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Article ; Online: Giant cell arteritis presenting with unilateral sixth nerve palsy.

Colquhoun, Matthew / Alegre Abarrategui, Javier / Shahzad, Muhammad Ibrahim / Ellis, Benjamin

BMJ case reports

2023 Volume 16, Issue 5

Abstract: Giant cell arteritis (GCA) usually presents with headache, scalp tenderness and raised inflammatory markers. GCA presenting with a clinically evident cranial nerve palsy is rare and may result in a delayed or missed diagnosis if not suspected. We present ...

Abstract	Giant cell arteritis (GCA) usually presents with headache, scalp tenderness and raised inflammatory markers. GCA presenting with a clinically evident cranial nerve palsy is rare and may result in a delayed or missed diagnosis if not suspected. We present the rare case of a woman in her 70s with histologically confirmed GCA presenting with a unilateral sixth nerve palsy, which responded to treatment with high-dose oral prednisolone.
MeSH term(s)	Female ; Humans ; Giant Cell Arteritis ; Abducens Nerve Diseases ; Headache ; Missed Diagnosis ; Pain
Language	English
Publishing date	2023-05-23
Publishing country	England
Document type	Case Reports ; Journal Article
ISSN	1757-790X
ISSN (online)	1757-790X
DOI	10.1136/bcr-2022-253484
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Article ; Online: Beyond Strains: Molecular Diversity in Alpha-Synuclein at the Center of Disease Heterogeneity.

Wojewska, Marcelina J / Otero-Jimenez, Maria / Guijarro-Nuez, Jose / Alegre-Abarrategui, Javier

International journal of molecular sciences

2023 Volume 24, Issue 17

Abstract: Alpha-synucleinopathies (α-synucleinopathies) such as Parkinson's disease (PD), Parkinson's disease dementia (PDD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA) are all characterized by aggregates of alpha-synuclein (α-syn), but ... ...

Abstract	Alpha-synucleinopathies (α-synucleinopathies) such as Parkinson's disease (PD), Parkinson's disease dementia (PDD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA) are all characterized by aggregates of alpha-synuclein (α-syn), but display heterogeneous clinical and pathological phenotypes. The mechanism underlying this heterogeneity is thought to be due to diversity in the α-syn strains present across the diseases. α-syn obtained from the post-mortem brain of patients who lived with these conditions is heterogenous, and displays a different protease sensitivity, ultrastructure, cytotoxicity, and seeding potential. The primary aim of this review is to summarize previous studies investigating these concepts, which not only reflect the idea of different syn strains being present, but demonstrate that each property explains a small part of a much larger puzzle. Strains of α-syn appear at the center of the correlation between α-syn properties and the disease phenotype, likely influenced by external factors. There are considerable similarities in the properties of disease-specific α-syn strains, but MSA seems to consistently display more aggressive traits. Elucidating the molecular underpinnings of heterogeneity amongst α-synucleinopathies holds promise for future clinical translation, allowing for the development of personalized medicine approaches tackling the root cause of each α-synucleinopathy.
MeSH term(s)	Humans ; alpha-Synuclein/genetics ; Synucleinopathies ; Dementia ; Parkinson Disease/genetics ; Multiple System Atrophy/genetics
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2023-08-25
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/ijms241713199
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Article ; Online: Alpha-Synuclein Proximity Ligation Assay (AS-PLA) in Brain Sections to Probe for Alpha-Synuclein Oligomers.

Roberts, Rosalind F / Bengoa-Vergniory, Nora / Alegre-Abarrategui, Javier

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

2019 Volume 1948, Page(s) 69–76

Abstract: Alpha-synuclein oligomers are thought to be toxic mediators of Parkinson's disease and other alpha-synucleinopathies, but their histological detection in situ in diseased brain has been a challenge in the field for some time. Here we describe a method, ... ...

Abstract	Alpha-synuclein oligomers are thought to be toxic mediators of Parkinson's disease and other alpha-synucleinopathies, but their histological detection in situ in diseased brain has been a challenge in the field for some time. Here we describe a method, the alpha-synuclein proximity ligation assay (AS-PLA), to detect alpha-synuclein oligomers in paraffin-embedded brain sections. Using AS-PLA previously unobserved alpha-synuclein oligomeric pathology is revealed.
MeSH term(s)	Brain/metabolism ; Humans ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Protein Aggregates ; Protein Aggregation, Pathological/metabolism ; Protein Multimerization ; alpha-Synuclein/chemistry ; alpha-Synuclein/metabolism
Chemical Substances	Protein Aggregates ; alpha-Synuclein
Language	English
Publishing date	2019-02-15
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-9124-2_7
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Article ; Online: A rare case of atypical skull base meningioma with perineural spread.

Walton, Henry / Morley, Simon / Alegre-Abarrategui, Javier

Journal of radiology case reports

2015 Volume 9, Issue 12, Page(s) 1–14

Abstract: Atypical meningioma is a rare cause of perineural tumour spread. In this report, we present the case of a 46-year-old female with an atypical meningioma of the skull base demonstrating perineural tumour spread. We describe the imaging features of this ... ...

