared lower. In addition, dendritic spines in their brains and the overall structure of synapses (i.e., junctions between neurons) appeared to be restored.

"We next looked at how CBD achieves the effects we observed," said Du. "We found that it activates the TrkB-PI3K-AKT pathway—a critical pathway for neuronal survival and plasticity. ..."

From the abstract:
"Alzheimer’s disease (AD) is characterized by progressive synaptic failure, neuroinflammation, amyloid and tau pathology, yet effective disease-modifying therapies remain limited. Cannabidiol (CBD) has shown neuroprotective potential in AD, but its direct molecular targets and signaling mechanisms remain unclear. Here, we demonstrate that CBD ameliorates cognitive and emotional deficits in 3×Tg-AD mice by restoring synaptic integrity and plasticity.
At the mechanistic level, CBD activated TrkB signaling independently of BDNF, leading to suppression of tau hyperphosphorylation via the PI3K/AKT/GSK3β pathway and attenuation of neuroinflammation and amyloid pathology through inhibition of the JAK2/STAT3/SOCS1 axis.
Using isothermal shift assays combined with biophysical binding analyses, we identified FRS2, a core adaptor protein of TrkB, as a direct molecular target of CBD
Molecular dynamics simulations further revealed that CBD stabilizes the FRS2–TrkB interface, thereby facilitating TrkB activation.
Importantly, genetic knockdown of FRS2 abolished CBD-induced TrkB signaling and its downstream neuroprotective effects in both cellular and in vivo AD models. Together, these findings identify FRS2 as a critical signaling node mediating BDNF-independent TrkB activation by CBD and establish a mechanistic framework linking CBD to disease-modifying pathways in AD."

CBD found to reverse brain damage in mouse model of Alzheimer's disease

Monday, March 16, 2026

Parthanatos pathway behind neuron loss in multiple sclerosis identified

Good news! This research indicates possible new treatment options!

"... Researchers... recently carried out a mouse study investigating the possible contribution of a specific molecular process that leads to cell death, called parthanatos, in the loss of neurons resulting from neuroinflammation, such as that associated with MS. Their findings ... suggest that damage to neurons associated with MS is caused by immune responses that trigger internal cell death programs. ...

The researchers subsequently blocked the final stage of parthanatos using genetic pharmacological approaches to inhibit MIF nuclease activity. MIF nuclease is the enzyme responsible for DNA damage in parthanathos. Remarkably, they found that blocking this enzyme reduced DNA fragmentation, led to the survival of more neurons and significantly lowered the severity of the symptoms presented by mice. ..."

From the abstract:
"Central nervous system inflammation is implicated in neurodegeneration across several disorders, including multiple sclerosis (MS). While marked therapeutic progress has been made in preventing relapses in MS, primary neuroprotection in this disease remains elusive. This, in part, is due to an incomplete understanding of the molecular pathways involved in immune-mediated neuronal death.
Here we show that parthanatos, a recently described caspase-independent and DNA damage-induced cell death program, contributes to neuron death in the experimental autoimmune encephalomyelitis (EAE) mouse model of autoimmune neuroinflammation.
We reveal that DNA damage increases in neurons during EAE, and that neurons are progressively lost over the disease course. Neurons in affected areas display intracellular hallmarks of the parthanatos cascade.
Genetic or pharmacologic blockade of the final step in parthanatos, genomic fragmentation by macrophage migration inhibitory factor (MIF) nuclease, reduces neuron loss and disease severity.
Transcriptomic characterization of neurons with and without MIF nuclease activity reveals parthanatos-dependent differences in response to EAE. Together, this work establishes parthanatos as a key mechanism of neuron cell death during neuroinflammation."

Parthanatos pathway behind neuron loss in multiple sclerosis identified



Fig. 2: Accumulation of parthanatos markers in lumbar spinal cord neurons during EAE.


Saturday, February 07, 2026

Scientists uncover why some brain cells resist Alzheimer's disease and they identified a key player

Good news!

"Key takeaways
  • Tau is the most common protein that aggregates in neurodegeneration diseases. However, researchers had not determined why some types of neurons are affected more than others.
  • The work identified a protein complex called CRL5SOCS4 that marks tau for degradation. The findings suggest that strengthening this natural defense mechanism could represent a new therapeutic strategy for neurodegenerative diseases.
  • Enhancing CRL5SOCS4 activity could help neurons clear tau more effectively, while strategies to maintain proteasome function during stress might prevent the formation of toxic tau fragments.
...

uncovered why certain brain cells are more resilient than others to the buildup of a toxic protein that is a hallmark of Alzheimer’s disease and related dementias ...

used a novel CRISPR-based genetic screening approach on lab-grown human brain cells to determine the cellular machinery that controls the accumulation of tau protein in the brain. ...

Among more than 1,000 genes identified, the CRL5SOCS4 protein complex emerged as a key player that attaches molecular tags to tau, marking it for destruction by the cell’s recycling machinery.

Importantly, analysis of brain tissue from Alzheimer’s patients revealed that higher expression of CRL5SOCS4 components made neurons more likely to survive despite the accumulation of tau protein. 

The study also revealed an unexpected connection between mitochondrial dysfunction and tau toxicity. When the researchers disrupted the cellular powerhouses that generate energy, they triggered the production of a specific tau fragment approximately 25 kilodaltons in size. This fragment closely resembles a biomarker found in the blood and spinal fluid of Alzheimer’s patients, known as NTA-tau. ..."

