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  1. Article: Cellular Regulation of Amyloid Formation in Aging and Disease.

    Stroo, Esther / Koopman, Mandy / Nollen, Ellen A A / Mata-Cabana, Alejandro

    Frontiers in neuroscience

    2017  Volume 11, Page(s) 64

    Abstract: As the population is aging, the incidence of age-related neurodegenerative diseases, such as Alzheimer and Parkinson disease, is growing. The pathology of neurodegenerative diseases is characterized by the presence of protein aggregates of disease ... ...

    Abstract As the population is aging, the incidence of age-related neurodegenerative diseases, such as Alzheimer and Parkinson disease, is growing. The pathology of neurodegenerative diseases is characterized by the presence of protein aggregates of disease specific proteins in the brain of patients. Under certain conditions these disease proteins can undergo structural rearrangements resulting in misfolded proteins that can lead to the formation of aggregates with a fibrillar amyloid-like structure. Cells have different mechanisms to deal with this protein aggregation, where the molecular chaperone machinery constitutes the first line of defense against misfolded proteins. Proteins that cannot be refolded are subjected to degradation and compartmentalization processes. Amyloid formation has traditionally been described as responsible for the proteotoxicity associated with different neurodegenerative disorders. Several mechanisms have been suggested to explain such toxicity, including the sequestration of key proteins and the overload of the protein quality control system. Here, we review different aspects of the involvement of amyloid-forming proteins in disease, mechanisms of toxicity, structural features, and biological functions of amyloids, as well as the cellular mechanisms that modulate and regulate protein aggregation, including the presence of enhancers and suppressors of aggregation, and how aging impacts the functioning of these mechanisms, with special attention to the molecular chaperones.
    Language English
    Publishing date 2017-02-14
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2411902-7
    ISSN 1662-453X ; 1662-4548
    ISSN (online) 1662-453X
    ISSN 1662-4548
    DOI 10.3389/fnins.2017.00064
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  2. Article ; Online: Deletion of SERF2 in mice delays embryonic development and alters amyloid deposit structure in the brain.

    Stroo, Esther / Janssen, Leen / Sin, Olga / Hogewerf, Wytse / Koster, Mirjam / Harkema, Liesbeth / Youssef, Sameh A / Beschorner, Natalie / Wolters, Anouk Hg / Bakker, Bjorn / Becker, Lore / Garrett, Lilian / Marschall, Susan / Hoelter, Sabine M / Wurst, Wolfgang / Fuchs, Helmut / Gailus-Durner, Valerie / Hrabe de Angelis, Martin / Thathiah, Amantha /
    Foijer, Floris / van de Sluis, Bart / van Deursen, Jan / Jucker, Matthias / de Bruin, Alain / Nollen, Ellen Aa

    Life science alliance

    2023  Volume 6, Issue 7

    Abstract: In age-related neurodegenerative diseases, like Alzheimer's and Parkinson's, disease-specific proteins become aggregation-prone and form amyloid-like deposits. Depletion of SERF proteins ameliorates this toxic process in worm and human cell models for ... ...

    Abstract In age-related neurodegenerative diseases, like Alzheimer's and Parkinson's, disease-specific proteins become aggregation-prone and form amyloid-like deposits. Depletion of SERF proteins ameliorates this toxic process in worm and human cell models for diseases. Whether SERF modifies amyloid pathology in mammalian brain, however, has remained unknown. Here, we generated conditional
    MeSH term(s) Animals ; Humans ; Mice ; Amyloid beta-Peptides/metabolism ; Brain/embryology ; Brain/metabolism ; Embryonic Development/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Mice, Knockout ; Plaque, Amyloid/metabolism
    Chemical Substances Amyloid beta-Peptides ; Intracellular Signaling Peptides and Proteins ; Serf2 protein, mouse
    Language English
    Publishing date 2023-05-02
    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.202201730
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation.

    Pras, Anita / Houben, Bert / Aprile, Francesco A / Seinstra, Renée / Gallardo, Rodrigo / Janssen, Leen / Hogewerf, Wytse / Gallrein, Christian / De Vleeschouwer, Matthias / Mata-Cabana, Alejandro / Koopman, Mandy / Stroo, Esther / de Vries, Minke / Louise Edwards, Samantha / Kirstein, Janine / Vendruscolo, Michele / Falsone, Salvatore Fabio / Rousseau, Frederic / Schymkowitz, Joost /
    Nollen, Ellen A A

    The EMBO journal

    2021  Volume 40, Issue 21, Page(s) e107568

    Abstract: While aggregation-prone proteins are known to accelerate aging and cause age-related diseases, the cellular mechanisms that drive their cytotoxicity remain unresolved. The orthologous proteins MOAG-4, SERF1A, and SERF2 have recently been identified as ... ...

