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  1. Article ; Online: C9orf72 dipeptides disrupt the nucleocytoplasmic transport machinery and cause TDP-43 mislocalisation to the cytoplasm.

    Ryan, Sarah / Rollinson, Sara / Hobbs, Eleanor / Pickering-Brown, Stuart

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 4799

    Abstract: A repeat expansion in C9orf72 is the major cause of both frontotemporal dementia and amyotrophic lateral sclerosis, accounting for approximately 1 in 12 cases of either disease. The expansion is translated to produce five dipeptide repeat proteins (DPRs) ...

    Abstract A repeat expansion in C9orf72 is the major cause of both frontotemporal dementia and amyotrophic lateral sclerosis, accounting for approximately 1 in 12 cases of either disease. The expansion is translated to produce five dipeptide repeat proteins (DPRs) which aggregate in patient brain and are toxic in numerous models, though the mechanisms underlying this toxicity are poorly understood. Recent studies highlight nucleocytoplasmic transport impairments as a potential mechanism underlying neurodegeneration in C9orf72-linked disease, although the contribution of DPRs to this remains unclear. We expressed DPRs in HeLa cells, in the absence of repeat RNA. Crucially, we expressed DPRs at repeat-lengths found in patients (> 1000 units), ensuring our findings were relevant to disease. Immunofluorescence imaging was used to investigate the impact of each DPR on the nucleus, nucleocytoplasmic transport machinery and TDP-43 localisation. DPRs impaired the structural integrity of the nucleus, causing nuclear membrane disruption and misshapen nuclei. Ran and RanGAP, two proteins required for nucleocytoplasmic transport, were also mislocalised in DPR-expressing cells. Furthermore, DPRs triggered mislocalisation of TDP-43 to the cytoplasm, and this occurred in the same cells as Ran and RanGAP mislocalisation, suggesting a potential link between DPRs, nucleocytoplasmic transport impairments and TDP-43 pathology.
    MeSH term(s) Active Transport, Cell Nucleus ; Amyotrophic Lateral Sclerosis/metabolism ; C9orf72 Protein/genetics ; C9orf72 Protein/metabolism ; Cytoplasm/metabolism ; DNA Repeat Expansion ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Dipeptides/metabolism ; Frontotemporal Dementia/pathology ; HeLa Cells ; Humans
    Chemical Substances C9orf72 Protein ; C9orf72 protein, human ; DNA-Binding Proteins ; Dipeptides ; TARDBP protein, human
    Language English
    Publishing date 2022-03-21
    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/s41598-022-08724-w
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  2. Article ; Online: Is SIGMAR1 a confirmed FTD/MND gene?

    Pickering-Brown, Stuart / Hardy, John

    Brain : a journal of neurology

    2015  Volume 138, Issue Pt 11, Page(s) e393

    MeSH term(s) Animals ; Endoplasmic Reticulum/genetics ; Mitochondria/genetics ; Motor Neuron Disease/genetics ; Receptors, sigma/genetics
    Chemical Substances Receptors, sigma
    Language English
    Publishing date 2015-11
    Publishing country England
    Document type Comment ; Letter
    ZDB-ID 80072-7
    ISSN 1460-2156 ; 0006-8950
    ISSN (online) 1460-2156
    ISSN 0006-8950
    DOI 10.1093/brain/awv173
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  3. Article ; Online: CRISPR/Cas9 does not facilitate stable expression of long C9orf72 dipeptides in mice.

    Ryan, Sarah / Hobbs, Eleanor / Rollinson, Sara / Pickering-Brown, Stuart M

    Neurobiology of aging

    2019  Volume 84, Page(s) 235.e1–235.e8

    Abstract: A C9orf72 repeat expansion is the most common cause of both frontotemporal dementia and motor neuron disease. The expansion is translated to produce dipeptide repeat proteins (DPRs), which are toxic in vivo and in vitro. However, the mechanisms ... ...