From the highlights and abstract:
"Highlights
• CRISPR screens in human neurons reveal modifiers of tau oligomer accumulation
• CUL5 and the substrate-specific adaptor SOCS4 function as tau E3 ubiquitin ligase
• Expression of CUL5 complexes is correlated with resilience in tauopathies
• Reactive oxygen species generate a disease-relevant tau proteolytic fragment

Summary
Aggregation of the protein tau defines tauopathies, the most common age-related neurodegenerative diseases, which include Alzheimer’s disease and frontotemporal dementia. Specific neuronal subtypes are selectively vulnerable to tau aggregation, dysfunction, and death. However, molecular mechanisms underlying cell-type-selective vulnerability are unknown. To systematically uncover the cellular factors controlling the accumulation of tau aggregates in human neurons, we conducted a genome-wide CRISPRi screen in induced pluripotent stem cell (iPSC)-derived neurons. The screen uncovered both known and unexpected pathways, including UFMylation and GPI anchor biosynthesis, which control tau oligomer levels. We discovered that the E3 ubiquitin ligase CRL5SOCS4 controls tau levels in human neurons, ubiquitinates tau, and is correlated with resilience to tauopathies in human disease. Disruption of mitochondrial function promotes proteasomal misprocessing of tau, generating disease-relevant tau proteolytic fragments and changing tau aggregation in vitro. These results systematically reveal principles of tau proteostasis in human neurons and suggest potential therapeutic targets for tauopathies."

Scientists uncover why some brain cells resist Alzheimer's disease | UCLA "Study identifies cellular defense system that protects neurons from toxic tau proteins, opening door to new treatments"



Graphical abstract


Saturday, January 31, 2026

A new molecular atlas of tau enables precision diagnostics and drug targeting across neurodegenerative diseases

Good news!

"Tau protein aggregation is a shared feature in over 20 neurodegenerative diseases (collectively referred to as "tauopathies"). New research led by Boston Children's Hospital challenges the current "one-size-fits-all" approach to diagnosing and treating these tauopathies. ...

analyzed brain tissue from 203 patients spanning several tauopathies, including Alzheimer's disease and chronic traumatic encephalopathy (CTE). They used a novel mass spectrometry tool called FLEXITau which enables absolute quantification of pathological tau species, measuring both the identities and abundances of disease-relevant chemical modifications. ...

that tau chemistry changes as the disease advances, and that the p217 Tau modification ranked as the most accurate diagnostic for Alzheimer's. p217 is now an FDA-approved diagnostic marker for Alzheimer's disease. ...

Using FLEXITau, the researchers identified 145 post-translational modifications and 195 cleavage sites across tau. Machine-learning models then ranked the molecular features that best distinguished each disease based on quantified chemical changes. ..."

From the highlights and abstract:
"Highlights
• Comprehensive mapping of tau identifies 145 PTMs and 195 cleavage sites in tauopathies
• Provides tau molar abundance and peptide modification stoichiometry in disease
• Machine learning classifies tauopathies using tau molecular features
• Identified disease-specific features are potential drug targets and diagnostics

Summary
In Alzheimer’s disease (AD), pathological tau protein shows a progressive accumulation of post-translational modifications (PTMs), reflecting disease severity, progression, and prion-like activity. Although many neurodegenerative diseases with dementia display tau aggregates, the pathological proteoforms of tau protein from each disease type remain unknown.
Here, using a quantitative mass spectrometry-based proteomics platform, FLEXITau, deep characterization of pathological tau protein isolated from the brains of 203 human subjects with AD, familial AD (fAD), chronic traumatic encephalopathy (CTE), corticobasal degeneration (CBD), Pick’s disease (PiD), progressive supranuclear palsy (PSP), dementia with Lewy bodies (DLB)—a non-tauopathy symptomatic control—and healthy controls (CTR) is performed. Unsupervised data analyses and supervised machine learning identify distinct molecular features of pathological tau for each disease, enabling molecular disease stratification.
This study identifies potential disease-specific biomarkers and therapeutic targets for tauopathies and provides critical quantitative information for pharmacokinetic modeling required for therapeutic and disease mechanism studies."

A new molecular atlas of tau enables precision diagnostics and drug targeting across neurodegenerative diseases


Graphical abstract



Figure 1 Workflow and quantification of pathological insoluble tau and isoforms across tauopathies and control human subjects


Saturday, December 06, 2025

How antibody therapy clears Alzheimer's plaques: Key immune mechanism identified

Good news!

"Lecanemab, sold under the name Leqembi, is a monoclonal antibody therapy for Alzheimer's disease that clears toxic amyloid plaques and delays cognitive decline. ...

They showed that the "Fc fragment" of this monoclonal antibody is essential for engaging microglia—the immune cells of the brain—thus initiating the cellular machinery needed for plaque removal. This is the first direct mechanistic explanation for how this class of therapies works. It clarifies uncertainties in the field and offers a blueprint for developing safer, more effective Alzheimer's treatments.  ...

They identified key cellular machinery needed to clear the amyloid plaques: namely, phagocytosis and lysosomal activity.

Without the Fc fragment, none of these critical cellular processes were triggered. ...  uncovered a microglial gene program, marked by strong expression of the gene SPP1.  ..."

From the abstract:
"Controversies over anti-amyloid immunotherapies underscore the need to elucidate their mechanisms of action.
Here we demonstrate that Lecanemab, a leading anti-β-amyloid (Aβ) antibody, mediates amyloid clearance by activating microglial effector functions.
Using a human microglia xenograft mouse model, we show that Lecanemab significantly reduces Aβ pathology and associated neuritic damage, while neither fragment crystallizable (Fc)-silenced Lecanemab nor microglia deficiency elicits this effect despite intact plaque binding.
Single-cell RNA sequencing and spatial transcriptomic analyses reveal that Lecanemab induces a focused transcriptional program that enhances phagocytosis, lysosomal degradation, metabolic reprogramming, interferon γ genes and antigen presentation.
Finally, we identify SPP1/osteopontin as a major factor induced by Lecanemab treatment and demonstrate its role in promoting Aβ clearance.
These findings highlight that effective amyloid removal depends on the engagement of microglia through the Fc fragment, providing critical insights for optimizing anti-amyloid therapies in Alzheimer’s disease."

