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  1. Book ; Online ; Thesis: Die Rolle von Neuregulin 1 in der Charcot-Marie-Tooth Erkrankung 1B (CMT1B)

    Krüger, Janina [Verfasser] / Gericke, Martin [Gutachter] / Roßner, Steffen [Gutachter]

    2024  

    Author's details Janina Krüger ; Gutachter: Martin Gericke, Steffen Roßner
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Universitätsbibliothek Leipzig
    Publishing place Leipzig
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  2. Article ; Online: Natural Products from Plants and Algae for Treatment of Alzheimer's Disease: A Review.

    Klose, Jana / Griehl, Carola / Roßner, Steffen / Schilling, Stephan

    Biomolecules

    2022  Volume 12, Issue 5

    Abstract: Neurodegenerative disorders including Parkinson's disease (PD), Huntington's disease (HD) and the most frequent, Alzheimer's disease (AD), represent one of the most urgent medical needs worldwide. Despite a significantly developed understanding of ... ...

    Abstract Neurodegenerative disorders including Parkinson's disease (PD), Huntington's disease (HD) and the most frequent, Alzheimer's disease (AD), represent one of the most urgent medical needs worldwide. Despite a significantly developed understanding of disease development and pathology, treatments that stop AD progression are not yet available. The recent approval of sodium oligomannate (GV-971) for AD treatment in China emphasized the potential value of natural products for the treatment of neurodegenerative disorders. Many current clinical studies include the administration of a natural compound as a single and combination treatment. The most prominent mechanisms of action are anti-inflammatory and anti-oxidative activities, thus preserving cellular survival. Here, we review current natural products that are either approved or are in testing for a treatment of neurodegeneration in AD. In addition to the most important compounds of plant origin, we also put special emphasis on compounds from algae, given their neuroprotective activity and their underlying mechanisms of neuroprotection.
    MeSH term(s) Alzheimer Disease/drug therapy ; Alzheimer Disease/pathology ; Biological Products/pharmacology ; Biological Products/therapeutic use ; Humans ; Huntington Disease ; Neurodegenerative Diseases/drug therapy ; Parkinson Disease/drug therapy
    Chemical Substances Biological Products
    Language English
    Publishing date 2022-05-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom12050694
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Tricellulin, α-Catenin and Microfibrillar-Associated Protein 5 Exhibit Concomitantly Altered Immunosignals along with Vascular, Extracellular and Cytoskeletal Elements after Experimental Focal Cerebral Ischemia.

    Höfling, Corinna / Roßner, Steffen / Flachmeyer, Bianca / Krueger, Martin / Härtig, Wolfgang / Michalski, Dominik

    International journal of molecular sciences

    2023  Volume 24, Issue 15

    Abstract: Along with initiatives to understand the pathophysiology of stroke in detail and to identify neuroprotective targets, cell-stabilizing elements have gained increasing attention. Although cell culture experiments have indicated that tricellulin, α-catenin ...

    Abstract Along with initiatives to understand the pathophysiology of stroke in detail and to identify neuroprotective targets, cell-stabilizing elements have gained increasing attention. Although cell culture experiments have indicated that tricellulin, α-catenin and microfibrillar-associated protein 5 (MFAP5) contribute to cellular integrity, these elements have not yet been investigated in the ischemic brain. Applying immunofluorescence labeling, this study explored tricellulin, MFAP5 and α-catenin in non-ischemic and ischemic brain areas of mice (24, 4 h of ischemia) and rats (4 h of ischemia), along with collagen IV and fibronectin as vascular and extracellular matrix constituents and microtubule-associated protein 2 (MAP2) and neurofilament light chain (NF-L) as cytoskeletal elements. Immunosignals of tricellulin and notably MFAP5 partially appeared in a fiber-like pattern, and α-catenin appeared more in a dotted pattern. Regional associations with vascular and extracellular constituents were found for tricellulin and α-catenin, particularly in ischemic areas. Due to ischemia, signals of tricellulin, MFAP5 and α-catenin decreased concomitantly with MAP2 and NF-L, whereby MFAP5 provided the most sensitive reaction. For the first time, this study demonstrated ischemia-related alterations in tricellulin, MFAP5 and α-catenin along with the vasculature, extracellular matrix and cytoskeleton. Confirmatory studies are needed, also exploring their role in cellular integrity and the potential for neuroprotective approaches in stroke.
    MeSH term(s) Animals ; Mice ; Rats ; alpha Catenin ; Brain Ischemia/metabolism ; Cerebral Infarction ; Cytoskeleton/metabolism ; Ischemia ; MARVEL Domain Containing 2 Protein ; Stroke/metabolism ; Intercellular Signaling Peptides and Proteins ; Contractile Proteins
    Chemical Substances alpha Catenin ; MARVEL Domain Containing 2 Protein ; Marveld2 protein, mouse ; Intercellular Signaling Peptides and Proteins ; Contractile Proteins
    Language English
    Publishing date 2023-07-25
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241511893
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Gender, GABAergic dysfunction and AD.

