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Article ; Online: Insights into amyloid disease from fly models.

Chen, Ko-Fan / Crowther, Damian C

2014 Volume 56, Page(s) 69–83

Abstract: The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic ... ...

Abstract	The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.
MeSH term(s)	Amyloid beta-Peptides/metabolism ; Amyloidosis/metabolism ; Amyloidosis/pathology ; Animals ; Disease Models, Animal ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Humans ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Drosophila Proteins ; tau Proteins
Language	English
Publishing date	2014-08-14
Publishing country	England
Document type	Journal Article
ISSN	1744-1358 ; 0071-1365
ISSN (online)	1744-1358
ISSN	0071-1365
DOI	10.1042/bse0560069
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Article ; Online: Drosophila melanogaster as a Model for Studies on the Early Stages of Alzheimer's Disease.

Lim, Jung Yeon / Ott, Stanislav / Crowther, Damian C

Methods in molecular biology (Clifton, N.J.)

2016 Volume 1303, Page(s) 227–239

Abstract: Fruit flies (Drosophila melanogaster) have been widely used to study the cellular and molecular basis of human neurodegenerative disease. The biological similarities between the human and the fly have been explored successfully to further investigate the ...

Abstract	Fruit flies (Drosophila melanogaster) have been widely used to study the cellular and molecular basis of human neurodegenerative disease. The biological similarities between the human and the fly have been explored successfully to further investigate the pathological basis of Alzheimer's disease (AD). Here, we discuss transgenic Drosophila models systems and the methodologies that have been employed in the study of AD.
MeSH term(s)	Alzheimer Disease ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Animals ; Brain/metabolism ; Brain/pathology ; Disease Models, Animal ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Drosophila melanogaster/physiology ; Female ; Hybridization, Genetic ; Immunoblotting ; Immunohistochemistry ; Longevity ; Male ; Motor Activity ; Solubility
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-2627-5_13
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Article ; Online: Progressive myoclonus epilepsy associated with neuroserpin inclusion bodies (neuroserpinosis).

Roussel, Benoit D / Lomas, David A / Crowther, Damian C

Epileptic disorders : international epilepsy journal with videotape

2016 Volume 18, Issue S2, Page(s) 103–110

Abstract: Familial encephalopathy with neuroserpin inclusion bodies (FENIB) is a conformational proteinopathy characterised by neuronal inclusion bodies composed of the serine protease inhibitor (SERPIN), neuroserpin. Presenting clinically as a familial dementia- ... ...

Abstract	Familial encephalopathy with neuroserpin inclusion bodies (FENIB) is a conformational proteinopathy characterised by neuronal inclusion bodies composed of the serine protease inhibitor (SERPIN), neuroserpin. Presenting clinically as a familial dementia-epilepsy syndrome, the molecular mechanism of the pathogenic abnormalities in neuroserpin has been characterised at atomic resolution. There is a remarkable genotype-phenotype correlation between the degree of molecular destabilisation of the several variants of the neuroserpin protein, their propensity to self-associate and the age of onset of the dementia-epilepsy complex. As with other serpinopathies there appears to be a mix of cell-autonomous toxicity, due to neuronal accumulation of neuroserpin, and non-cell autonomous toxicity, caused by loss of protease inhibition, in this case the dysregulated protease is likely to be tissue plasminogen activator (tPA). FENIB should be considered in cases of progressive myoclonic epilepsy and dementia particularly where there is family history of neuropsychiatric disease.
MeSH term(s)	Epilepsies, Myoclonic/genetics ; Epilepsies, Myoclonic/physiopathology ; Heredodegenerative Disorders, Nervous System/genetics ; Heredodegenerative Disorders, Nervous System/physiopathology ; Humans
Language	English
Publishing date	2016-09-12
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	2086797-9
ISSN	1950-6945 ; 1294-9361
ISSN (online)	1950-6945
ISSN	1294-9361
DOI	10.1684/epd.2016.0847
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Article ; Online: Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in a

Younan, Nadine D / Chen, Ko-Fan / Rose, Ruth-Sarah / Crowther, Damian C / Viles, John H

The Journal of biological chemistry

2018 Volume 293, Issue 34, Page(s) 13090–13099

Abstract: The cellular prion protein ( ... ...

Abstract	The cellular prion protein (PrP
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid/chemistry ; Amyloid beta-Peptides/chemistry ; Animals ; Circadian Rhythm ; Disease Models, Animal ; Drosophila melanogaster/growth & development ; Drosophila melanogaster/metabolism ; Longevity ; Mesocricetus ; Neurotoxicity Syndromes/etiology ; Neurotoxicity Syndromes/metabolism ; Neurotoxicity Syndromes/pathology ; Prion Proteins/metabolism ; Protein Binding ; Protein Multimerization
Chemical Substances	Amyloid ; Amyloid beta-Peptides ; Prion Proteins
Language	English
Publishing date	2018-06-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.003319
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Article ; Online: Central and peripheral circadian clocks and their role in Alzheimer's disease.

