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1.
Brain Neurosci Adv ; 8: 23982128241280001, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-39315091

RESUMO

Although neuritic plaques - comprised of aggregated fibrils of the misfolded protein, amyloid ß (Aß) - have formed a central focus of Alzheimer's disease (AD) research for decades, it is now well understood that plaque burden alone is a poor correlate of cognitive decline. This is highlighted especially when compared against other neuropathological hallmarks, such as synapse loss (the strongest correlate) and hyperphosphorylated protein tau. However, it is known that Familial AD arises due to autosomal dominant mutations directly influencing the generation of Aß, suggesting that Aß pathology may play a key upstream role in the disease. Such contrasting lines of evidence have thus raised questions as to why some aged individuals with high plaque burden develop AD while others remain cognitively healthy. In their recent study, published in Analytical Chemistry (June 2024), Enzlein and colleagues aimed to investigate whether differences in the molecular composition of plaques between individuals with sporadic Alzheimer's disease (N = 9) versus age-matched amyloid positive but cognitively unaffected controls (N = 8) could go towards explaining this outstanding question in the field. Using novel methods integrating mass spectrometry imaging with machine learning feature extraction, the authors compared peptide and lipid profiles to a resolving limit of 400 µm2 for >5000 individual plaques. In doing so, a distinct peptide signature was identified in sporadic Alzheimer's disease plaques that was characterised by strongly increased aggregation of the short amyloid ß isoform, Aß1-38 coupled with a lesser co-aggregation of pyroglutamate-modified Aß3-42pE. Sporadic Alzheimer's disease plaques also demonstrated a robust lipid signature denoted by an increased presence of cell membrane components, GM1 and GM2 gangliosides. Here, we review this work; aiming to place these findings within the context of existing literature and with a view to discussing their importance in developing our current knowledge of Alzheimer's disease.

2.
Brain Commun ; 6(5): fcae266, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-39229488

RESUMO

Our editor discusses taking a vacation without a computer and some neuroscience evidence supporting the need for work-life balance.

3.
Neuropathol Appl Neurobiol ; 50(4): e13006, 2024 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-39164997

RESUMO

AIMS: Mutations in the MAPT gene encoding tau protein can cause autosomal dominant neurodegenerative tauopathies including frontotemporal dementia (often with Parkinsonism). In Alzheimer's disease, the most common tauopathy, synapse loss is the strongest pathological correlate of cognitive decline. Recently, Positron Emission Tomography (PET) imaging with synaptic tracers revealed clinically relevant loss of synapses in primary tauopathies; however, the molecular mechanisms leading to synapse degeneration in primary tauopathies remain largely unknown. In this study, we examined post-mortem brain tissue from people who died with frontotemporal dementia with tau pathology (FTDtau) caused by the MAPT intronic exon 10 + 16 mutation, which increases splice variants containing exon 10 resulting in higher levels of tau with four microtubule-binding domains. METHODS: We used RNA sequencing and histopathology to examine temporal cortex and visual cortex, to look for molecular phenotypes compared to age, sex and RNA integrity matched participants who died without neurological disease (n = 12 FTDtau10 + 16 and 13 controls). RESULTS: Bulk tissue RNA sequencing reveals substantial downregulation of gene expression associated with synaptic function. Upregulated biological pathways in human MAPT 10 + 16 brain included those involved in transcriptional regulation, DNA damage response and neuroinflammation. Histopathology confirmed increased pathological tau accumulation in FTDtau10 + 16 cortex as well as a loss of presynaptic protein staining and region-specific increased colocalization of phospho-tau with synapses in temporal cortex. CONCLUSIONS: Our data indicate that synaptic pathology likely contributes to pathogenesis in FTDtau10 + 16 caused by the MAPT 10 + 16 mutation.