How antibody therapy clears Alzheimer's plaques: Key immune mechanism identified

New immune process identified that may alleviate Alzheimer's disease (original news release)



Fig. 1: Lecanemab drives strong transcriptional changes in human microglia associated with Aβ plaques.


Fig. 2: Lecanemab alleviates Aβ pathology by triggering effector functions in the microglia.


Sunday, November 16, 2025

NAD+ Corrects RNA Splicing to Restore Alzheimer's Memory

Good news!

"Boosting levels of a certain molecule that declines with age was found to restore memory and brain function in Alzheimer’s disease (AD) models – not just by improving energy metabolism, as previously thought, but by fixing RNA splicing errors that disrupt hundreds of genes crucial to neuron health. ...

a team of scientists ... has uncovered a mechanism driven by the natural metabolite, oxidized nicotinamide adenine dinucleotide (NAD⁺), which can shield the brain from the progressive damage of AD. ...

"Preliminary studies have shown that supplementation with NAD⁺ precursors, such as nicotinamide riboside (NR) or nicotinamide mononucleotide (NMN), can offer therapeutic benefits in AD animal models and early clinical trials," ... "However, the molecular mechanisms behind these benefits remain largely unclear." ..."

"... The new study reveals that NAD⁺ works through a previously unidentified RNA-splicing pathway. This pathway is regulated by a protein called EVA1C, which plays an essential role in the process of RNA splicing. RNA splicing allows a single gene to produce multiple isoforms of a protein, and one isoform may show distinctive effects to the other isoforms. Its dysregulation is one of the most recently acknowledged risk factor for AD.

The researchers discovered that when NAD⁺ levels are increased, EVA1C helps correct mistakes in RNA splicing. This restoration process improves the function of hundreds of genes, many crucial for brain health, which can help reverse the neurodegenerative damage caused by tau. ..."

From the abstract:
"Dysfunctional alternative splicing events (ASEs) in RNA are markers of aging and Alzheimer’s disease (AD).
As a key neuronal resilience metabolite, the oxidized nicotinamide adenine dinucleotide (NAD+) slows down AD progression in preclinical studies with several clinical trials ongoing. However, the underlying molecular mechanisms around how NAD+ enhances neuronal resilience, especially whether it has any effect on ASEs, have remained elusive.
This study shows that NAD+ augmentation corrects the ASEs of many genes via a key protein, EVA1C (epithelial V-like antigen 1 homolog C), which is involved in neuronal development and activities.
EVA1C is reduced in the hippocampus in patients with AD compared to cognitively normal ones.
NAD+-induced memory retention is partially dependent on EVA1C, as adeno-associated virus–based Eva1c knockdown in the hippocampal CA1 region annuls NAD+-induced memory improvement in pathological Tau–bearing mice.
We propose that NAD+ reduces AD pathologies, at least partially, via amplification of the NAD+-EVA1C splicing axis, pointing to a potential splice-switching therapy for AD."

NAD+ Corrects RNA Splicing to Restore Alzheimer's Memory

NAD⁺ restores memory in Alzheimer’s’ disease models by correcting RNA errors "A groundbreaking international study shows how boosting a natural molecule can help restore memory in animal models of Alzheimer’s disease. The new study offers hope for developing new therapies for patients with Alzheimer’s disease."



Fig. 1. Compromised mRNA splicing in Tau pathology and aging.


Monday, October 13, 2025

Scientists reverse Alzheimer's in mice using nanoparticles

Good news!

"... Unlike traditional nanomedicine, which relies on nanoparticles as carriers for therapeutic molecules, this approach employs nanoparticles that are bioactive in their own right: "supramolecular drugs." ...

Instead of targeting neurons directly, the therapy restores the proper function of the blood-brain barrier (BBB) ... By repairing this critical interface, the researchers achieved a reversal of Alzheimer's pathology in animal models. ...

The team demonstrated that targeting a specific mechanism enables undesirable "waste proteins" produced in the brain to pass through this barrier and be eliminated in the blood flow. In Alzheimer's disease, the main "waste" protein is amyloid-β (Aβ), whose accumulation impairs the normal functioning of the neurons. ..."

From the abstract:
"The blood‒brain barrier (BBB) is a highly selective permeability barrier that safeguards the central nervous system (CNS) from potentially harmful substances while regulating the transport of essential molecules. Its dysfunction is increasingly recognized as a pivotal factor in the pathogenesis of Alzheimer’s disease (AD), contributing to the accumulation of amyloid-β (Aβ) plaques.
We present a novel therapeutic strategy that targets low-density lipoprotein receptor-related protein 1 (LRP1) on the BBB. Our design leverages the multivalent nature and precise size of LRP1-targeted polymersomes to modulate receptor-mediated transport, biasing LRP1 trafficking toward transcytosis and thereby upregulating its expression to promote efficient Aβ removal.
In AD model mice, this intervention significantly reduced brain Aβ levels by nearly 45% and increased plasma Aβ levels by 8-fold within 2 h, as measured by ELISA.
Multiple imaging techniques confirmed the reduction in brain Aβ signals after treatment.
Cognitive assessments revealed that treated AD mice exhibited significant improvements in spatial learning and memory, with performance levels comparable to those of wild-type mice.
These cognitive benefits persisted for up to 6 months post-treatment.
This work pioneers a new paradigm in drug design, where function arises from the supramolecular nature of the nanomedicine, harnessing multivalency to elicit biological action at the membrane trafficking level.
Our findings also reaffirm the critical role of the BBB in AD pathogenesis and demonstrate that targeting the BBB can make therapeutic interventions significantly more effective.
We establish a compelling case for BBB modulation and LRP1-mediated Aβ clearance as a transformative foundation for future AD therapies."

