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  1. Article: Aging, Metabolism, Synaptic Activity, and Aβ in Alzheimer's Disease.

    Gouras, Gunnar K

    Frontiers in aging neuroscience

    2019  Volume 11, Page(s) 185

    Language English
    Publishing date 2019-07-23
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2558898-9
    ISSN 1663-4365
    ISSN 1663-4365
    DOI 10.3389/fnagi.2019.00185
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  2. Article ; Online: Correction: Lesion of the subiculum reduces the spread of amyloid beta pathology to interconnected brain regions in a mouse model of Alzheimer's disease.

    George, Sonia / Rönnbäck, Annica / Gouras, Gunnar K / Petit, Géraldine H / Grueninger, Fiona / Winblad, Bengt / Graff, Caroline / Brundin, Patrik

    Acta neuropathologica communications

    2024  Volume 12, Issue 1, Page(s) 26

    Language English
    Publishing date 2024-02-14
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2715589-4
    ISSN 2051-5960 ; 2051-5960
    ISSN (online) 2051-5960
    ISSN 2051-5960
    DOI 10.1186/s40478-023-01712-9
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  3. Article: Astrocytic and Neuronal Apolipoprotein E Isoforms Differentially Affect Neuronal Excitability.

    Konings, Sabine C / Torres-Garcia, Laura / Martinsson, Isak / Gouras, Gunnar K

    Frontiers in neuroscience

    2021  Volume 15, Page(s) 734001

    Abstract: Synaptic changes and neuronal network dysfunction are among the earliest changes in Alzheimer's disease (AD). Apolipoprotein E4 (ApoE4), the major genetic risk factor in AD, has been shown to be present at synapses and to induce hyperexcitability in ... ...

    Abstract Synaptic changes and neuronal network dysfunction are among the earliest changes in Alzheimer's disease (AD). Apolipoprotein E4 (ApoE4), the major genetic risk factor in AD, has been shown to be present at synapses and to induce hyperexcitability in mouse knock-in brain regions vulnerable to AD. ApoE in the brain is mainly generated by astrocytes, however, neurons can also produce ApoE under stress conditions such as aging. The potential synaptic function(s) of ApoE and whether the cellular source of ApoE might affect neuronal excitability remain poorly understood. Therefore, the aim of this study was to elucidate the synaptic localization and effects on neuronal activity of the two main human ApoE isoforms from different cellular sources in control and AD-like
    Language English
    Publishing date 2021-09-21
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2411902-7
    ISSN 1662-453X ; 1662-4548
    ISSN (online) 1662-453X
    ISSN 1662-4548
    DOI 10.3389/fnins.2021.734001
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  4. Article ; Online: Cerebral Aβ deposition precedes reduced cerebrospinal fluid and serum Aβ42/Aβ40 ratios in the App

    Andersson, Emelie / Schultz, Nina / Saito, Takashi / Saido, Takaomi C / Blennow, Kaj / Gouras, Gunnar K / Zetterberg, Henrik / Hansson, Oskar

    Alzheimer's research & therapy

    2023  Volume 15, Issue 1, Page(s) 64

    Abstract: Background: Aβ42/Aβ40 ratios in cerebrospinal fluid (CSF) and blood are reduced in preclinical Alzheimer's disease (AD), but their temporal and correlative relationship with cerebral Aβ pathology at this early disease stage is not well understood. In ... ...

    Abstract Background: Aβ42/Aβ40 ratios in cerebrospinal fluid (CSF) and blood are reduced in preclinical Alzheimer's disease (AD), but their temporal and correlative relationship with cerebral Aβ pathology at this early disease stage is not well understood. In the present study, we aim to investigate such relationships using App knock-in mouse models of preclinical AD.
    Methods: CSF, serum, and brain tissue were collected from 3- to 18-month-old App
    Results: In App
    Conclusions: Our findings suggest a temporal sequence of events in App
    MeSH term(s) Humans ; Mice ; Animals ; Alzheimer Disease/cerebrospinal fluid ; Mobile Applications ; Amyloid beta-Peptides/cerebrospinal fluid ; Peptide Fragments/cerebrospinal fluid ; Plaque, Amyloid/pathology ; Biomarkers/cerebrospinal fluid
    Chemical Substances amyloid beta-protein (1-42) ; Amyloid beta-Peptides ; Peptide Fragments ; Biomarkers
    Language English
    Publishing date 2023-03-25
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2506521-X
    ISSN 1758-9193 ; 1758-9193
    ISSN (online) 1758-9193
    ISSN 1758-9193
    DOI 10.1186/s13195-023-01196-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Sphingosine 1-Phoshpate Receptors are Located in Synapses and Control Spontaneous Activity of Mouse Neurons in Culture.

    Skoug, Cecilia / Martinsson, Isak / Gouras, Gunnar K / Meissner, Anja / Duarte, João M N

    Neurochemical research

    2022  Volume 47, Issue 10, Page(s) 3114–3125

    Abstract: Sphingosine-1-phosphate (S1P) is best known for its roles as vascular and immune regulator. Besides, it is also present in the central nervous system (CNS) where it can act as neuromodulator via five S1P receptors (S1PRs), and thus control ... ...