Assuntos
Demência Frontotemporal , Mutação , Sinapses , Proteínas tau , Humanos , Proteínas tau/genética , Proteínas tau/metabolismo , Demência Frontotemporal/genética , Demência Frontotemporal/patologia , Masculino , Feminino , Sinapses/patologia , Sinapses/metabolismo , Idoso , Pessoa de Meia-Idade , Expressão Gênica/genética , Encéfalo/patologia , Encéfalo/metabolismo , Tauopatias/genética , Tauopatias/patologia , Tauopatias/metabolismo
4.
Brain Commun ; 6(4): fcae256, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-39130515

RESUMO

Alzheimer's disease is the most common cause of dementia in the elderly, prompting extensive efforts to pinpoint novel therapeutic targets for effective intervention. Among the hallmark features of Alzheimer's disease is the development of neurofibrillary tangles comprised of hyperphosphorylated tau protein, whose progressive spread throughout the brain is associated with neuronal death. Trans-synaptic propagation of tau has been observed in mouse models, and indirect evidence for tau spread via synapses has been observed in human Alzheimer's disease. Halting tau propagation is a promising therapeutic target for Alzheimer's disease; thus, a scalable model system to screen for modifiers of tau spread would be very useful for the field. To this end, we sought to emulate the trans-synaptic spread of human tau in Drosophila melanogaster. Employing the trans-Tango circuit mapping technique, we investigated whether tau spreads between synaptically connected neurons. Immunohistochemistry and confocal imaging were used to look for tau propagation. Examination of hundreds of flies expressing four different human tau constructs in two distinct neuronal populations reveals a robust resistance in Drosophila to the trans-synaptic spread of human tau. This resistance persisted in lines with concurrent expression of amyloid-ß, in lines with global human tau knock-in to provide a template for human tau in downstream neurons, and with manipulations of temperature. These negative data are important for the field as we establish that Drosophila expressing human tau in subsets of neurons are unlikely to be useful to perform screens to find mechanisms to reduce the trans-synaptic spread of tau. The inherent resistance observed in Drosophila may serve as a valuable clue, offering insights into strategies for impeding tau spread in future studies.

5.
Circ Heart Fail ; 17(9): e011358, 2024 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-39206544

RESUMO

BACKGROUND: Cardiogenic shock (CS) can stem from multiple causes and portends poor prognosis. Prior studies have focused on acute myocardial infarction-CS; however, acute decompensated heart failure (ADHF)-CS accounts for most cases. We studied patients suffering ADHF-CS to identify clinical factors, early in their trajectory, associated with a higher probability of successful outcomes. METHODS: Consecutive patients with CS were evaluated (N=1162). We studied patients who developed ADHF-CS at our hospital (N=562). Primary end point was native heart survival (NHS), defined as survival to discharge without receiving advanced HF therapies. Secondary end points were adverse events, survival, major cardiac interventions, and hospital readmissions within 1 year following index hospitalization discharge. Association of clinical data with NHS was analyzed using logistic regression. RESULTS: Overall, 357 (63.5%) patients achieved NHS, 165 (29.2%) died, and 41 (7.3%) were discharged post advanced HF therapies. Of 398 discharged patients (70.8%), 303 (53.9%) were alive at 1 year. Patients with NHS less commonly suffered cardiac arrest, underwent intubation or pulmonary artery catheter placement, or received temporary mechanical circulatory support, had better hemodynamic and echocardiographic profiles, and had a lower vasoactive-inotropic score at shock onset. Bleeding, hemorrhagic stroke, hemolysis in patients with mechanical circulatory support, and acute kidney injury requiring renal replacement therapy were less common compared with patients who died or received advanced HF therapies. After multivariable adjustments, clinical variables associated with NHS likelihood included younger age, history of systemic hypertension, absence of cardiac arrest or acute kidney injury requiring renal replacement therapy, lower pulmonary capillary wedge pressure and vasoactive-inotropic score, and higher tricuspid annular plane systolic excursion at shock onset (all P<0.05). CONCLUSIONS: By studying contemporary patients with ADHF-CS, we identified clinical factors that can inform clinical management and provide future research targets. Right ventricular function, renal function, pulmonary artery catheter placement, and type and timing of temporary mechanical circulatory support warrant further investigation to improve outcomes of this devastating condition.