Scientists reverse Alzheimer's in mice using nanoparticles



Fig. 1 Schematics of LRP1 shuttling across brain endothelial cells




Monday, October 06, 2025

Alzheimer’s precursor protein may boost aging immune system and improves antitumor immunity

Amazing stuff!

"A protein notorious for its role in Alzheimer’s disease may hold the key to supercharging the aging immune system, according to new research. Scientists have found that a byproduct of amyloid-beta rejuvenates T cells, boosting their tumor-fighting power and dramatically reducing cancer risk. ...

In the present study, five years of nationally representative surveys were analyzed, and the researchers found that adults over 59 with Alzheimer’s disease were a staggering 21 times less likely to develop cancer than those without the disease. ..."

"... Their new study ... reveals how a protein tied to Alzheimer’s disease also strengthens the immune system, offering insights that could inspire innovative treatments for cancer, aging and neurodegenerative diseases. ...

To test this finding, the researchers transplanted mitochondria from Alzheimer’s T-cells into aging T-cells that did not have Alzheimer’s. ...

“Older T-cells began functioning like young, active T-cells again. That was an incredible finding because it suggests a whole new way to think about rejuvenating the immune system.”

The results also revealed that amyloid beta contributes to cancer in another way – by depleting fumarate, a small molecule made inside mitochondria during energy production. Fumarate acts like a brake, keeping mitophagy from running out of control. When fumarate levels drop, cells recycle too many of their healthy mitochondria, resulting in a loss of strength. ..."

From the abstract:
"Patients with Alzheimer's disease (AD) have a decreased incidence of cancer, with a cross-sectional analysis of a nationwide sample of adults finding 21-fold higher odds of cancer diagnosis in non-AD individuals compared with those with AD.
In this study, we demonstrated that mitochondrial localization of AD-associated amyloid-β precursor protein (APP) and its cleavage product amyloid-β 40, but not mutant APP that lacks a mitochondrial localization signal, inhibits lipid stress–mediated hyperactive mitophagy in aging T cells, improving their antitumor functions.
Growth of melanoma xenograft or carcinogen-induced oral cancer models was highly reduced in AD mice. Additionally, adoptive cell transfer–based immunotherapy using aging T cells isolated from AD mice suppressed tumor growth.
The metabolic signature of stress-dependent mitophagy in T cells showed fumarate depletion, which was linked to decreased succination of Parkin and enhanced mitochondrial damage.
Mechanistically, APP interaction with the TOMM complex at the outer mitochondrial membrane attenuated trafficking of ceramide synthase CerS6 to mitochondria in aging AD T cells, preventing ceramide-dependent mitophagy. Thus, APP restored mitochondrial fumarate metabolism and Parkin succination, improving antitumor functions of AD T cells in vitro and in vivo.
Exogenous fumarate supplementation or healthy AD mitochondria transfer functionally mimicked the AD/APP phenotype in aging T cells, enhancing their antitumor activity to control tumor growth.
Moreover, T cells isolated from aging donors showed elevated mitophagy with fumarate depletion, which was restored in T cells isolated from age-matched patients with AD.
Together, these findings show that AD protects T cells against ceramide-dependent mitophagy and fumarate depletion to enhance antitumor functions."

Alzheimer’s protein may boost aging immune system


Sunday, October 05, 2025

Neurons may use newly discovered nanotubes to communicate and spread disease

Amazing stuff! This could be huge!

"Neuroscientists have been studying synapses, the fundamental junctions that allow rapid communication between neurons, for well over a century. But now, a research team has identified a different set of neuronal connections in the brain—one that might bypass synapses altogether.

Using high-resolution images of mouse and human brains, the researchers documented a network of tubes, each about 3 micrometers long and just a few hundred nanometers thick, connecting neurons to one another.
In mouse cells, the team found evidence of neuron-to-neuron transfer of electrical signals via these nanotubes. They also showed that beta amyloid, a protein implicated in Alzheimer’s disease, moved along these tubes from one cell to the next when inserted into mouse neurons. ..."

From the editor's summary and abstract:
"Editor’s summary
Synaptic connections mediate classical intercellular communication in the brain. However, recent data have demonstrated the existence of noncanonical routes of interneuronal communication mediating the transport of materials including calcium, mitochondria, and pathogenic proteins such as amyloid beta (Aβ). Using super-resolution and electron microscopy, Chang et al. identified and characterized structures called nanotubular bridges that connect dendrites in the brain ... These bridges mediate the transport of calcium ions, small molecules, and Aβ peptides, and may contribute to the spreading and accumulation of pathological Aβ in Alzheimer’s disease. ...

Structured Abstract
INTRODUCTION
Communication between neurons is fundamental to brain function and has long been thought to occur primarily through specialized junctions called synapses. However, the observed transfer of large molecules and proteins between neurons suggests the existence of other, less understood communication pathways.
In other biological systems, long-range intercellular transport is mediated by ultrathin membrane bridges known as nanotubes.
These structures can transport a vast range of materials, from small ions (10−10 m) to large mitochondria (10−6 m). Despite their potential importance, the fragile, dynamic nature of nanotubes and a lack of specific markers have made them difficult to study in tissue, leaving their existence and physiological role in the brain unconfirmed. We hypothesized that a network of these nanotubes forms an additional layer of neuronal connectivity, operating in parallel with synapses.

