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  1. Book ; Online: The Role of Glia in Alzheimer's Disease

    Perez-Nievas, Beatriz G. / Serrano-Pozo, Alberto

    2019  

    Keywords Science: general issues ; Neurosciences ; Alzheimer's disease ; amyloid plaques ; Astrocytes ; Cytokines ; glia ; Microglia ; multiphoton microscopy ; Neurofibrillary Tangles ; Neuroinflammation ; positron emission tomography
    Size 1 electronic resource (128 pages)
    Publisher Frontiers Media SA
    Document type Book ; Online
    Note English ; Open Access
    HBZ-ID HT021231470
    ISBN 9782889457649 ; 2889457648
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: Astrocyte adaptation in Alzheimer's disease: a focus on astrocytic P2X7R.

    Beltran-Lobo, Paula / Reid, Matthew J / Jimenez-Sanchez, Maria / Verkhratsky, Alexei / Perez-Nievas, Beatriz G / Noble, Wendy

    Essays in biochemistry

    2023  Volume 67, Issue 1, Page(s) 119–130

    Abstract: Astrocytes are key homeostatic and defensive cells of the central nervous system (CNS). They undertake numerous functions during development and in adulthood to support and protect the brain through finely regulated communication with other cellular ... ...

    Abstract Astrocytes are key homeostatic and defensive cells of the central nervous system (CNS). They undertake numerous functions during development and in adulthood to support and protect the brain through finely regulated communication with other cellular elements of the nervous tissue. In Alzheimer's disease (AD), astrocytes undergo heterogeneous morphological, molecular and functional alterations represented by reactive remodelling, asthenia and loss of function. Reactive astrocytes closely associate with amyloid β (Aβ) plaques and neurofibrillary tangles in advanced AD. The specific contribution of astrocytes to AD could potentially evolve along the disease process and includes alterations in their signalling, interactions with pathological protein aggregates, metabolic and synaptic impairments. In this review, we focus on the purinergic receptor, P2X7R, and discuss the evidence that P2X7R activation contributes to altered astrocyte functions in AD. Expression of P2X7R is increased in AD brain relative to non-demented controls, and animal studies have shown that P2X7R antagonism improves cognitive and synaptic impairments in models of amyloidosis and tauopathy. While P2X7R activation can induce inflammatory signalling pathways, particularly in microglia, we focus here specifically on the contributions of astrocytic P2X7R to synaptic changes and protein aggregate clearance in AD, highlighting cell-specific roles of this purinoceptor activation that could be targeted to slow disease progression.
    MeSH term(s) Animals ; Alzheimer Disease/metabolism ; Astrocytes/metabolism ; Astrocytes/pathology ; Amyloid beta-Peptides/metabolism ; Brain/metabolism ; Signal Transduction
    Chemical Substances Amyloid beta-Peptides
    Language English
    Publishing date 2023-01-18
    Publishing country England
    Document type Review ; Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1744-1358 ; 0071-1365
    ISSN (online) 1744-1358
    ISSN 0071-1365
    DOI 10.1042/EBC20220079
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Editorial: The Role of Glia in Alzheimer's Disease.

    Pérez-Nievas, Beatriz G / Serrano-Pozo, Alberto

    Frontiers in neurology

    2019  Volume 9, Page(s) 1161

    Language English
    Publishing date 2019-01-11
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2564214-5
    ISSN 1664-2295
    ISSN 1664-2295
    DOI 10.3389/fneur.2018.01161
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Deciphering the Astrocyte Reaction in Alzheimer's Disease.

    Perez-Nievas, Beatriz G / Serrano-Pozo, Alberto

    Frontiers in aging neuroscience

    2018  Volume 10, Page(s) 114

    Abstract: Reactive astrocytes were identified as a component ... ...

    Abstract Reactive astrocytes were identified as a component of
    Language English
    Publishing date 2018-04-25
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2558898-9
    ISSN 1663-4365
    ISSN 1663-4365
    DOI 10.3389/fnagi.2018.00114
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Reactive astrocytes secrete the chaperone HSPB1 to mediate neuroprotection.

    Yang, Fangjia / Beltran-Lobo, Paula / Sung, Katherine / Goldrick, Caoimhe / Croft, Cara L / Nishimura, Agnes / Hedges, Erin / Mahiddine, Farah / Troakes, Claire / Golde, Todd E / Perez-Nievas, Beatriz G / Hanger, Diane P / Noble, Wendy / Jimenez-Sanchez, Maria

    Science advances

    2024  Volume 10, Issue 12, Page(s) eadk9884

    Abstract: Molecular chaperones are protective in neurodegenerative diseases by preventing protein misfolding and aggregation, such as extracellular amyloid plaques and intracellular tau neurofibrillary tangles in Alzheimer's disease (AD). In addition, AD is ... ...