    Abstract Sphingosine-1-phosphate (S1P) is best known for its roles as vascular and immune regulator. Besides, it is also present in the central nervous system (CNS) where it can act as neuromodulator via five S1P receptors (S1PRs), and thus control neurotransmitter release. The distribution of S1PRs in the active zone and postsynaptic density of CNS synapses remains unknown. In the current study, we investigated the localization of S1PR1-5 in synapses of the mouse cortex. Cortical nerve terminals purified in a sucrose gradient were endowed with all five S1PRs. Further subcellular fractionation of cortical nerve terminals revealed S1PR2 and S1PR4 immunoreactivity in the active zone of presynaptic nerve terminals. Interestingly, only S1PR2 and S1PR3 immunoreactivity was found in the postsynaptic density. All receptors were present outside the active zone of nerve terminals. Neurons in the mouse cortex and primary neurons in culture showed immunoreactivity against all five S1PRs, and Ca
    MeSH term(s) Animals ; Lysophospholipids ; Mice ; Neurons ; Receptors, Lysosphingolipid ; Sphingosine/analogs & derivatives ; Synapses
    Chemical Substances Lysophospholipids ; Receptors, Lysosphingolipid ; sphingosine 1-phosphate (26993-30-6) ; Sphingosine (NGZ37HRE42)
    Language English
    Publishing date 2022-07-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 199335-5
    ISSN 1573-6903 ; 0364-3190
    ISSN (online) 1573-6903
    ISSN 0364-3190
    DOI 10.1007/s11064-022-03664-3
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1368: Show issues Location:
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  6. Article ; Online: Apolipoprotein E intersects with amyloid-β within neurons.

    Konings, Sabine C / Nyberg, Emma / Martinsson, Isak / Torres-Garcia, Laura / Klementieva, Oxana / Guimas Almeida, Claudia / Gouras, Gunnar K

    Life science alliance

    2023  Volume 6, Issue 8

    Abstract: Apolipoprotein E4 (ApoE4) is the most important genetic risk factor for Alzheimer's disease (AD). Among the earliest changes in AD is endosomal enlargement in neurons, which was reported as enhanced in ApoE4 carriers. ApoE is thought to be internalized ... ...

    Abstract Apolipoprotein E4 (ApoE4) is the most important genetic risk factor for Alzheimer's disease (AD). Among the earliest changes in AD is endosomal enlargement in neurons, which was reported as enhanced in ApoE4 carriers. ApoE is thought to be internalized into endosomes of neurons, whereas β-amyloid (Aβ) accumulates within neuronal endosomes early in AD. However, it remains unknown whether ApoE and Aβ intersect intracellularly. We show that internalized astrocytic ApoE localizes mostly to lysosomes in neuroblastoma cells and astrocytes, whereas in neurons, it preferentially localizes to endosomes-autophagosomes of neurites. In AD transgenic neurons, astrocyte-derived ApoE intersects intracellularly with amyloid precursor protein/Aβ. Moreover, ApoE4 increases the levels of endogenous and internalized Aβ
    MeSH term(s) Humans ; Amyloid beta-Protein Precursor/genetics ; Apolipoprotein E4/genetics ; Apolipoproteins E/genetics ; Amyloid beta-Peptides/genetics ; Alzheimer Disease/genetics ; Neurons/physiology
    Chemical Substances Amyloid beta-Protein Precursor ; Apolipoprotein E4 ; Apolipoproteins E ; Amyloid beta-Peptides
    Language English
    Publishing date 2023-06-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2575-1077
    ISSN (online) 2575-1077
    DOI 10.26508/lsa.202201887
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  7. Article ; Online: mTOR: at the crossroads of aging, chaperones, and Alzheimer's disease.

    Gouras, Gunnar K

    Journal of neurochemistry

    2013  Volume 124, Issue 6, Page(s) 747–748

    MeSH term(s) Aged ; Aging/genetics ; Aging/metabolism ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Animals ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Signal Transduction/physiology ; TOR Serine-Threonine Kinases/genetics ; TOR Serine-Threonine Kinases/metabolism
    Chemical Substances Molecular Chaperones ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1)
    Language English
    Publishing date 2013-03
    Publishing country England
    Document type Editorial
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/jnc.12098
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    In stock of ZB MED Cologne/Königswinter

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  8. Article: Convergence of synapses, endosomes, and prions in the biology of neurodegenerative diseases.

    Gouras, Gunnar K

    International journal of cell biology

    2013  Volume 2013, Page(s) 141083

    Abstract: Age-related misfolding and aggregation of disease-linked proteins in selective brain regions is a characteristic of neurodegenerative diseases. Although neuropathological aggregates that characterize these various diseases are found at sites other than ... ...