Assuntos
Insuficiência Cardíaca , Choque Cardiogênico , Humanos , Choque Cardiogênico/terapia , Choque Cardiogênico/mortalidade , Choque Cardiogênico/etiologia , Choque Cardiogênico/fisiopatologia , Masculino , Feminino , Insuficiência Cardíaca/terapia , Insuficiência Cardíaca/fisiopatologia , Insuficiência Cardíaca/complicações , Insuficiência Cardíaca/mortalidade , Idoso , Pessoa de Meia-Idade , Estudos Retrospectivos , Idoso de 80 Anos ou mais , Fatores de Risco , Readmissão do Paciente , Doença Aguda , Resultado do Tratamento , Prognóstico
7.
Sci Transl Med ; 16(754): eadq6489, 2024 Jul 03.
Artigo em Inglês | MEDLINE | ID: mdl-38959325

RESUMO

Nasal delivery of an oligomeric tau antibody loaded into micelles reduces pathology and ameliorates cognition in a mouse model of tauopathy.


Assuntos
Administração Intranasal , Tauopatias , Proteínas tau , Animais , Proteínas tau/metabolismo , Camundongos , Tauopatias/metabolismo , Tauopatias/patologia , Humanos , Modelos Animais de Doenças , Micelas , Nariz , Anticorpos/uso terapêutico , Anticorpos/imunologia
8.
Brain Commun ; 6(4): fcae203, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38961869

RESUMO

Our editor discusses recognition of achievement in translational neuroscience and the wider issues around incentivization of research.

9.
medRxiv ; 2024 Apr 12.
Artigo em Inglês | MEDLINE | ID: mdl-38645146

RESUMO

Mutations in the MAPT gene encoding tau protein can cause autosomal dominant neurodegenerative tauopathies including frontotemporal dementia (often with Parkinsonism). In Alzheimer's disease, the most common tauopathy, synapse loss is the strongest pathological correlate of cognitive decline. Recently, PET imaging with synaptic tracers revealed clinically relevant loss of synapses in primary tauopathies; however, the molecular mechanisms leading to synapse degeneration in primary tauopathies remain largely unknown. In this study, we examined post-mortem brain tissue from people who died with frontotemporal dementia with tau pathology (FTDtau) caused by the MAPT intronic exon 10+16 mutation, which increases splice variants containing exon 10 resulting in higher levels of tau with four microtubule binding domains. We used RNA sequencing and histopathology to examine temporal cortex and visual cortex, to look for molecular phenotypes compared to age, sex, and RNA integrity matched participants who died without neurological disease (n=12 per group). Bulk tissue RNA sequencing reveals substantial downregulation of gene expression associated with synaptic function. Upregulated biological pathways in human MAPT 10+16 brain included those involved in transcriptional regulation, DNA damage response, and neuroinflammation. Histopathology confirmed increased pathological tau accumulation in FTDtau cortex as well as a loss of presynaptic protein staining, and region-specific increased colocalization of phospho-tau with synapses in temporal cortex. Our data indicate that synaptic pathology likely contributes to pathogenesis in FTDtau caused by the MAPT 10+16 mutation.

10.
Brain Commun ; 6(2): fcae029, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38444910

RESUMO

Our editor discusses our editorial board members, who come from eight countries on four continents, and wider issues of the peer review system.

11.
Acta Neuropathol Commun ; 12(1): 22, 2024 Feb 05.
Artigo em Inglês | MEDLINE | ID: mdl-38317196

RESUMO

Deposition of amyloid beta (Aß) into plaques is a major hallmark of Alzheimer's disease (AD). Different amyloid precursor protein (APP) mutations cause early-onset AD by altering the production or aggregation properties of Aß. We recently identified the Uppsala APP mutation (APPUpp), which causes Aß pathology by a triple mechanism: increased ß-secretase and altered α-secretase APP cleavage, leading to increased formation of a unique Aß conformer that rapidly aggregates and deposits in the brain. The aim of this study was to further explore the effects of APPUpp in a transgenic mouse model (tg-UppSwe), expressing human APP with the APPUpp mutation together with the APPSwe mutation. Aß pathology was studied in tg-UppSwe brains at different ages, using ELISA and immunohistochemistry. In vivo PET imaging with three different PET radioligands was conducted in aged tg-UppSwe mice and two other mouse models; tg-ArcSwe and tg-Swe. Finally, glial responses to Aß pathology were studied in cell culture models and mouse brain tissue, using ELISA and immunohistochemistry. Tg-UppSwe mice displayed increased ß-secretase cleavage and suppressed α-secretase cleavage, resulting in AßUpp42 dominated diffuse plaque pathology appearing from the age of 5-6 months. The γ-secretase cleavage was not affected. Contrary to tg-ArcSwe and tg-Swe mice, tg-UppSwe mice were [11C]PiB-PET negative. Antibody-based PET with the 3D6 ligand visualized Aß pathology in all models, whereas the Aß protofibril selective mAb158 ligand did not give any signals in tg-UppSwe mice. Moreover, unlike the other two models, tg-UppSwe mice displayed a very faint glial response to the Aß pathology. The tg-UppSwe mouse model thus recapitulates several pathological features of the Uppsala APP mutation carriers. The presumed unique structural features of AßUpp42 aggregates were found to affect their interaction with anti-Aß antibodies and profoundly modify the Aß-mediated glial response, which may be important aspects to consider for further development of AD therapies.