    Abstract A C9orf72 repeat expansion is the most common cause of both frontotemporal dementia and motor neuron disease. The expansion is translated to produce dipeptide repeat proteins (DPRs), which are toxic in vivo and in vitro. However, the mechanisms underlying DPR toxicity remain unclear. Mouse models which express DPRs at repeat lengths found in human disease are urgently required to investigate this. We aimed to generate transgenic mice expressing DPRs at repeat lengths of >1000 using alternative codon sequences, to reduce the repetitive nature of the insert. We found that although these inserts did integrate into the mouse genome, the alternative codon sequences did not protect from instability between generations. Our findings suggest that stable integration of long DPR sequences may not be possible. Administration of viral vectors after birth may be a more effective delivery method for long repeats.
    MeSH term(s) Animals ; C9orf72 Protein ; Clustered Regularly Interspaced Short Palindromic Repeats ; Mice ; Mice, Transgenic ; Trinucleotide Repeat Expansion
    Chemical Substances C9orf72 Protein ; C9orf72 protein, mouse
    Language English
    Publishing date 2019-09-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 604505-4
    ISSN 1558-1497 ; 0197-4580
    ISSN (online) 1558-1497
    ISSN 0197-4580
    DOI 10.1016/j.neurobiolaging.2019.09.010
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  4. Article ; Online: The cellular expression and proteolytic processing of the amyloid precursor protein is independent of TDP-43.

    Hicks, David A / Jones, Alys C / Pickering-Brown, Stuart M / Hooper, Nigel M

    Bioscience reports

    2020  Volume 40, Issue 4

    Abstract: Alzheimer's disease (AD) is a neurodegenerative condition, of which one of the cardinal pathological hallmarks is the extracellular accumulation of amyloid β (Aβ) peptides. These peptides are generated via proteolysis of the amyloid precursor protein ( ... ...

    Abstract Alzheimer's disease (AD) is a neurodegenerative condition, of which one of the cardinal pathological hallmarks is the extracellular accumulation of amyloid β (Aβ) peptides. These peptides are generated via proteolysis of the amyloid precursor protein (APP), in a manner dependent on the β-secretase, BACE1 and the multicomponent γ-secretase complex. Recent data also suggest a contributory role in AD of transactive response DNA binding protein 43 (TDP-43). There is little insight into a possible mechanism linking TDP-43 and APP processing. To this end, we used cultured human neuronal cells to investigate the ability of TDP-43 to interact with APP and modulate its proteolytic processing. Immunocytochemistry showed TDP-43 to be spatially segregated from both the extranuclear APP holoprotein and its nuclear C-terminal fragment. The latter (APP intracellular domain) was shown to predominantly localise to nucleoli, from which TDP-43 was excluded. Furthermore, neither overexpression of each of the APP isoforms nor siRNA-mediated knockdown of APP had any effect on TDP-43 expression. Doxycycline-stimulated overexpression of TDP-43 was explored in an inducible cell line. Overexpression of TDP-43 had no effect on expression of the APP holoprotein, nor any of the key proteins involved in its proteolysis. Furthermore, increased TDP-43 expression had no effect on BACE1 enzymatic activity or immunoreactivity of Aβ1-40, Aβ1-42 or the Aβ1-40:Aβ1-42 ratio. Also, siRNA-mediated knockdown of TDP-43 had no effect on BACE1 immunoreactivity. Taken together, these data indicate that TDP-43 function and/or dysfunction in AD is likely independent from dysregulation of APP expression and proteolytic processing and Aβ generation.
    MeSH term(s) Alzheimer Disease/pathology ; Amyloid Precursor Protein Secretases/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Aspartic Acid Endopeptidases/metabolism ; Cell Line, Tumor ; Cell Nucleus/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Knockdown Techniques ; Humans ; Neurons/cytology ; Neurons/metabolism ; Proteolysis ; RNA, Small Interfering/metabolism
    Chemical Substances APP protein, human ; Amyloid beta-Protein Precursor ; DNA-Binding Proteins ; RNA, Small Interfering ; TARDBP protein, human ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; BACE1 protein, human (EC 3.4.23.46)
    Language English
    Publishing date 2020-04-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 764946-0
    ISSN 1573-4935 ; 0144-8463
    ISSN (online) 1573-4935
    ISSN 0144-8463
    DOI 10.1042/BSR20200435
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  5. Article ; Online: Extracellular Vesicles Isolated from Human Induced Pluripotent Stem Cell-Derived Neurons Contain a Transcriptional Network.