RATIONALE
In other cell types, nanotubes often form when thin, exploratory cell protrusions contact a neighboring cell and establish a stable connection.
In the brain, dendritic protrusions, known as filopodia, have historically been viewed only as precursors to synapses.
The possibility that they could form nonsynaptic connections with other dendrites has been largely overlooked.
Our investigation began by reexamining existing high-resolution electron microscopy images of mouse and human brain tissue. We discovered instances where a filopodium from one neuron’s dendrite formed a direct, membrane-to-membrane contact with the dendrite of a neighboring neuron without any of the typical structural features of a chemical synapse. This observation led us to propose that these were a previously unidentified form of neuronal connection: dendritic nanotubes.

RESULTS
By using advanced superresolution microscopy on specially prepared mouse brain tissue, we visualized these dendritic nanotubes connecting pyramidal neurons in the primary visual cortex.
A machine learning–based classification confirmed that their shape was distinct from that of synaptic structures.
In cultured neurons, we observed these nanotubes forming dynamically and confirmed that they possessed a distinct internal structure, setting them apart from other neuronal extensions.
Functionally, these neuronal nanotubes created a path for calcium signals to travel between connected neurons; blocking nanotube formation halted this nonsynaptic transfer.

To test whether these nanotubular structures could transport disease-related molecules, we injected human β-amyloid (Aβ), a peptide central to Alzheimer’s disease (AD), into a single neuron in a mouse brain slice. The peptides spread to neighboring neurons, and this propagation was stopped when nanotube formation was inhibited, confirming that the nanotubes acted as direct conduits.

Lastly, we investigated the role of these dendritic nanotubes in a mouse model of AD. We found that the nanotube network was significantly altered early in the disease, even before the formation of amyloid plaques, a hallmark of AD.
Our computational model supported these findings, predicting that overactivation in the nanotube network could accelerate the toxic accumulation of amyloid in specific neurons, thereby providing a mechanistic link between nanotube alterations and the progression of AD pathology.

CONCLUSION
This study provides the first comprehensive characterization of a nanotubular communication network in the brain, establishing a new framework for nonsynaptic signaling between neurons. By demonstrating that these dendritic nanotubes can transport disease-implicated proteins, such as Aβ, we have revealed a previously unknown mechanism that may contribute to the spread of pathology in the early stages of neurodegenerative disorders. The discovery of this parallel neural network opens up entirely new avenues for research into brain connectivity, intercellular communication, and the fundamental processes driving neurological disease."

ScienceAdviser

Hidden networks in the brain (Perspective, no public access)




Neuronal nanotubes mediate intercellular transport and disease.


Supplementary Figure 1.
Nonsynaptic dendritic filopodia contacting other dendrites in the EM-resolved mouse brain


Figure 1. Dendritic nanotubes (DNTs) in dissociated cortical neurons


Friday, October 03, 2025

Parkinson’s ‘trigger’ directly observed in post-mortem human brain tissue for the first time

Good news! Better diagnosis, better treatment!

That this study was only done on post-mortem brain tissue is possibly a critical limitation!

"These tiny clusters, called alpha-synuclein oligomers, have long been considered the likely culprits for Parkinson’s disease to start developing in the brain, but until now, they have evaded direct detection in human brain tissue.

Now, researchers ... have developed an imaging technique that allows them to see, count and compare oligomers in human brain tissue ..."

From the abstract:
"Parkinson’s disease (PD) is a neurodegenerative condition characterized by the presence of intraneuronal aggregates containing fibrillar ɑ-synuclein known as Lewy bodies. These large end-stage species are formed by smaller soluble protein nanoscale assemblies, often termed oligomers, which are proposed as early drivers of pathogenesis.
Until now, this hypothesis has remained controversial, at least in part because it has not been possible to directly visualize nanoscale assemblies in human brain tissue. Here we present Advanced Sensing of Aggregates Parkinson’s Disease, an imaging method to generate large-scale α-synuclein aggregate maps in post-mortem human brain tissue. We combined autofluorescence suppression with single-molecule fluorescence microscopy, which together enable the detection of nanoscale α-synuclein aggregates.
To demonstrate the use of this platform, we analysed ~1.2 million nanoscale aggregates from the anterior cingulate cortex in human post-mortem brain samples from patients with PD and healthy controls.
Our data reveal a disease-specific shift in a subpopulation of nanoscale assemblies that represent an early feature of the proteinopathy that underlies PD. We anticipate that quantitative information about this distribution provided by Advanced Sensing of Aggregates—Parkinson’s Disease will enable mechanistic studies to reveal the pathological processes caused by α-synuclein aggregation."

Parkinson’s ‘trigger’ directly observed in human brain tissue for the first time | University of Cambridge "Scientists have, for the first time, directly visualised and quantified the protein clusters believed to trigger Parkinson’s, marking a major advance in the study of the world’s fastest-growing neurological disease."



Fig. 1: ASA–PD.


Diabetes drug and antihistamine could together repair multiple sclerosis damage, trial finds

Good news! It appears, the results of this study are not yet published in a journal.

"A combination of metformin, a common diabetes drug, and clemastine, an antihistamine, can help repair myelin – the protective coating around nerves, which gets damaged in multiple sclerosis (MS) causing symptoms like fatigue, pain, spasms and problems with walking. ...

Some 70 people with relapsing MS took part in the trials for six months, half of whom took the drug combination and half took a placebo. The primary outcome used to gauge the effectiveness of the drug was a ‘visual evoked potential’ test, which measures how quickly signals travel between the eyes and the brain. The speed of signals slowed down in the placebo group over the course of six months, but remained constant in the drug group. ..."