Chauhan, Ruchi / Chen, Ko-Fan / Kent, Brianne A / Crowther, Damian C

Disease models & mechanisms

2017 Volume 10, Issue 10, Page(s) 1187–1199

Abstract: Molecular and cellular oscillations constitute an internal clock that tracks the time of day and permits organisms to optimize their behaviour and metabolism to suit the daily demands they face. The workings of this internal clock become impaired with ... ...

Abstract	Molecular and cellular oscillations constitute an internal clock that tracks the time of day and permits organisms to optimize their behaviour and metabolism to suit the daily demands they face. The workings of this internal clock become impaired with age. In this review, we discuss whether such age-related impairments in the circadian clock interact with age-related neurodegenerative disorders, such as Alzheimer's disease. Findings from mouse and fly models of Alzheimer's disease have accelerated our understanding of the interaction between neurodegeneration and circadian biology. These models show that neurodegeneration likely impairs circadian rhythms either by damaging the central clock or by blocking its communication with other brain areas and with peripheral tissues. The consequent sleep and metabolic deficits could enhance the susceptibility of the brain to further degenerative processes. Thus, circadian dysfunction might be both a cause and an effect of neurodegeneration. We also discuss the primary role of light in the entrainment of the central clock and describe important, alternative time signals, such as food, that play a role in entraining central and peripheral circadian clocks. Finally, we propose how these recent insights could inform efforts to develop novel therapeutic approaches to re-entrain arrhythmic individuals with neurodegenerative disease.
MeSH term(s)	Age Factors ; Aging/metabolism ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/physiopathology ; Alzheimer Disease/psychology ; Animals ; Brain/metabolism ; Brain/physiopathology ; Circadian Clocks/genetics ; Circadian Rhythm/genetics ; Circadian Rhythm Signaling Peptides and Proteins/genetics ; Circadian Rhythm Signaling Peptides and Proteins/metabolism ; Disease Models, Animal ; Energy Metabolism ; Humans ; Nerve Degeneration ; Plaque, Amyloid ; Signal Transduction ; Sleep
Chemical Substances	Circadian Rhythm Signaling Peptides and Proteins
Language	English
Publishing date	2017-10-06
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2451104-3
ISSN	1754-8411 ; 1754-8403
ISSN (online)	1754-8411
ISSN	1754-8403
DOI	10.1242/dmm.030627
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Article ; Online: Functional genomics in Drosophila models of human disease.

Chen, Ko-Fan / Crowther, Damian C

Briefings in functional genomics

2012 Volume 11, Issue 5, Page(s) 405–415

Abstract: It is occasionally observed that common sporadic diseases have rare familial counterparts in which mutations at a single locus result in a similar disorder exhibiting simple Mendelian inheritance. Such an observation is often sufficient justification for ...

Abstract	It is occasionally observed that common sporadic diseases have rare familial counterparts in which mutations at a single locus result in a similar disorder exhibiting simple Mendelian inheritance. Such an observation is often sufficient justification for the creation of a disease model in the fly. Whether the system is based on the over-expression of a toxic variant of a human protein or requires the loss of function of an orthologous fly gene, the consequent phenotypes can be used to understand pathogenesis through the discovery of genetic modifiers. Such genetic screening can be completed rapidly in the fly and in this review we outline how libraries of mutants are generated and how consequent changes in disease-related phenotypes are assessed. The bioinformatic approaches to processing the copious amounts of data so generated are also presented. The next phase of fly modelling will tackle the challenges of complex diseases in which many genes are associated with risk in the human. There is growing interest in the use of interactomics and epigenetics to provide proteome- and genome-scale descriptions of the regulatory dysfunction that results in disease.
MeSH term(s)	Animals ; Disease/genetics ; Disease Models, Animal ; Drosophila/genetics ; Genome, Insect ; Genomics ; Humans ; Phenotype ; Proteome/genetics
Chemical Substances	Proteome
Language	English
Publishing date	2012-08-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2540916-5
ISSN	2041-2657 ; 2041-2649 ; 2041-2647
ISSN (online)	2041-2657
ISSN	2041-2649 ; 2041-2647
DOI	10.1093/bfgp/els038
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Article ; Online: Utilizing microphysiological systems and induced pluripotent stem cells for disease modeling: a case study for blood brain barrier research in a pharmaceutical setting.