    Abstract While aggregation-prone proteins are known to accelerate aging and cause age-related diseases, the cellular mechanisms that drive their cytotoxicity remain unresolved. The orthologous proteins MOAG-4, SERF1A, and SERF2 have recently been identified as cellular modifiers of such proteotoxicity. Using a peptide array screening approach on human amyloidogenic proteins, we found that SERF2 interacted with protein segments enriched in negatively charged and hydrophobic, aromatic amino acids. The absence of such segments, or the neutralization of the positive charge in SERF2, prevented these interactions and abolished the amyloid-promoting activity of SERF2. In protein aggregation models in the nematode worm Caenorhabditis elegans, protein aggregation and toxicity were suppressed by mutating the endogenous locus of MOAG-4 to neutralize charge. Our data indicate that MOAG-4 and SERF2 drive protein aggregation and toxicity by interactions with negatively charged segments in aggregation-prone proteins. Such charge interactions might accelerate primary nucleation of amyloid by initiating structural changes and by decreasing colloidal stability. Our study points at charge interactions between cellular modifiers and amyloidogenic proteins as potential targets for interventions to reduce age-related protein toxicity.
    MeSH term(s) Amino Acid Sequence ; Amyloid/chemistry ; Amyloid/genetics ; Amyloid/metabolism ; Amyloidogenic Proteins/chemistry ; Amyloidogenic Proteins/genetics ; Amyloidogenic Proteins/metabolism ; Animals ; Binding Sites ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Gene Expression Regulation ; HEK293 Cells ; Humans ; Hydrophobic and Hydrophilic Interactions ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Peptides/genetics ; Peptides/metabolism ; Protein Aggregates ; Protein Array Analysis ; Protein Binding ; Signal Transduction ; Static Electricity ; alpha-Synuclein/chemistry ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
    Chemical Substances Amyloid ; Amyloidogenic Proteins ; Caenorhabditis elegans Proteins ; Intracellular Signaling Peptides and Proteins ; MOAG-4 protein, C elegans ; Nerve Tissue Proteins ; Peptides ; Protein Aggregates ; SERF1A protein, human ; SERF2 protein, human ; alpha-Synuclein
    Language English
    Publishing date 2021-10-07
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2020107568
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
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  4. Article ; Online: Tissue transglutaminase in marmoset experimental multiple sclerosis: discrepancy between white and grey matter.

    Espitia Pinzon, Nathaly / Stroo, Esther / 't Hart, Bert A / Bol, John G J M / Drukarch, Benjamin / Bauer, Jan / van Dam, Anne-Marie

    PloS one

    2014  Volume 9, Issue 6, Page(s) e100574

    Abstract: Infiltration of leukocytes is a major pathological event in white matter lesion formation in the brain of multiple sclerosis (MS) patients. In grey matter lesions, less infiltration of these cells occur, but microglial activation is present. Thus far, ... ...