Diabetes drug and antihistamine could together repair multiple sclerosis damage, trial finds | University of Cambridge "Scientists behind the trial say they are “on the brink of a new class of treatments” and that the findings take us another step closer to stopping disease progression in MS."

Dolphins may develop an Alzheimer’s-type brain disease similar to humans due to climate change? Really!

Did we not know how smart dolphins are since the famous Flipper TV show series of the 1960s?

This could be very interesting! How about e.g. elephants?

I am seriously troubled that the study resorts to climate change as an explanation! This mixup is not helpful! It is muddying the water (pardon my pun)! This could indicate a serious bias on part of the involved scientists.

"Scientists say dolphins may develop an Alzheimer’s-type brain disease similar to humans, which could explain why some are found disoriented, stranded far from home."

From the abstract:
"Climate warming [???] is one factor increasing the severity of harmful algal blooms (HABs). Innovative exposure models are needed to understand how HABs affect brain health. Here, we examined HAB exposure on the brain transcriptome of dolphins found stranded in Florida’s Indian River Lagoon.
We report the neurotoxin 2,4-diaminobutyric acid (2,4-DAB) is 2900 times more concentrated in dolphin brains during bloom seasons compared to non-bloom seasons.
The same dolphins show 536 differentially expressed genes whose enrichment reveal impairment in GABAergic synapses, basement membrane alteration, and Alzheimer’s disease (AD) risk factors that increase with each subsequent season
Dolphins also display concurrent AD-like neuropathological changes and elevated AD gene expression with 2,4-DAB exposure.
Our study demonstrates disproportionate seasonal exposure to 2,4-DAB increases AD signatures in the brain transcriptome.
As our climate warms [???], HABs will continue to intensify. Understanding the impact of HAB exposures will help to identify populations at risk for neurological illnesses."
 
Friday, October 3, 2025 - Join The Flyover




Fig. 5: Alzheimer’s disease-like neuropathological changes in Indian River Lagoon dolphins.


Saturday, September 16, 2023

A long overlooked, Completely New Cause of Alzheimer's and vascular dementia Uncovered

Good news! What else have researchers missed? Pardon my facetiousness!

"... "We've missed a major form of cell death in Alzheimer's disease and vascular dementia," ... "We hadn't been giving much attention to microglia as vulnerable cells, and white matter injury in the brain has received relatively little attention." ...
The researchers discovered that the microglia cells themselves are also destroyed as they sweep away the damaged myelin, seemingly by overdosing on iron that is contained within the white matter in significant quantities. ...
The cascading effect of microglia death and white matter degeneration appears to play a part in the cognitive decline linked to Alzheimer's and vascular dementia, according to the new study  ..."

"... A new study,  ... reveals for the first time that a form of cell death known as ferroptosis — caused by a buildup of iron in cells — destroys microglia cells, a type of cell involved in the brain’s immune response,  in cases of Alzheimer’s and vascular dementia. ...
The researchers discovered that microglia degenerates in the white matter of the brain of patients with Alzheimer’s and vascular dementia. ...
When myelin is damaged, microglia swarm in to clear the debris. In the new study, researchers found that microglia themselves are destroyed by the act of clearing iron-rich myelin — a form of cell death known as ferroptosis. ..."

From the abstract:
"Objective
Because the role of white matter (WM) degenerating microglia (DM) in remyelination failure is unclear, we sought to define the core features of this novel population of aging human microglia.
Methods
We analyzed postmortem human brain tissue to define a population of DM in aging WM lesions. We used immunofluorescence staining and gene expression analysis to investigate molecular mechanisms related to the degeneration of DM.
Results
We found that DM, which accumulated myelin debris were selectively enriched in the iron-binding protein light chain ferritin, and accumulated PLIN2-labeled lipid droplets. DM displayed lipid peroxidation injury and enhanced expression for TOM20, a mitochondrial translocase, and a sensor of oxidative stress. DM also displayed enhanced expression of the DNA fragmentation marker phospho-histone H2A.X. We identified a unique set of ferroptosis-related genes involving iron-mediated lipid dysmetabolism and oxidative stress that were preferentially expressed in WM injury relative to gray matter neurodegeneration.
Interpretation
Ferroptosis appears to be a major mechanism of WM injury in Alzheimer's disease and vascular dementia. WM DM are a novel therapeutic target to potentially reduce the impact of WM injury and myelin loss on the progression of cognitive impairment."

A Completely New Cause of Alzheimer's Uncovered in Our Brain's White Matter : ScienceAlert

OHSU scientists discover new cause of Alzheimer’s, vascular dementia (primary source) Study highlights microglia degeneration in brain caused by iron toxicity


Figure 7 Summary of data supporting a role for ferroptosis in microglial degeneration in human WMI related to vascular dementia or AD. 



Friday, September 01, 2023

A biotech company says it put dopamine-making cells into people’s brains to treat Parkinson's Disease

Good news! This is my second blog post today on new treatments for Parkinson's.

"In an important test for stem-cell medicine, a biotech company says implants of lab-made neurons introduced into the brains of 12 people with Parkinson’s disease appear to be safe and may have reduced symptoms for some of them.

The added cells should produce the neurotransmitter dopamine, a shortage of which is what produces the devastating symptoms of Parkinson’s, including problems moving.  ..."

A biotech company says it put dopamine-making cells into people’s brains | MIT Technology Review The experiment to treat Parkinson’s is a critical early test of stem cells’ potential to tackle serious disease.

Mix of existing medications Alleviates Parkinson's Symptoms In New Study

Good news! Sometimes mixing medications improves symptoms.