Fabre, Kristin M / Delsing, Louise / Hicks, Ryan / Colclough, Nicola / Crowther, Damian C / Ewart, Lorna

Advanced drug delivery reviews

2018 Volume 140, Page(s) 129–135

Abstract: Microphysiological systems (MPS) may be able to provide the pharmaceutical industry models that can reflect human physiological responses to improve drug discovery and translational outcomes. With lack of efficacy being the primary cause for drug ... ...

Abstract	Microphysiological systems (MPS) may be able to provide the pharmaceutical industry models that can reflect human physiological responses to improve drug discovery and translational outcomes. With lack of efficacy being the primary cause for drug attrition, developing MPS disease models would help researchers identify novel targets, study mechanisms in more physiologically-relevant depth, screen for novel biomarkers and test/optimize various therapeutics (small molecules, nanoparticles and biologics). Furthermore, with advances in inducible pluripotent stem cell technology (iPSC), pharmaceutical companies can access cells from patients to help recreate specific disease phenotypes in MPS platforms. Combining iPSC and MPS technologies will contribute to our understanding of the complexities of neurodegenerative diseases and of the blood brain barrier (BBB) leading to development of enhanced therapeutics.
MeSH term(s)	Animals ; Blood-Brain Barrier ; Drug Discovery ; Humans ; Induced Pluripotent Stem Cells ; Models, Biological ; Translational Medical Research
Language	English
Publishing date	2018-09-22
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	639113-8
ISSN	1872-8294 ; 0169-409X
ISSN (online)	1872-8294
ISSN	0169-409X
DOI	10.1016/j.addr.2018.09.009
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Article ; Online: Iron is a specific cofactor for distinct oxidation- and aggregation-dependent Aβ toxicity mechanisms in a Drosophila model.

Ott, Stanislav / Dziadulewicz, Nikolas / Crowther, Damian C

Disease models & mechanisms

2015 Volume 8, Issue 7, Page(s) 657–667

Abstract: Metals, including iron, are present at high concentrations in amyloid plaques in individuals with Alzheimer's disease, where they are also thought to be cofactors in generating oxidative stress and modulating amyloid formation. In this study, we present ... ...

Abstract	Metals, including iron, are present at high concentrations in amyloid plaques in individuals with Alzheimer's disease, where they are also thought to be cofactors in generating oxidative stress and modulating amyloid formation. In this study, we present data from several Drosophila models of neurodegenerative proteinopathies indicating that the interaction between iron and amyloid beta peptide (Aβ) is specific and is not seen for other aggregation-prone polypeptides. The interaction with iron is likely to be important in the dimerisation of Aβ and is mediated by three N-terminal histidines. Transgenic fly lines systematically expressing all combinations of His>Ala substitutions in Aβ were generated and used to study the pathological role of these residues. Developmental eye phenotypes, longevity and histological examinations indicate that the N-terminal histidines have distinct position-dependent and -independent mechanisms. The former mediate the toxic effects of metals and Aβ aggregation under non-oxidising conditions and the latter are relevant under oxidising conditions. Understanding how Aβ mediates neurotoxic effects in vivo will help to better target pathological pathways using aggregation blockers and metal-modifying agents.
MeSH term(s)	Alzheimer Disease/etiology ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Amino Acid Substitution ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Animals ; Animals, Genetically Modified ; Disease Models, Animal ; Drosophila/genetics ; Drosophila/metabolism ; Female ; Ferritins/metabolism ; Histidine/chemistry ; Humans ; In Vitro Techniques ; Iron/metabolism ; Oxidation-Reduction ; Phenotype ; Protein Aggregates ; Protein Aggregation, Pathological/etiology ; Protein Aggregation, Pathological/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Protein Aggregates ; Recombinant Proteins ; Histidine (4QD397987E) ; Ferritins (9007-73-2) ; Iron (E1UOL152H7)
Language	English
Publishing date	2015-04-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2451104-3
ISSN	1754-8411 ; 1754-8403
ISSN (online)	1754-8411
ISSN	1754-8403
DOI	10.1242/dmm.019042
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Article ; Online: The pro-domains of neurotrophins, including BDNF, are linked to Alzheimer's disease through a toxic synergy with Aβ.

Lim, Jung Yeon / Reighard, Charles P / Crowther, Damian C

Human molecular genetics

2015 Volume 24, Issue 14, Page(s) 3929–3938

Abstract: Brain-derived neurotrophic factor (BDNF) has a crucial role in learning and memory by promoting neuronal survival and modulating synaptic connectivity. BDNF levels are lower in the brains of individuals with Alzheimer's disease (AD), suggesting a ... ...