    Abstract Infiltration of leukocytes is a major pathological event in white matter lesion formation in the brain of multiple sclerosis (MS) patients. In grey matter lesions, less infiltration of these cells occur, but microglial activation is present. Thus far, the interaction of β-integrins with extracellular matrix proteins, e.g. fibronectin, is considered to be of importance for the influx of immune cells. Recent in vitro studies indicate a possible role for the enzyme tissue Transglutaminase (TG2) in mediating cell adhesion and migration. In the present study we questioned whether TG2 is present in white and grey matter lesions observed in the marmoset model for MS. To this end, immunohistochemical studies were performed. We observed that TG2, expressed by infiltrating monocytes in white matter lesions co-expressed β1-integrin and is located in close apposition to deposited fibronectin. These data suggest an important role for TG2 in the adhesion and migration of infiltrating monocytes during white matter lesion formation. Moreover, in grey matter lesions, TG2 is mainly present in microglial cells together with some β1-integrin, whereas fibronectin is absent in these lesions. These data imply an alternative role for microglial-derived TG2 in grey matter lesions, e.g. cell proliferation. Further research should clarify the functional role of TG2 in monocytes or microglial cells in MS lesion formation.
    MeSH term(s) Animals ; Astrocytes/metabolism ; Callithrix ; Disease Models, Animal ; Encephalomyelitis, Autoimmune, Experimental/enzymology ; Encephalomyelitis, Autoimmune, Experimental/pathology ; Fibronectins/immunology ; Fibronectins/metabolism ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/immunology ; GTP-Binding Proteins/metabolism ; Gene Expression ; Gray Matter/enzymology ; Gray Matter/immunology ; Gray Matter/pathology ; Immunohistochemistry ; Integrin beta1/immunology ; Integrin beta1/metabolism ; Lymphocyte Subsets/immunology ; Lymphocyte Subsets/metabolism ; Microglia/metabolism ; Monocytes/metabolism ; Multiple Sclerosis/enzymology ; Multiple Sclerosis/genetics ; Multiple Sclerosis/immunology ; Multiple Sclerosis/pathology ; Oligodendroglia ; Organ Specificity ; Transglutaminases/genetics ; Transglutaminases/immunology ; Transglutaminases/metabolism ; White Matter/enzymology ; White Matter/immunology ; White Matter/pathology
    Chemical Substances Fibronectins ; Integrin beta1 ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-)
    Language English
    Publishing date 2014-06-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0100574
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  5. Article ; Online: Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation.

    Sin, Olga / de Jong, Tristan / Mata-Cabana, Alejandro / Kudron, Michelle / Zaini, Mohamad Amr / Aprile, Francesco A / Seinstra, Renée I / Stroo, Esther / Prins, Roméo Willinge / Martineau, Céline N / Wang, Hai Hui / Hogewerf, Wytse / Steinhof, Anne / Wanker, Erich E / Vendruscolo, Michele / Calkhoven, Cornelis F / Reinke, Valerie / Guryev, Victor / Nollen, Ellen A A

    Molecular cell

    2017  Volume 65, Issue 6, Page(s) 1096–1108.e6

    Abstract: Protein aggregation is associated with age-related neurodegenerative disorders, such as Alzheimer's and polyglutamine diseases. As a causal relationship between protein aggregation and neurodegeneration remains elusive, understanding the cellular ... ...

    Abstract Protein aggregation is associated with age-related neurodegenerative disorders, such as Alzheimer's and polyglutamine diseases. As a causal relationship between protein aggregation and neurodegeneration remains elusive, understanding the cellular mechanisms regulating protein aggregation will help develop future treatments. To identify such mechanisms, we conducted a forward genetic screen in a C. elegans model of polyglutamine aggregation and identified the protein MOAG-2/LIR-3 as a driver of protein aggregation. In the absence of polyglutamine, MOAG-2/LIR-3 regulates the RNA polymerase III-associated transcription of small non-coding RNAs. This regulation is lost in the presence of polyglutamine, which mislocalizes MOAG-2/LIR-3 from the nucleus to the cytosol. We then show biochemically that MOAG-2/LIR-3 can also catalyze the aggregation of polyglutamine-expanded huntingtin. These results suggest that polyglutamine can induce an aggregation-promoting activity of MOAG-2/LIR-3 in the cytosol. The concept that certain aggregation-prone proteins can convert other endogenous proteins into drivers of aggregation and toxicity adds to the understanding of how cellular homeostasis can be deteriorated in protein misfolding diseases.
    MeSH term(s) Active Transport, Cell Nucleus ; Animals ; Animals, Genetically Modified ; Binding Sites ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Nucleus/enzymology ; Cytosol/enzymology ; Disease Models, Animal ; Neurodegenerative Diseases/enzymology ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/pathology ; Peptides/metabolism ; Promoter Regions, Genetic ; Protein Aggregates ; Protein Aggregation, Pathological ; Protein Binding ; RNA Interference ; RNA Polymerase III/genetics ; RNA Polymerase III/metabolism ; RNA, Small Untranslated/genetics ; RNA, Small Untranslated/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription, Genetic
    Chemical Substances Caenorhabditis elegans Proteins ; LIR-3 protein, C elegans ; Peptides ; Protein Aggregates ; RNA, Small Untranslated ; Transcription Factors ; polyglutamine (26700-71-0) ; RNA Polymerase III (EC 2.7.7.6)
    Language English
    Publishing date 2017-03-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2017.02.022
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: Show issues Location:
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  6. Article ; Online: Tissue transglutaminase in marmoset experimental multiple sclerosis

    Nathaly Espitia Pinzon / Esther Stroo / Bert A 't Hart / John G J M Bol / Benjamin Drukarch / Jan Bauer / Anne-Marie van Dam

    PLoS ONE, Vol 9, Iss 6, p e

    discrepancy between white and grey matter.