    Alia, A / Roßner, Steffen

    Aging

    2018  Volume 10, Issue 12, Page(s) 3636–3637

    MeSH term(s) Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/physiopathology ; Alzheimer Disease/psychology ; Animals ; Astrocytes/metabolism ; Astrocytes/pathology ; Female ; Hippocampus/metabolism ; Hippocampus/pathology ; Hippocampus/physiopathology ; Humans ; Male ; Memory ; Mice ; Sex Characteristics ; Sex Factors ; Synaptic Transmission ; gamma-Aminobutyric Acid/metabolism
    Chemical Substances gamma-Aminobutyric Acid (56-12-2)
    Language English
    Publishing date 2018-11-22
    Publishing country United States
    Document type Editorial ; Research Support, Non-U.S. Gov't
    ISSN 1945-4589
    ISSN (online) 1945-4589
    DOI 10.18632/aging.101672
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Inter-library loan at ZB MED

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  5. Book ; Online ; Thesis: Beteiligung des P2Y1-Rezeptors an der Astrogliose und Apoptose nach einem Schädel-Hirn-Trauma im Mausmodell

    Krügel, Thomas [Verfasser] / Franke, Heike [Akademischer Betreuer] / Schaefer, Michael [Akademischer Betreuer] / Roßner, Steffen [Gutachter] / Lupp, Amelie [Gutachter]

    2023  

    Author's details Thomas Krügel ; Gutachter: Steffen Roßner, Amelie Lupp ; Heike Franke, Michael Schaefer
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Universitätsbibliothek Leipzig
    Publishing place Leipzig
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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    Inter-library loan at ZB MED

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  6. Article ; Online: Natural products from plants and algae for treatment of Alzheimer’s disease

    Klose, Jana / Griehl, Carola / Roßner, Steffen / Schilling, Stephan

    A review

    2022  

    Abstract: Neurodegenerative disorders including Parkinson’s disease (PD), Huntington’s disease (HD) and the most frequent, Alzheimer’s disease (AD), represent one of the most urgent medical needs worldwide. Despite a significantly developed understanding of ... ...

    Abstract Neurodegenerative disorders including Parkinson’s disease (PD), Huntington’s disease (HD) and the most frequent, Alzheimer’s disease (AD), represent one of the most urgent medical needs worldwide. Despite a significantly developed understanding of disease development and pathology, treatments that stop AD progression are not yet available. The recent approval of sodium oligomannate (GV-971) for AD treatment in China emphasized the potential value of natural products for the treatment of neurodegenerative disorders. Many current clinical studies include the administration of a natural compound as a single and combination treatment. The most prominent mechanisms of action are anti-inflammatory and anti-oxidative activities, thus preserving cellular survival. Here, we review current natural products that are either approved or are in testing for a treatment of neurodegeneration in AD. In addition to the most important compounds of plant origin, we also put special emphasis on compounds from algae, given their neuroprotective activity and their underlying mechanisms of neuroprotection.

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    5
    Keywords Alzheimer's disease ; Neurodegeneration ; Drug development ; Clinical studies
    Subject code 610
    Language English
    Publishing country de
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Tricellulin, α-Catenin and Microfibrillar-Associated Protein 5 Exhibit Concomitantly Altered Immunosignals along with Vascular, Extracellular and Cytoskeletal Elements after Experimental Focal Cerebral Ischemia

    Corinna Höfling / Steffen Roßner / Bianca Flachmeyer / Martin Krueger / Wolfgang Härtig / Dominik Michalski

    International Journal of Molecular Sciences, Vol 24, Iss 11893, p

    2023  Volume 11893

    Abstract: Along with initiatives to understand the pathophysiology of stroke in detail and to identify neuroprotective targets, cell-stabilizing elements have gained increasing attention. Although cell culture experiments have indicated that tricellulin, α-catenin ...