    Hicks, David A / Jones, Alys C / Corbett, Nicola J / Fisher, Kate / Pickering-Brown, Stuart M / Ashe, Mark P / Hooper, Nigel M

    Neurochemical research

    2020  Volume 45, Issue 7, Page(s) 1711–1728

    Abstract: Healthy brain function is mediated by several complementary signalling pathways, many of which are driven by extracellular vesicles (EVs). EVs are heterogeneous in both size and cargo and are constitutively released from cells into the extracellular ... ...

    Abstract Healthy brain function is mediated by several complementary signalling pathways, many of which are driven by extracellular vesicles (EVs). EVs are heterogeneous in both size and cargo and are constitutively released from cells into the extracellular milieu. They are subsequently trafficked to recipient cells, whereupon their entry can modify the cellular phenotype. Here, in order to further analyse the mRNA and protein cargo of neuronal EVs, we isolated EVs by size exclusion chromatography from human induced pluripotent stem cell (iPSC)-derived neurons. Electron microscopy and dynamic light scattering revealed that the isolated EVs had a diameter of 30-100 nm. Transcriptomic and proteomics analyses of the EVs and neurons identified key molecules enriched in the EVs involved in cell surface interaction (integrins and collagens), internalisation pathways (clathrin- and caveolin-dependent), downstream signalling pathways (phospholipases, integrin-linked kinase and MAPKs), and long-term impacts on cellular development and maintenance. Overall, we show that key signalling networks and mechanisms are enriched in EVs isolated from human iPSC-derived neurons.
    MeSH term(s) Extracellular Vesicles/genetics ; Extracellular Vesicles/metabolism ; Gene Regulatory Networks/physiology ; Humans ; Induced Pluripotent Stem Cells/physiology ; Neurons/physiology ; Transcription, Genetic/physiology
    Language English
    Publishing date 2020-05-02
    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/s11064-020-03019-w
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  6. Article ; Online: Co-expression of C9orf72 related dipeptide-repeats over 1000 repeat units reveals age- and combination-specific phenotypic profiles in Drosophila.

    West, Ryan J H / Sharpe, Joanne L / Voelzmann, André / Munro, Anna L / Hahn, Ines / Baines, Richard A / Pickering-Brown, Stuart

    Acta neuropathologica communications

    2020  Volume 8, Issue 1, Page(s) 158

    Abstract: A large intronic hexanucleotide repeat expansion (GGGGCC) within the C9orf72 (C9orf72-SMCR8 Complex Subunit) locus is the most prevalent genetic cause of both Frontotemporal Dementia (FTD) and Motor Neuron Disease (MND). In patients this expansion is ... ...

    Abstract A large intronic hexanucleotide repeat expansion (GGGGCC) within the C9orf72 (C9orf72-SMCR8 Complex Subunit) locus is the most prevalent genetic cause of both Frontotemporal Dementia (FTD) and Motor Neuron Disease (MND). In patients this expansion is typically hundreds to thousands of repeat units in length. Repeat associated non-AUG translation of the expansion leads to the formation of toxic, pathological Dipeptide-Repeat Proteins (DPRs). To date there remains a lack of in vivo models expressing C9orf72 related DPRs with a repeat length of more than a few hundred repeats. As such our understanding of how physiologically relevant repeat length DPRs effect the nervous system in an ageing in vivo system remains limited. In this study we generated Drosophila models expressing DPRs over 1000 repeat units in length, a known pathological length in humans. Using these models, we demonstrate each DPR exhibits a unique, age-dependent, phenotypic and pathological profile. Furthermore, we show co-expression of specific DPR combinations leads to distinct, age-dependent, phenotypes not observed through expression of single DPRs. We propose these models represent a unique, in vivo, tool for dissecting the molecular mechanisms implicated in disease pathology, opening up new avenues in the study of both MND and FTD.
    MeSH term(s) Animals ; C9orf72 Protein/genetics ; DNA Repeat Expansion/genetics ; Dipeptides/genetics ; Disease Models, Animal ; Drosophila ; Frontotemporal Dementia ; Motor Neuron Disease ; Phenotype
    Chemical Substances C9orf72 Protein ; Dipeptides
    Language English
    Publishing date 2020-09-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2715589-4
    ISSN 2051-5960 ; 2051-5960
    ISSN (online) 2051-5960
    ISSN 2051-5960
    DOI 10.1186/s40478-020-01028-y
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  7. Article: The complex aetiology of frontotemporal lobar degeneration.