    2014  Volume 100574

    Abstract: Infiltration of leukocytes is a major pathological event in white matter lesion formation in the brain of multiple sclerosis (MS) patients. In grey matter lesions, less infiltration of these cells occur, but microglial activation is present. Thus far, ... ...

    Abstract Infiltration of leukocytes is a major pathological event in white matter lesion formation in the brain of multiple sclerosis (MS) patients. In grey matter lesions, less infiltration of these cells occur, but microglial activation is present. Thus far, the interaction of β-integrins with extracellular matrix proteins, e.g. fibronectin, is considered to be of importance for the influx of immune cells. Recent in vitro studies indicate a possible role for the enzyme tissue Transglutaminase (TG2) in mediating cell adhesion and migration. In the present study we questioned whether TG2 is present in white and grey matter lesions observed in the marmoset model for MS. To this end, immunohistochemical studies were performed. We observed that TG2, expressed by infiltrating monocytes in white matter lesions co-expressed β1-integrin and is located in close apposition to deposited fibronectin. These data suggest an important role for TG2 in the adhesion and migration of infiltrating monocytes during white matter lesion formation. Moreover, in grey matter lesions, TG2 is mainly present in microglial cells together with some β1-integrin, whereas fibronectin is absent in these lesions. These data imply an alternative role for microglial-derived TG2 in grey matter lesions, e.g. cell proliferation. Further research should clarify the functional role of TG2 in monocytes or microglial cells in MS lesion formation.
    Keywords Medicine ; R ; Science ; Q
    Subject code 610
    Language English
    Publishing date 2014-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation

    Sin, Olga / Alejandro Mata-Cabana / Anne Steinhof / Céline N. Martineau / Cornelis F. Calkhoven / Ellen A.A. Nollen / Erich E. Wanker / Esther Stroo / Francesco A. Aprile / Hai Hui Wang / Michele Vendruscolo / Michelle Kudron / Mohamad Amr Zaini / Renée I. Seinstra / Roméo Willinge Prins / Tristan de Jong / Valerie Reinke / Victor Guryev / Wytse Hogewerf

    Molecular cell. 2017 Mar. 16, v. 65, no. 6

    2017  

    Abstract: Protein aggregation is associated with age-related neurodegenerative disorders, such as Alzheimer’s and polyglutamine diseases. As a causal relationship between protein aggregation and neurodegeneration remains elusive, understanding the cellular ... ...

    Abstract Protein aggregation is associated with age-related neurodegenerative disorders, such as Alzheimer’s and polyglutamine diseases. As a causal relationship between protein aggregation and neurodegeneration remains elusive, understanding the cellular mechanisms regulating protein aggregation will help develop future treatments. To identify such mechanisms, we conducted a forward genetic screen in a C. elegans model of polyglutamine aggregation and identified the protein MOAG-2/LIR-3 as a driver of protein aggregation. In the absence of polyglutamine, MOAG-2/LIR-3 regulates the RNA polymerase III-associated transcription of small non-coding RNAs. This regulation is lost in the presence of polyglutamine, which mislocalizes MOAG-2/LIR-3 from the nucleus to the cytosol. We then show biochemically that MOAG-2/LIR-3 can also catalyze the aggregation of polyglutamine-expanded huntingtin. These results suggest that polyglutamine can induce an aggregation-promoting activity of MOAG-2/LIR-3 in the cytosol. The concept that certain aggregation-prone proteins can convert other endogenous proteins into drivers of aggregation and toxicity adds to the understanding of how cellular homeostasis can be deteriorated in protein misfolding diseases.
    Keywords cytosol ; DNA-directed RNA polymerase ; homeostasis ; models ; neurodegenerative diseases ; non-coding RNA ; protein folding ; proteins ; toxicity
    Language English
    Dates of publication 2017-0316
    Size p. 1096-1108.e6.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2017.02.022
    Database NAL-Catalogue (AGRICOLA)

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