Assuntos
Doença de Alzheimer , Peptídeos beta-Amiloides , Animais , Humanos , Camundongos , Doença de Alzheimer/patologia , Peptídeos beta-Amiloides/metabolismo , Precursor de Proteína beta-Amiloide/genética , Precursor de Proteína beta-Amiloide/metabolismo , Secretases da Proteína Precursora do Amiloide/metabolismo , Encéfalo/patologia , Modelos Animais de Doenças , Gliose/patologia , Ligantes , Camundongos Transgênicos
12.
Acta Neuropathol ; 147(1): 32, 2024 02 06.
Artigo em Inglês | MEDLINE | ID: mdl-38319380

RESUMO

Synapse loss correlates with cognitive decline in Alzheimer's disease, and soluble oligomeric amyloid beta (Aß) is implicated in synaptic dysfunction and loss. An important knowledge gap is the lack of understanding of how Aß leads to synapse degeneration. In particular, there has been difficulty in determining whether there is a synaptic receptor that binds Aß and mediates toxicity. While many candidates have been observed in model systems, their relevance to human AD brain remains unknown. This is in part due to methodological limitations preventing visualization of Aß binding at individual synapses. To overcome this limitation, we combined two high resolution microscopy techniques: array tomography and Förster resonance energy transfer (FRET) to image over 1 million individual synaptic terminals in temporal cortex from AD (n = 11) and control cases (n = 9). Within presynapses and post-synaptic densities, oligomeric Aß generates a FRET signal with transmembrane protein 97. Further, Aß generates a FRET signal with cellular prion protein, and post-synaptic density 95 within post synapses. Transmembrane protein 97 is also present in a higher proportion of post synapses in Alzheimer's brain compared to controls. We inhibited Aß/transmembrane protein 97 interaction in a mouse model of amyloidopathy by treating with the allosteric modulator CT1812. CT1812 drug concentration correlated negatively with synaptic FRET signal between transmembrane protein 97 and Aß. In human-induced pluripotent stem cell derived neurons, transmembrane protein 97 is present in synapses and colocalizes with Aß when neurons are challenged with human Alzheimer's brain homogenate. Transcriptional changes are induced by Aß including changes in genes involved in neurodegeneration and neuroinflammation. CT1812 treatment of these neurons caused changes in gene sets involved in synaptic function. These data support a role for transmembrane protein 97 in the synaptic binding of Aß in human Alzheimer's disease brain where it may mediate synaptotoxicity.


Assuntos
Doença de Alzheimer , Disfunção Cognitiva , Proteínas de Membrana , Animais , Humanos , Camundongos , Peptídeos beta-Amiloides , Encéfalo , Sinapses , Proteínas de Membrana/metabolismo
13.
Brain Commun ; 6(1): fcad335, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38162908

RESUMO

Our editor invites nominations for the early career researcher paper prize for an article published in Brain Communications in 2023.