    Pickering-Brown, Stuart M

    Experimental neurology

    2007  Volume 206, Issue 1, Page(s) 1–10

    Abstract: Frontotemporal lobar degeneration (FTLD) is now a widely recognised form of dementia. This heterogeneous disease has been of particular interest to geneticists due to its high rate of heritability with up to 40% of patients reporting a family history of ... ...

    Abstract Frontotemporal lobar degeneration (FTLD) is now a widely recognised form of dementia. This heterogeneous disease has been of particular interest to geneticists due to its high rate of heritability with up to 40% of patients reporting a family history of the disease in at least one extra family member. There have been several chromosome loci linked to this disorder and three genes have already been identified. Remarkably, it has been recently demonstrated that 2 of these are only 1.7 Mb from one another on chromosome 17q21, these being tau and progranulin. The identification of these genes has contributed greatly to our understanding of the differing neuropathologies associated with FTLD. Furthermore, the discovery that TDP-43 is a component of the neuronal inclusions seen in the most common neuropathological subtype has also helped expand the biochemical pathways that are the focus of much FTLD research. Nevertheless, other genes causing FTLD remain to be identified and their biology elucidated before we have a complete understanding of the complex aetiology of this disease.
    MeSH term(s) Brain/metabolism ; Brain/physiopathology ; Chromosomes, Human, Pair 17/genetics ; DNA-Binding Proteins ; Dementia/genetics ; Dementia/metabolism ; Dementia/physiopathology ; Genetic Predisposition to Disease/genetics ; Humans ; Inclusion Bodies/genetics ; Inclusion Bodies/metabolism ; Intercellular Signaling Peptides and Proteins/genetics ; Mutation/genetics ; Progranulins ; tau Proteins/genetics
    Chemical Substances DNA-Binding Proteins ; GRN protein, human ; Intercellular Signaling Peptides and Proteins ; Progranulins ; tau Proteins
    Language English
    Publishing date 2007-03-24
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207148-4
    ISSN 1090-2430 ; 0014-4886
    ISSN (online) 1090-2430
    ISSN 0014-4886
    DOI 10.1016/j.expneurol.2007.03.017
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  8. Article: Progranulin and frontotemporal lobar degeneration.

    Pickering-Brown, Stuart M

    Acta neuropathologica

    2007  Volume 114, Issue 1, Page(s) 39–47

    Abstract: Frontotemporal lobar degeneration is the term used to describe the non-Alzheimer clinical syndromes of frontotemporal dementia, semantic dementia and progressive non-fluent aphasia, regardless of the underlying neuropathological features. Considerable ... ...

    Abstract Frontotemporal lobar degeneration is the term used to describe the non-Alzheimer clinical syndromes of frontotemporal dementia, semantic dementia and progressive non-fluent aphasia, regardless of the underlying neuropathological features. Considerable progress has been made in recent years in our understanding of the aetiology of this disorder, notably the identification of mutations in tau and progranulin genes, both on chromosome 17q21. Mutations in tau appear to affect the ability of tau to bind microtubules and/or increase this protein's ability to form fibrils. In contrast, progranulin mutations cause haploinsufficiency leading to TDP-43 accumulation. These genes collectively account for 10-20% of FTLD. However, it is clear that much remains to be discovered before our knowledge of this heterogeneous condition is complete.
    MeSH term(s) DNA-Binding Proteins/metabolism ; Dementia/genetics ; Dementia/metabolism ; Dementia/pathology ; Humans ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Mutation/genetics ; Progranulins ; tau Proteins/genetics ; tau Proteins/metabolism
    Chemical Substances DNA-Binding Proteins ; GRN protein, human ; Intercellular Signaling Peptides and Proteins ; MAPT protein, human ; Progranulins ; tau Proteins
    Language English
    Publishing date 2007-06-16
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1079-0
    ISSN 1432-0533 ; 0001-6322
    ISSN (online) 1432-0533
    ISSN 0001-6322
    DOI 10.1007/s00401-007-0241-6
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  9. Article ; Online: Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS.