"Pharma Two B has developed a once-a-day injection that combines two existing Parkinson’s disease (PD) treatments, pramipexole and rasagiline, at low doses that are not commercially available.
The firm’s recent clinical trial compared the effects of its P2B001 therapy against conventional treatments in over 500 patients over the course of 12 weeks.
It found that the treatment not only significantly improved the motor symptoms and daily function of the patients, but resulted in fewer side effects than other treatments. ..."

Revolutionary Jab Alleviates Parkinson's Symptoms In New Study An Israeli pharma company has found that its jab to alleviate the symptoms of patients with early Parkinson’s disease is more effective than those currently on the market.

Tuesday, August 08, 2023

Study reveals insights into link between genetic mutation and Parkinson’s

Good news! Towards defeating those dreaded neurodegenerative diseases!

"... In a new study, ... researchers reveal new insights into this question, finding that the LRRK2 gene can suppress activity in lysosomes, microscopic organelles that play a key role in breaking down and disposing of cellular waste. ...
LRRK2 genes can also reduce activity of macrophages and microglia, specialized cells that act as the body’s scavengers, clearing away misfolded proteins, cell debris, dead cells, and pathogens, the researchers found. In the brain, microglia help protect neurons from threats posed by these excess materials. ...
The loss of such protective functions as a result of LRRK2 genetic mutations could explain the link between LRRK2 and Parkinson’s disease, the researchers say. Furthermore, outside the brain, the suppression of lysosomes by LRRK2 in macrophages may help explain links between LRRK2 and other diseases including leprosy and Crohn’s disease. ...
“LRRK2 acts like a brake on a garbage truck and if the brake is too strong it limits the ability of these scavenger cells to eliminate damaging material,”  ..."

From the significance and abstract:
"Significance
This study defines a homeostatic mechanism that allows macrophages and microglia to match the degradative activity of their lysosomes to ongoing changes in cellular demand. It shows that the leucine-rich repeat kinase 2 (LRRK2) protein suppresses lysosome degradative activity by inhibiting the expression and nuclear localization of the MiT-TFE family of transcription factors that control the expression of multiple genes that encode lysosome proteins. It further demonstrates that a Parkinson’s disease mutation that hyperactivates LRRK2 kinase activity limits the degradative activity of lysosomes more strongly. These findings support a model wherein LRRK2 protects cells from excessive lysosome degradative activity and suggest that overactivation of this pathway may increase Parkinson’s disease risk by limiting the degradative activity of lysosomes.
Abstract
Cells maintain optimal levels of lysosome degradative activity to protect against pathogens, clear waste, and generate nutrients. Here, we show that LRRK2, a protein that is tightly linked to Parkinson’s disease, negatively regulates lysosome degradative activity in macrophages and microglia via a transcriptional mechanism. Depletion of LRRK2 and inhibition of LRRK2 kinase activity enhanced lysosomal proteolytic activity and increased the expression of multiple lysosomal hydrolases. Conversely, the kinase hyperactive LRRK2 G2019S Parkinson’s disease mutant suppressed lysosomal degradative activity and gene expression. We identified MiT-TFE transcription factors (TFE3, TFEB, and MITF) as mediators of LRRK2-dependent control of lysosomal gene expression. LRRK2 negatively regulated the abundance and nuclear localization of these transcription factors and their depletion prevented LRRK2-dependent changes in lysosome protein levels. These observations define a role for LRRK2 in controlling lysosome degradative activity and support a model wherein LRRK2 hyperactivity may increase Parkinson’s disease risk by suppressing lysosome degradative activity."

Study reveals insights into link between genetic mutation and Parkinson’s | YaleNews In a new study, ... researchers reveal new insights into the role of the LRRK2 gene in triggering the devastating neurodegenerative disease.


Fig. 2 LRRK2 negatively regulates the levels of multiple lysosomal proteins in human iPSC-derived macrophages.



Monday, July 24, 2023

Erroneous genetic sequences identified for the first time in specific cells of ALS and frontotemporal dementia patients

Good news! Are we finally zeroing in on discovering the genetics behind some of the severe neurodegenerative diseases!

Perhaps, there is hope for the senile, demented, and corrupted 46th President (pardon my bad joke)!

"Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are devastating neurodegenerative diseases with mean survival of 2-5 years and 6-8 years, respectively. ...
In some cases, the same genetic mutations occur in both. One of those mutations is a repetitive expansion in the DNA of a gene called C9ORF72. ... One of the significant changes that happens in the majority of cases of ALS and around half of the cases of FTD, is when a protein called TAR DNA binding protein (TDP-43) clumps together and stops working correctly. When TDP-43 doesn’t function properly, it puts incorrect genetic instructions into the RNA, which are called “cryptic exons.”
Now, a team of scientists ... have detected these cryptic exons in specific brain cells from ALS and FTD patients carrying a mutation in the C9ORF72 gene. ..."

From the abstract:
"The C9ORF72-linked diseases amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are characterized by the nuclear depletion and cytoplasmic accumulation of TAR DNA-binding protein 43 (TDP-43). Recent studies have shown that the loss of TDP-43 function leads to the inclusion of cryptic exons (CE) in several RNA transcript targets of TDP-43. Here, we show for the first time the detection of CEs in a single-nuclei RNA sequencing (snRNA-seq) dataset obtained from frontal and occipital cortices of C9ORF72 patients that phenotypically span the ALS-FTD disease spectrum. We assessed each cellular cluster for detection of recently described TDP-43-induced CEs. Transcripts containing CEs in the genes STMN2 and KALRN were detected in the frontal cortex of all C9ORF72 disease groups with the highest frequency in excitatory neurons in the C9ORF72-FTD group. Within the excitatory neurons, the cluster with the highest proportion of cells containing a CE had transcriptomic similarities to von Economo neurons, which are known to be vulnerable to TDP-43 pathology and selectively lost in C9ORF72-FTD. Differential gene expression and pathway analysis of CE-containing neurons revealed multiple dysregulated metabolic processes. Our findings reveal novel insights into the transcriptomic changes of neurons vulnerable to TDP-43 pathology."