    Abstract Molecular chaperones are protective in neurodegenerative diseases by preventing protein misfolding and aggregation, such as extracellular amyloid plaques and intracellular tau neurofibrillary tangles in Alzheimer's disease (AD). In addition, AD is characterized by an increase in astrocyte reactivity. The chaperone HSPB1 has been proposed as a marker for reactive astrocytes; however, its astrocytic functions in neurodegeneration remain to be elucidated. Here, we identify that HSPB1 is secreted from astrocytes to exert non-cell-autonomous protective functions. We show that in human AD brain, HSPB1 levels increase in astrocytes that cluster around amyloid plaques, as well as in the adjacent extracellular space. Moreover, in conditions that mimic an inflammatory reactive response, astrocytes increase HSPB1 secretion. Concomitantly, astrocytes and neurons can uptake astrocyte-secreted HSPB1, which is accompanied by an attenuation of the inflammatory response in reactive astrocytes and reduced pathological tau inclusions. Our findings highlight a protective mechanism in disease conditions that encompasses the secretion of a chaperone typically regarded as intracellular.
    MeSH term(s) Humans ; Astrocytes/metabolism ; tau Proteins/metabolism ; Plaque, Amyloid/pathology ; Neuroprotection ; Molecular Chaperones/metabolism ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Heat-Shock Proteins/metabolism
    Chemical Substances tau Proteins ; Molecular Chaperones ; Amyloid beta-Peptides ; HSPB1 protein, human ; Heat-Shock Proteins
    Language English
    Publishing date 2024-03-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.adk9884
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Considerations for future tau-targeted therapeutics: can they deliver?

    Noble, Wendy / Jimenez-Sanchez, Maria / Perez-Nievas, Beatriz G / Hanger, Diane P

    Expert opinion on drug discovery

    2019  Volume 15, Issue 3, Page(s) 265–267

    MeSH term(s) Alzheimer Disease/drug therapy ; Alzheimer Disease/physiopathology ; Animals ; Drug Development ; Humans ; Tauopathies/drug therapy ; Tauopathies/physiopathology ; tau Proteins/metabolism
    Chemical Substances tau Proteins
    Language English
    Publishing date 2019-10-29
    Publishing country England
    Document type Editorial
    ZDB-ID 2259618-5
    ISSN 1746-045X ; 1746-0441
    ISSN (online) 1746-045X
    ISSN 1746-0441
    DOI 10.1080/17460441.2020.1685977
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6388: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: P2X

    Beltran-Lobo, Paula / Hughes, Martina M / Troakes, Claire / Croft, Cara L / Rupawala, Huzefa / Jutzi, Daniel / Ruepp, Marc-David / Jimenez-Sanchez, Maria / Perkinton, Michael S / Kassiou, Michael / Golde, Todd E / Hanger, Diane P / Verkhratsky, Alexei / Perez-Nievas, Beatriz G / Noble, Wendy

    Brain, behavior, and immunity

    2023  Volume 114, Page(s) 414–429

    Abstract: The purinoceptor ... ...

    Abstract The purinoceptor P2X
    MeSH term(s) Animals ; Humans ; Mice ; Alzheimer Disease/metabolism ; Astrocytes/metabolism ; Brain/metabolism ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/pathology ; Microglia/metabolism ; RNA, Messenger/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism ; Tauopathies/metabolism
    Chemical Substances RNA, Messenger ; tau Proteins ; P2RX7 protein, human ; MAPT protein, human
    Language English
    Publishing date 2023-09-15
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639219-2
    ISSN 1090-2139 ; 0889-1591
    ISSN (online) 1090-2139
    ISSN 0889-1591
    DOI 10.1016/j.bbi.2023.09.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2276: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 327: Show issues

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  8. Article ; Online: Astrocytic C-X-C motif chemokine ligand-1 mediates β-amyloid-induced synaptotoxicity.

    Perez-Nievas, Beatriz G / Johnson, Louisa / Beltran-Lobo, Paula / Hughes, Martina M / Gammallieri, Luciana / Tarsitano, Francesca / Myszczynska, Monika A / Vazquez-Villasenor, Irina / Jimenez-Sanchez, Maria / Troakes, Claire / Wharton, Stephen B / Ferraiuolo, Laura / Noble, Wendy

    Journal of neuroinflammation

    2021  Volume 18, Issue 1, Page(s) 306

    Abstract: Background: Pathological interactions between β-amyloid (Aβ) and tau drive synapse loss and cognitive decline in Alzheimer's disease (AD). Reactive astrocytes, displaying altered functions, are also a prominent feature of AD brain. This large and ... ...