14.
Acta Neuropathol ; 147(1): 7, 2024 01 04.
Artigo em Inglês | MEDLINE | ID: mdl-38175261

RESUMO

Tau hyperphosphorylation and aggregation is a common feature of many dementia-causing neurodegenerative diseases. Tau can be phosphorylated at up to 85 different sites, and there is increasing interest in whether tau phosphorylation at specific epitopes, by specific kinases, plays an important role in disease progression. The AMP-activated protein kinase (AMPK)-related enzyme NUAK1 has been identified as a potential mediator of tau pathology, whereby NUAK1-mediated phosphorylation of tau at Ser356 prevents the degradation of tau by the proteasome, further exacerbating tau hyperphosphorylation and accumulation. This study provides a detailed characterisation of the association of p-tau Ser356 with progression of Alzheimer's disease pathology, identifying a Braak stage-dependent increase in p-tau Ser356 protein levels and an almost ubiquitous presence in neurofibrillary tangles. We also demonstrate, using sub-diffraction-limit resolution array tomography imaging, that p-tau Ser356 co-localises with synapses in AD postmortem brain tissue, increasing evidence that this form of tau may play important roles in AD progression. To assess the potential impacts of pharmacological NUAK inhibition in an ex vivo system that retains multiple cell types and brain-relevant neuronal architecture, we treated postnatal mouse organotypic brain slice cultures from wildtype or APP/PS1 littermates with the commercially available NUAK1/2 inhibitor WZ4003. Whilst there were no genotype-specific effects, we found that WZ4003 results in a culture-phase-dependent loss of total tau and p-tau Ser356, which corresponds with a reduction in neuronal and synaptic proteins. By contrast, application of WZ4003 to live human brain slice cultures results in a specific lowering of p-tau Ser356, alongside increased neuronal tubulin protein. This work identifies differential responses of postnatal mouse organotypic brain slice cultures and adult human brain slice cultures to NUAK1 inhibition that will be important to consider in future work developing tau-targeting therapeutics for human disease.


Assuntos
Doença de Alzheimer , Adulto , Humanos , Animais , Camundongos , Encéfalo , Anilidas , Emaranhados Neurofibrilares , Proteínas Quinases , Proteínas Repressoras
15.
Elife ; 122023 12 12.
Artigo em Inglês | MEDLINE | ID: mdl-38085657

RESUMO

Microglial endolysosomal (dys)function is strongly implicated in neurodegenerative disease. Transcriptomic studies show that a microglial state characterised by a set of genes involved in endolysosomal function is induced in both mouse Alzheimer's disease (AD) models and human AD brain, and that the emergence of this state is emphasised in females. Cst7 (encoding cystatin F) is among the most highly upregulated genes in these microglia. However, despite such striking and robust upregulation, the function of Cst7 in neurodegenerative disease is not understood. Here, we crossed Cst7-/- mice with the AppNL-G-F mouse to test the role of Cst7 in a model of amyloid-driven AD. Surprisingly, we found that Cst7 plays a sexually dimorphic role regulating microglia in this model. In females, Cst7-/-AppNL-G-F microglia had greater endolysosomal gene expression, lysosomal burden, and amyloid beta (Aß) burden in vivo and were more phagocytic in vitro. However, in males, Cst7-/-AppNL-G-F microglia were less inflammatory and had a reduction in lysosomal burden but had no change in Aß burden. Overall, our study reveals functional roles for one of the most commonly upregulated genes in microglia across disease models, and the sex-specific profiles of Cst7-/--altered microglial disease phenotypes. More broadly, the findings raise important implications for AD including crucial questions on sexual dimorphism in neurodegenerative disease and the interplay between endolysosomal and inflammatory pathways in AD pathology.


Assuntos
Doença de Alzheimer , Cistatinas , Doenças Neurodegenerativas , Animais , Feminino , Humanos , Masculino , Camundongos , Doença de Alzheimer/metabolismo , Peptídeos beta-Amiloides/genética , Peptídeos beta-Amiloides/metabolismo , Precursor de Proteína beta-Amiloide/metabolismo , Cistatinas/metabolismo , Modelos Animais de Doenças , Camundongos Transgênicos , Microglia/metabolismo , Doenças Neurodegenerativas/patologia
16.
Neurobiol Aging ; 132: 154-174, 2023 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-37837732