Erroneous genetic sequences identified for the first time in specific cells of ALS and frontotemporal dementia patients | AZBio Gene splicing defect known as “cryptic exons” detected using single-nuclei RNA sequencing


Fig. 1 Detection of STMN2 and KALRN cryptic exons in single-nuclei sequencing data from subjects with C9-ALS, C9-ALS-FTD, and C9-FTD.


Friday, July 07, 2023

Tracking Your Tears In Early Test For Alzheimer's And Parkinson's

Good news! Amazing stuff! Confirms one more time that Israel is a hotbed for innovation!

Cry it all out!

"... Early detection is crucial for both diseases, however, as treatments to slow the progression of both are more successful the sooner they are administered. ...
LacriScan diagnosis test uses tears, which are both easily accessible and intrinsically linked to the central nervous system.  
Because of these two factors, “we can identify a component in the tears that reflects processes in the brain, and in the early stages before the patient with Alzheimer’s or Parkinson’s develops clinical symptoms,” ...
The diagnostic process itself is based on the commonly used Schirmer Test that monitors tear production, which involves inserting a paper strip inside the lower eyelid to gather the fluid. 
Once collected, the tears undergo ... patented analysis, looking for biochemical markers ... of the two diseases. The two ailments ... “have a shared identity. ...
... was already working with the use of tears as a diagnosis tool during his research into a rare genetic disorder called NGLY1 deficiency, which has less than 100 cases worldwide, but five instances in the same family in northern Israel. And one of the symptoms of NGLY1 deficiency is alacrima, or abnormal tear production. ” ...
While similar tests for neurological diseases using tears have already been developed, ... that his method differs in two ways: a more sensitive test response and analysis that looks for multiple brain chemical markers of the two diseases. ..."

Tracking Your Tears In Early Test For Alzheimer's And Parkinson's An Israeli researcher has patented a way of using a patient’s tears to diagnose Alzheimer’s and Parkinson’s – the two most common neurodegenerative diseases in the world – in their pre-symptom stages. 

Wednesday, July 05, 2023

Anti-ageing protein klotho injection boosts monkeys’ memories

Here is a business proposition! 😊

"Injecting ageing monkeys with a ‘longevity factor’ protein can improve their cognitive function, a study reveals. ... could lead to new treatments for neurodegenerative diseases.
It is the first time that restoring levels of klotho — a naturally occurring protein that declines in our bodies with age — has been shown to improve cognition in a primate. Previous research on mice had shown that injections of klotho can extend the animals’ lives and increases synaptic plasticity — the capacity to control communication between neurons, at junctions called synapses. ..."

From the abstract:
"Cognitive dysfunction in aging is a major biomedical challenge. Whether treatment with klotho, a longevity factor, could enhance cognition in human-relevant models such as in nonhuman primates is unknown and represents a major knowledge gap in the path to therapeutics. We validated the rhesus form of the klotho protein in mice showing it increased synaptic plasticity and cognition. We then found that a single administration of low-dose, but not high-dose, klotho enhanced memory in aged nonhuman primates. Systemic low-dose klotho treatment may prove therapeutic in aging humans."

Anti-ageing protein injection boosts monkeys’ memories First primate studies to show cognitive benefits of the protein klotho could be a step towards clinical applications.

Tuesday, May 30, 2023

New research shows astrocytes are key to swaying the pendulum in Alzheimer's disease progression

Good news!

"... By testing the blood of more than 1,000 cognitively unimpaired elderly people with and without amyloid pathology, the Pitt-led research team found that only those who had a combination of amyloid burden and blood markers of abnormal astrocyte activation, or reactivity, would progress to symptomatic Alzheimer's in the future, a critical discovery for drug development aimed at halting progression. ...
Inclusion of astrocyte reactivity markers, such as GFAP, in the panel of diagnostic tests will allow for improved selection of patients who are likely to progress to later stages of Alzheimer's and, therefore, help fine-tune selection of candidates for therapeutic interventions who are more likely to benefit. ..."

From the abstract (this one is not easy to interpret):
"An unresolved question for the understanding of Alzheimer’s disease (AD) pathophysiology is why a significant percentage of amyloid-β (Aβ)-positive cognitively unimpaired (CU) individuals do not develop detectable downstream tau pathology and, consequently, clinical deterioration. In vitro evidence suggests that reactive astrocytes unleash Aβ effects in pathological tau phosphorylation. Here, in a biomarker study across three cohorts (n = 1,016), we tested whether astrocyte reactivity modulates the association of Aβ with tau phosphorylation in CU individuals. We found that Aβ was associated with increased plasma phosphorylated tau only in individuals positive for astrocyte reactivity (Ast+). Cross-sectional and longitudinal tau–positron emission tomography analyses revealed an AD-like pattern of tau tangle accumulation as a function of Aβ only in CU Ast+ individuals. Our findings suggest astrocyte reactivity as an important upstream event linking Aβ with initial tau pathology, which may have implications for the biological definition of preclinical AD and for selecting CU individuals for clinical trials."

New research shows astrocytes are key to swaying the pendulum in Alzheimer's disease progression


Fig. 1: Astrocyte reactivity influences Aβ-dependent tau phosphorylation.