    Abstract Age-related misfolding and aggregation of disease-linked proteins in selective brain regions is a characteristic of neurodegenerative diseases. Although neuropathological aggregates that characterize these various diseases are found at sites other than synapses, increasing evidence supports the idea that synapses are where the pathogenesis begins. Understanding these diseases is hampered by our lack of knowledge of what the normal functions of these proteins are and how they are affected by aging. Evidence has supported the idea that neurodegenerative disease-linked proteins have a common propensity for prion protein-like cell-to-cell propagation. However, it is not thought that the prion-like quality of these proteins/peptides that allows their cell-to-cell transmission implies a role for human-to-human spread in common age-related neurodegenerative diseases. It will be important to better understand the molecular and cellular mechanisms governing the role of these aggregating proteins in neural function, especially at synapses, how their propagation occurs and how pathogenesis is promoted by aging.
    Language English
    Publishing date 2013-11-07
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2536742-0
    ISSN 1687-8884 ; 1687-8876
    ISSN (online) 1687-8884
    ISSN 1687-8876
    DOI 10.1155/2013/141083
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  9. Article ; Online: Neuronal α-amylase is important for neuronal activity and glycogenolysis and reduces in presence of amyloid beta pathology.

    Byman, Elin / Martinsson, Isak / Haukedal, Henriette / Gouras, Gunnar / Freude, Kristine K / Wennström, Malin

    Aging cell

    2021  Volume 20, Issue 8, Page(s) e13433

    Abstract: Recent studies indicate a crucial role for neuronal glycogen storage and degradation in memory formation. We have previously identified alpha-amylase (α-amylase), a glycogen degradation enzyme, located within synaptic-like structures in CA1 pyramidal ... ...

    Abstract Recent studies indicate a crucial role for neuronal glycogen storage and degradation in memory formation. We have previously identified alpha-amylase (α-amylase), a glycogen degradation enzyme, located within synaptic-like structures in CA1 pyramidal neurons and shown that individuals with a high copy number variation of α-amylase perform better on the episodic memory test. We reported that neuronal α-amylase was absent in patients with Alzheimer's disease (AD) and that this loss corresponded to increased AD pathology. In the current study, we verified these findings in a larger patient cohort and determined a similar reduction in α-amylase immunoreactivity in the molecular layer of hippocampus in AD patients. Next, we demonstrated reduced α-amylase concentrations in oligomer amyloid beta 42 (Aβ
    MeSH term(s) Alzheimer Disease/physiopathology ; Amyloid beta-Peptides/metabolism ; Animals ; Glycogenolysis/genetics ; Humans ; Male ; Mice ; alpha-Amylases/metabolism
    Chemical Substances Amyloid beta-Peptides ; alpha-Amylases (EC 3.2.1.1)
    Language English
    Publishing date 2021-07-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2113083-8
    ISSN 1474-9726 ; 1474-9718
    ISSN (online) 1474-9726
    ISSN 1474-9718
    DOI 10.1111/acel.13433
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    Zs.A 6581: Show issues Location:
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  10. Article ; Online: Upregulation of APP endocytosis by neuronal aging drives amyloid-dependent synapse loss.

    Burrinha, Tatiana / Martinsson, Isak / Gomes, Ricardo / Terrasso, Ana Paula / Gouras, Gunnar K / Almeida, Cláudia Guimas

    Journal of cell science

    2021  Volume 134, Issue 9

    Abstract: Neuronal aging increases the risk of late-onset Alzheimer's disease. During normal aging, synapses decline, and β-amyloid (Aβ) accumulates intraneuronally. However, little is known about the underlying cell biological mechanisms. We studied neuronal ... ...

    Abstract Neuronal aging increases the risk of late-onset Alzheimer's disease. During normal aging, synapses decline, and β-amyloid (Aβ) accumulates intraneuronally. However, little is known about the underlying cell biological mechanisms. We studied neuronal aging using normal-aged brain and aged mouse primary neurons that accumulate lysosomal lipofuscin and show synapse loss. We identified the upregulation of amyloid precursor protein (APP) endocytosis as a neuronal aging mechanism that potentiates APP processing and Aβ production in vitro and in vivo. The increased APP endocytosis may contribute to the early endosome enlargement observed in the aged brain. Mechanistically, we showed that clathrin-dependent APP endocytosis requires F-actin and that clathrin and endocytic F-actin increase with neuronal aging. Finally, Aβ production inhibition reverts synaptic decline in aged neurons, whereas Aβ accumulation, promoted by endocytosis upregulation in younger neurons, recapitulates aging-related synapse decline. Overall, we identify APP endocytosis upregulation as a potential mechanism of neuronal aging and, thus, a novel target to prevent late-onset Alzheimer's disease. This article has an associated First Person interview with the first author of the paper.
    MeSH term(s) Aging ; Alzheimer Disease/genetics ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Endocytosis ; Mice ; Neurons/metabolism ; Synapses/metabolism ; Up-Regulation
    Chemical Substances Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
    Language English
    Publishing date 2021-05-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.255752
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