RESUMO

Amyloid ß (Aß) accumulation is a hallmark of Alzheimer's disease. In adult Drosophila brains, human Aß overexpression harms climbing and lifespan. It's uncertain whether Aß is intrinsically toxic or activates downstream neurodegeneration pathways. Our study uncovers a novel protective role against Aß toxicity: intra-endoplasmic reticulum (ER) protein accumulation with a focus on laminin and collagen subunits. Despite high Aß, laminin B1 (LanB1) overexpression robustly counters toxicity, suggesting a potential Aß resistance mechanism. Other laminin subunits and collagen IV also alleviate Aß toxicity; combining them with LanB1 augments the effect. Imaging reveals ER retention of LanB1 without altering Aß secretion. LanB1's rescue function operates independently of the IRE1α/XBP1 ER stress response. ER-targeted GFP overexpression also mitigates Aß toxicity, highlighting broader ER protein retention advantages. Proof-of-principle tests in murine hippocampal slices using mouse Lamb1 demonstrate ER retention in transduced cells, indicating a conserved mechanism. Though ER protein retention generally harms, it could paradoxically counter neuronal Aß toxicity, offering a new therapeutic avenue for Alzheimer's disease.


Assuntos
Doença de Alzheimer , Peptídeos beta-Amiloides , Animais , Camundongos , Humanos , Peptídeos beta-Amiloides/toxicidade , Peptídeos beta-Amiloides/metabolismo , Drosophila , Doença de Alzheimer/genética , Doença de Alzheimer/metabolismo , Endorribonucleases/metabolismo , Laminina/metabolismo , Proteínas Serina-Treonina Quinases/metabolismo , Estresse do Retículo Endoplasmático , Retículo Endoplasmático/metabolismo , Colágeno/metabolismo
17.
Brain Commun ; 5(5): fcad220, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-37663129

RESUMO

Two members of our Editorial Board discuss how the proceeds from article processing charges from Brain Communications and our sister journal Brain are put back into the translational neuroscience community.

18.
Brain Neurosci Adv ; 7: 23982128231191046, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-37600228

RESUMO

A key hallmark of Alzheimer's disease (AD) is the accumulation of hyperphosphorylated tau in neurofibrillary tangles. This occurs alongside neuroinflammation and neurodegeneration. Pathological tau propagates through the AD brain in a defined manner, which correlates with neuron and synapse loss and cognitive decline. One proposed mechanism of tau spread is through synaptically connected brain structures. Apolipoprotein E4 (APOE4) genotype is the strongest genetic risk factor for late-onset AD and is associated with increased tau burden. Whether the apolipoprotein E (APOE) genotype influences neurodegeneration via tau spread is currently unknown. Here, we demonstrate that virally expressed human tau (with the P301L mutation) injected into mouse entorhinal cortex at 5-6 months or 15-16 months of age spreads trans-synaptically to the hippocampus by 14 weeks post-injection. Injections of tau in mice expressing human APOE2, APOE3 or APOE4, as well as APOE knock-outs, showed that tau can spread trans-synaptically in all genotypes and that APOE genotype and age do not affect the spread of tau. These data suggest that APOE genotype is not directly linked to synaptic spread of tau in our model, but other mechanisms involving non-cell autonomous manners of tau spread are still possible.

19.
Cell Rep Med ; 4(9): 101175, 2023 09 19.
Artigo em Inglês | MEDLINE | ID: mdl-37652017

RESUMO

Synapse loss correlates with cognitive decline in Alzheimer's disease (AD). Data from mouse models suggests microglia are important for synapse degeneration, but direct human evidence for any glial involvement in synapse removal in human AD remains to be established. Here we observe astrocytes and microglia from human brains contain greater amounts of synaptic protein in AD compared with non-disease controls, and that proximity to amyloid-ß plaques and the APOE4 risk gene exacerbate this effect. In culture, mouse and human astrocytes and primary mouse and human microglia phagocytose AD patient-derived synapses more than synapses from controls. Inhibiting interactions of MFG-E8 rescues the elevated engulfment of AD synapses by astrocytes and microglia without affecting control synapse uptake. Thus, AD promotes increased synapse ingestion by human glial cells at least in part via an MFG-E8 opsonophagocytic mechanism with potential for targeted therapeutic manipulation.


Assuntos
Doença de Alzheimer , Microglia , Animais , Humanos , Camundongos , Astrócitos , Ingestão de Alimentos , Sinapses
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