    Abstract Background: Pathological interactions between β-amyloid (Aβ) and tau drive synapse loss and cognitive decline in Alzheimer's disease (AD). Reactive astrocytes, displaying altered functions, are also a prominent feature of AD brain. This large and heterogeneous population of cells are increasingly recognised as contributing to early phases of disease. However, the contribution of astrocytes to Aβ-induced synaptotoxicity in AD is not well understood.
    Methods: We stimulated mouse and human astrocytes with conditioned medium containing concentrations and species of human Aβ that mimic those in human AD brain. Medium from stimulated astrocytes was collected and immunodepleted of Aβ before being added to naïve rodent or human neuron cultures. A cytokine, identified in unbiased screens of stimulated astrocyte media and in postmortem human AD brain lysates was also applied to neurons, including those pre-treated with a chemokine receptor antagonist. Tau mislocalisation, synaptic markers and dendritic spine numbers were measured in cultured neurons and organotypic brain slice cultures.
    Results: We found that conditioned medium from stimulated astrocytes induces exaggerated synaptotoxicity that is recapitulated following spiking of neuron culture medium with recombinant C-X-C motif chemokine ligand-1 (CXCL1), a chemokine upregulated in AD brain. Antagonism of neuronal C-X-C motif chemokine receptor 2 (CXCR2) prevented synaptotoxicity in response to CXCL1 and Aβ-stimulated astrocyte secretions.
    Conclusions: Our data indicate that astrocytes exacerbate the synaptotoxic effects of Aβ via interactions of astrocytic CXCL1 and neuronal CXCR2 receptors, highlighting this chemokine-receptor pair as a novel target for therapeutic intervention in AD.
    MeSH term(s) Adult ; Aged ; Aged, 80 and over ; Alzheimer Disease/genetics ; Amyloid beta-Peptides/toxicity ; Animals ; Astrocytes/pathology ; Cells, Cultured ; Chemokine CXCL1/antagonists & inhibitors ; Chemokine CXCL1/chemistry ; Culture Media, Conditioned ; Dendritic Spines/pathology ; Female ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Middle Aged ; Neurons/drug effects ; Receptors, Interleukin-8B/antagonists & inhibitors ; Synapses/pathology ; tau Proteins/chemistry ; tau Proteins/toxicity
    Chemical Substances Amyloid beta-Peptides ; CXCL1 protein, human ; CXCR2 protein, human ; Chemokine CXCL1 ; Culture Media, Conditioned ; MAPT protein, human ; Receptors, Interleukin-8B ; tau Proteins
    Language English
    Publishing date 2021-12-28
    Publishing country England
    Document type Journal Article
    ZDB-ID 2156455-3
    ISSN 1742-2094 ; 1742-2094
    ISSN (online) 1742-2094
    ISSN 1742-2094
    DOI 10.1186/s12974-021-02371-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Bridging Integrator-1 protein loss in Alzheimer's disease promotes synaptic tau accumulation and disrupts tau release.

    Glennon, Elizabeth B / Lau, Dawn H-W / Gabriele, Rebecca M C / Taylor, Matthew F / Troakes, Claire / Opie-Martin, Sarah / Elliott, Christina / Killick, Richard / Hanger, Diane P / Perez-Nievas, Beatriz G / Noble, Wendy

    Brain communications

    2020  Volume 2, Issue 1

    Abstract: Polymorphisms associated ... ...

    Abstract Polymorphisms associated with
    Language English
    Publishing date 2020-02-14
    Publishing country England
    Document type Journal Article
    ISSN 2632-1297
    ISSN (online) 2632-1297
    DOI 10.1093/braincomms/fcaa011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Isoform-selective decrease of glycogen synthase kinase-3-beta (GSK-3β) reduces synaptic tau phosphorylation, transcellular spreading, and aggregation.

    Amaral, Ana Claudia / Perez-Nievas, Beatriz G / Siao Tick Chong, Michael / Gonzalez-Martinez, Alicia / Argente-Escrig, Herminia / Rubio-Guerra, Sara / Commins, Caitlin / Muftu, Serra / Eftekharzadeh, Bahareh / Hudry, Eloise / Fan, Zhanyun / Ramanan, Prianca / Takeda, Shuko / Frosch, Matthew P / Wegmann, Susanne / Gomez-Isla, Teresa

    iScience

    2021  Volume 24, Issue 2, Page(s) 102058

    Abstract: It has been suggested that aberrant activation of glycogen synthase kinase-3-beta (GSK-3β) can trigger abnormal tau hyperphosphorylation and aggregation, which ultimately leads to neuronal/synaptic damage and impaired cognition in Alzheimer disease (AD). ...

    Abstract It has been suggested that aberrant activation of glycogen synthase kinase-3-beta (GSK-3β) can trigger abnormal tau hyperphosphorylation and aggregation, which ultimately leads to neuronal/synaptic damage and impaired cognition in Alzheimer disease (AD). We examined if isoform-selective partial reduction of GSK-3β can decrease pathological tau changes, including hyperphosphorylation, aggregation, and spreading, in mice with localized human wild-type tau (hTau) expression in the brain. We used adeno-associated viruses (AAVs) to express hTau locally in the entorhinal cortex of wild-type and GSK-3β hemi-knockout (GSK-3β-HK) mice. GSK-3β-HK mice had significantly less accumulation of hyperphosphorylated tau in synapses and showed a significant decrease of tau protein spread between neurons. In primary neuronal cultures from GSK-3β-HK mice, the aggregation of exogenous FTD-mutant tau was also significantly reduced. These results show that a partial decrease of GSK-3β significantly represses tau-initiated neurodegenerative changes in the brain, and therefore is a promising therapeutic target for AD and other tauopathies.
    Language English
    Publishing date 2021-01-13
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2021.102058
    Database MEDical Literature Analysis and Retrieval System OnLINE

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