    Abstract Along with initiatives to understand the pathophysiology of stroke in detail and to identify neuroprotective targets, cell-stabilizing elements have gained increasing attention. Although cell culture experiments have indicated that tricellulin, α-catenin and microfibrillar-associated protein 5 (MFAP5) contribute to cellular integrity, these elements have not yet been investigated in the ischemic brain. Applying immunofluorescence labeling, this study explored tricellulin, MFAP5 and α-catenin in non-ischemic and ischemic brain areas of mice (24, 4 h of ischemia) and rats (4 h of ischemia), along with collagen IV and fibronectin as vascular and extracellular matrix constituents and microtubule-associated protein 2 (MAP2) and neurofilament light chain (NF-L) as cytoskeletal elements. Immunosignals of tricellulin and notably MFAP5 partially appeared in a fiber-like pattern, and α-catenin appeared more in a dotted pattern. Regional associations with vascular and extracellular constituents were found for tricellulin and α-catenin, particularly in ischemic areas. Due to ischemia, signals of tricellulin, MFAP5 and α-catenin decreased concomitantly with MAP2 and NF-L, whereby MFAP5 provided the most sensitive reaction. For the first time, this study demonstrated ischemia-related alterations in tricellulin, MFAP5 and α-catenin along with the vasculature, extracellular matrix and cytoskeleton. Confirmatory studies are needed, also exploring their role in cellular integrity and the potential for neuroprotective approaches in stroke.
    Keywords tricellulin ; microfibrillar-associated protein 5 ; α-catenin ; neurovascular unit ; NVU ; experimental stroke ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 612
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Book ; Online ; Thesis: The regulation of the expression of PMCA isoforms by neuroplastin has an impact on the calcium clearance in cultured hippocampal neurons

    Junge, Lennart [Verfasser] / Brunner-Weinzierl, Monika [Gutachter] / Roßner, Steffen [Gutachter]

    2021  

    Author's details Lennart Junge ; Gutachter: Monika Brunner-Weinzierl, Steffen Roßner
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek Otto-von-Guericke-Universität
    Publishing place Magdeburg
    Document type Book ; Online ; Thesis
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  9. Article ; Online: Peptide backbone modifications of amyloid β (1-40) impact fibrillation behavior and neuronal toxicity.

    Schwarze, Benedikt / Korn, Alexander / Höfling, Corinna / Zeitschel, Ulrike / Krueger, Martin / Roßner, Steffen / Huster, Daniel

    Scientific reports

    2021  Volume 11, Issue 1, Page(s) 23767

    Abstract: Fibril formation of amyloid β (Aβ) peptides is one of the key molecular events connected to Alzheimer's disease. The pathway of formation and mechanism of action of Aβ aggregates in biological systems is still object of very active research. To this end, ...

    Abstract Fibril formation of amyloid β (Aβ) peptides is one of the key molecular events connected to Alzheimer's disease. The pathway of formation and mechanism of action of Aβ aggregates in biological systems is still object of very active research. To this end, systematic modifications of the Phe
    MeSH term(s) Amino Acids/metabolism ; Amyloid/chemistry ; Amyloid/genetics ; Amyloid/metabolism ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Mutation ; Neurons/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Aggregation, Pathological/metabolism ; Protein Conformation ; Spectrum Analysis
    Chemical Substances Amino Acids ; Amyloid ; Amyloid beta-Peptides ; Peptide Fragments ; amyloid beta-protein (1-40)
    Language English
    Publishing date 2021-12-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-03091-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Proteolytic α-Synuclein Cleavage in Health and Disease.

    Bluhm, Alexandra / Schrempel, Sarah / von Hörsten, Stephan / Schulze, Anja / Roßner, Steffen

    International journal of molecular sciences

    2021  Volume 22, Issue 11

    Abstract: In Parkinson's disease, aggregates of α-synuclein within Lewy bodies and Lewy neurites represent neuropathological hallmarks. However, the cellular and molecular mechanisms triggering oligomeric and fibrillary α-synuclein aggregation are not fully ... ...

    Abstract In Parkinson's disease, aggregates of α-synuclein within Lewy bodies and Lewy neurites represent neuropathological hallmarks. However, the cellular and molecular mechanisms triggering oligomeric and fibrillary α-synuclein aggregation are not fully understood. Recent evidence indicates that oxidative stress induced by metal ions and post-translational modifications such as phosphorylation, ubiquitination, nitration, glycation, and SUMOylation affect α-synuclein conformation along with its aggregation propensity and neurotoxic profiles. In addition, proteolytic cleavage of α-synuclein by specific proteases results in the formation of a broad spectrum of fragments with consecutively altered and not fully understood physiological and/or pathological properties. In the present review, we summarize the current knowledge on proteolytical α-synuclein cleavage by neurosin, calpain-1, cathepsin D, and matrix metalloproteinase-3 in health and disease. We also shed light on the contribution of the same enzymes to proteolytical processing of pathogenic proteins in Alzheimer's disease and report potential cross-disease mechanisms of pathogenic protein aggregation.
    MeSH term(s) Alzheimer Disease/metabolism ; Animals ; Humans ; Parkinson Disease/metabolism ; Peptide Hydrolases/metabolism ; Protein Aggregates/physiology ; Proteolysis ; alpha-Synuclein/metabolism
    Chemical Substances Protein Aggregates ; alpha-Synuclein ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2021-05-21
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22115450
    Database MEDical Literature Analysis and Retrieval System OnLINE

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