    Bennion Callister, Janis / Pickering-Brown, Stuart M

    Experimental neurology

    2014  Volume 262 Pt B, Page(s) 84–90

    Abstract: One of the most interesting findings in the field of neurodegeneration in recent years is tfche discovery of a genetic mutation in the C9orf72 gene, the most common mutation found to be causative of sporadic and familial frontotemporal lobar degeneration ...

    Abstract One of the most interesting findings in the field of neurodegeneration in recent years is tfche discovery of a genetic mutation in the C9orf72 gene, the most common mutation found to be causative of sporadic and familial frontotemporal lobar degeneration (FTLD), amyotrophic lateral sclerosis (ALS) and concomitant FTD-ALS (DeJesus-Hernandez et al., 2011b; Renton et al., 2011). While clinical and molecular data, such as the identification of TDP-43 being a common pathological protein (Neumann et al., 2006) have hinted at such a link for years, the identification of what was formally known as "the chromosome 9 FTLD-ALS gene" has provided a foundation for better understanding of the relationship between the two. Indeed, it is now recognized that ALS and FTLD-TDP represent a disease spectrum. In this review, we will discuss the current genetic and pathological features of the FTLD-ALS spectrum.
    MeSH term(s) Amyotrophic Lateral Sclerosis/complications ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/pathology ; DNA-Binding Proteins/genetics ; Frontotemporal Dementia/complications ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/pathology ; Humans ; Mutation/genetics
    Chemical Substances DNA-Binding Proteins
    Language English
    Publishing date 2014-06-08
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207148-4
    ISSN 1090-2430 ; 0014-4886
    ISSN (online) 1090-2430
    ISSN 0014-4886
    DOI 10.1016/j.expneurol.2014.06.001
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  10. Article: The tau gene locus and frontotemporal dementia.

    Pickering-Brown, Stuart

    Dementia and geriatric cognitive disorders

    2004  Volume 17, Issue 4, Page(s) 258–260

    Abstract: Frontotemporal lobar degeneration (FTLD) has become an increasingly recognised form of dementia. It has been demonstrated that a proportion of cases of FTLD result from mutations in the tau gene on chromosome 17. A pathological hallmark in the brains ... ...

    Abstract Frontotemporal lobar degeneration (FTLD) has become an increasingly recognised form of dementia. It has been demonstrated that a proportion of cases of FTLD result from mutations in the tau gene on chromosome 17. A pathological hallmark in the brains from patients with tau mutations is an accumulation of insoluble tau within neurons and glia that is considered neurotoxic. However, there are reports of families with FTLD linked to the tau locus on chromosome 17 in which no mutations have been found, and these families lack any accumulation of insoluble tau. Recently, two new tau mutations have been described that also appear to cause disease in the absence of any tau accumulation. The role of the tau locus and tau accumulation in contributing to the neurodegenerative process in chromosome-17-linked families without mutations and in families with tau mutations without insoluble tau is discussed.
    MeSH term(s) Chromosome Mapping ; Chromosomes, Human, Pair 17 ; Dementia/genetics ; Dementia/metabolism ; Humans ; tau Proteins/genetics ; tau Proteins/metabolism
    Chemical Substances tau Proteins
    Language English
    Publishing date 2004
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1026007-9
    ISSN 1420-8008 ; 1013-7424
    ISSN 1420-8008 ; 1013-7424
    DOI 10.1159/000077149
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