Abstract	Brain-derived neurotrophic factor (BDNF) has a crucial role in learning and memory by promoting neuronal survival and modulating synaptic connectivity. BDNF levels are lower in the brains of individuals with Alzheimer's disease (AD), suggesting a pathogenic involvement. The Drosophila orthologue of BDNF is the highly conserved Neurotrophin 1 (DNT1). BDNF and DNT1 have the same overall protein structure and can be cleaved, resulting in the conversion of a full-length polypeptide into separate pro- and mature-domains. While the BDNF mature-domain is neuroprotective, the role of the pro-domain is less clear. In flies and mammalian cells, we have identified a synergistic toxic interaction between the amyloid-β peptide (Aβ1-42) and the pro-domains of both DNT1 and BDNF. Specifically, we show that DNT1 pro-domain acquires a neurotoxic activity in the presence of Aβ1-42. In contrast, DNT1 mature-domain is protective against Aβ1-42 toxicity. Likewise, in SH-SY5Y cell culture, BDNF pro-domain is toxic only in the presence of Aβ1-42. Western blots indicate that this synergistic interaction likely results from the Aβ1-42-induced upregulation of the BDNF pro-domain receptor p75(NTR). The clinical relevance of these findings is underlined by a greater than thirty fold increase in the ratio of BDNF pro- to mature-domains in the brains of individuals with AD. This unbalanced BDNF pro:mature-domain ratio in patients represents a possible biomarker of AD and may offer a target for therapeutic intervention.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/genetics ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Animals ; Brain/metabolism ; Brain-Derived Neurotrophic Factor/genetics ; Brain-Derived Neurotrophic Factor/metabolism ; Cell Line, Tumor ; Cell Survival ; Drosophila/genetics ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Female ; Genetic Markers ; Humans ; Male ; Middle Aged ; Nerve Growth Factors/genetics ; Nerve Growth Factors/metabolism ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Interaction Maps ; Receptor, trkB/genetics ; Receptor, trkB/metabolism ; Up-Regulation
Chemical Substances	Amyloid beta-Peptides ; Brain-Derived Neurotrophic Factor ; Drosophila Proteins ; Genetic Markers ; Nerve Growth Factors ; Peptide Fragments ; amyloid beta-protein (1-42) ; neurotrophin 1, Drosophila ; BDNF protein, human (7171WSG8A2) ; Receptor, trkB (EC 2.7.10.1)
Language	English
Publishing date	2015-05-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddv130
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Article ; Online: Metabolic changes may precede proteostatic dysfunction in a Drosophila model of amyloid beta peptide toxicity.

Ott, Stanislav / Vishnivetskaya, Anastasia / Malmendal, Anders / Crowther, Damian C

Neurobiology of aging

2016 Volume 41, Page(s) 39–52

Abstract: Amyloid beta (Aβ) peptide aggregation is linked to the initiation of Alzheimer's disease; accordingly, aggregation-prone isoforms of Aβ, expressed in the brain, shorten the lifespan of Drosophila melanogaster. However, the lethal effects of Aβ are not ... ...

Abstract	Amyloid beta (Aβ) peptide aggregation is linked to the initiation of Alzheimer's disease; accordingly, aggregation-prone isoforms of Aβ, expressed in the brain, shorten the lifespan of Drosophila melanogaster. However, the lethal effects of Aβ are not apparent until after day 15. We used shibire(TS) flies that exhibit a temperature-sensitive paralysis phenotype as a reporter of proteostatic robustness. In this model, we found that increasing age but not Aβ expression lowered the flies' permissive temperature, suggesting that Aβ did not exert its lethal effects by proteostatic disruption. Instead, we observed that chemical challenges, in particular oxidative stressors, discriminated clearly between young (robust) and old (sensitive) flies. Using nuclear magnetic resonance spectroscopy in combination with multivariate analysis, we compared water-soluble metabolite profiles at various ages in flies expressing Aβ in their brains. We observed 2 genotype-linked metabolomic signals, the first reported the presence of any Aβ isoform and the second the effects of the lethal Arctic Aβ. Lethality was specifically associated with signs of oxidative respiration dysfunction and oxidative stress.
MeSH term(s)	Aging/metabolism ; Alzheimer Disease/etiology ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/toxicity ; Animals ; Brain/metabolism ; Disease Models, Animal ; Drosophila melanogaster ; Oxidative Stress ; Protein Isoforms/metabolism ; Protein Isoforms/toxicity ; Proteostasis Deficiencies/etiology ; Proteostasis Deficiencies/metabolism ; Temperature
Chemical Substances	Amyloid beta-Peptides ; Protein Isoforms
Language	English
Publishing date	2016-05
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.2016.01.009
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