Abstract	Atypical meningioma is a rare cause of perineural tumour spread. In this report, we present the case of a 46-year-old female with an atypical meningioma of the skull base demonstrating perineural tumour spread. We describe the imaging features of this condition and its distinguishing features from other tumours exhibiting perineural spread.
Language	English
Publishing date	2015-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2586384-8
ISSN	1943-0922 ; 1943-0922
ISSN (online)	1943-0922
ISSN	1943-0922
DOI	10.3941/jrcr.v9i12.2648
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Article ; Online: RNA dysfunction and aggrephagy at the centre of an amyotrophic lateral sclerosis/frontotemporal dementia disease continuum.

Thomas, Matthew / Alegre-Abarrategui, Javier / Wade-Martins, Richard

Brain : a journal of neurology

2013 Volume 136, Issue Pt 5, Page(s) 1345–1360

Abstract: Amyotrophic lateral sclerosis and frontotemporal dementia form two poles of a genetically, pathologically and clinically-related disease continuum. Analysis of the genes and proteins at the heart of this continuum highlights dysfunction of RNA processing ...

Abstract	Amyotrophic lateral sclerosis and frontotemporal dementia form two poles of a genetically, pathologically and clinically-related disease continuum. Analysis of the genes and proteins at the heart of this continuum highlights dysfunction of RNA processing and aggrephagy as crucial disease-associated pathways. TAR DNA binding protein and fused in sarcoma (FUS) are both RNA processing proteins whose dysfunction impacts on global cellular RNA regulation. The recent discovery that expression of repeat expansions in the C9orf72 gene may induce RNA foci that could sequester RNA binding proteins such as TAR DNA binding protein and FUS highlights a further possibly important mechanism of RNA dysfunction in disease. Furthermore, sequestration of key RNA binding proteins may also play an important role in sporadic disease due to the association of TAR DNA binding protein and FUS with stress granules. In a further functional convergence, ubiquilin 2, p62, valosin-containing protein and optineurin are all linked to aggrephagy, a cargo-specific subtype of autophagy important for degrading ubiquitinated target proteins through the lysosome. Notably these two key pathways interact; TAR DNA binding protein and FUS bind and regulate key aggrephagy-related genes whereas dysfunction of aggrephagy leads to cytoplasmic relocalization and aggregation of TAR DNA binding protein. The convergence of amyotrophic lateral sclerosis and frontotemporal dementia linked genes into these two pathways highlights RNA dysfunction and aggrephagy as promising areas for drug discovery. In this review we discuss the importance of each of these pathways and suggest mechanisms by which they may cause both sporadic and familial disease.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/physiopathology ; Animals ; Autophagy/genetics ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/physiopathology ; Humans ; RNA Processing, Post-Transcriptional/genetics ; Signal Transduction/genetics
Language	English
Publishing date	2013-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80072-7
ISSN	1460-2156 ; 0006-8950
ISSN (online)	1460-2156
ISSN	0006-8950
DOI	10.1093/brain/awt030
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Article ; Online: Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain.

Roberts, Rosalind F / Wade-Martins, Richard / Alegre-Abarrategui, Javier

Brain : a journal of neurology

2015 Volume 138, Issue Pt 6, Page(s) 1642–1657

Abstract: Oligomeric forms of alpha-synuclein are emerging as key mediators of pathogenesis in Parkinson's disease. Our understanding of the exact contribution of alpha-synuclein oligomers to disease is limited by the lack of a technique for their specific ... ...

Abstract	Oligomeric forms of alpha-synuclein are emerging as key mediators of pathogenesis in Parkinson's disease. Our understanding of the exact contribution of alpha-synuclein oligomers to disease is limited by the lack of a technique for their specific detection. We describe a novel method, the alpha-synuclein proximity ligation assay, which specifically recognizes alpha-synuclein oligomers. In a blinded study with post-mortem brain tissue from patients with Parkinson's disease (n = 8, age range 73-92 years, four males and four females) and age- and sex-matched controls (n = 8), we show that the alpha-synuclein proximity ligation assay reveals previously unrecognized pathology in the form of extensive diffuse deposition of alpha-synuclein oligomers. These oligomers are often localized, in the absence of Lewy bodies, to neuroanatomical regions mildly affected in Parkinson's disease. Diffuse alpha-synuclein proximity ligation assay signal is significantly more abundant in patients compared to controls in regions including the cingulate cortex (1.6-fold increase) and the reticular formation of the medulla (6.5-fold increase). In addition, the alpha-synuclein proximity ligation assay labels very early perikaryal aggregates in morphologically intact neurons that may precede the development of classical Parkinson's disease lesions, such as pale bodies or Lewy bodies. Furthermore, the alpha-synuclein proximity ligation assay preferentially detects early-stage, loosely compacted lesions such as pale bodies in patient tissue, whereas Lewy bodies, considered heavily compacted late lesions are only very exceptionally stained. The alpha-synuclein proximity ligation assay preferentially labels alpha-synuclein oligomers produced in vitro compared to monomers and fibrils, while stained oligomers in human brain display a distinct intermediate proteinase K resistance, suggesting the detection of a conformer that is different from both physiological, presynaptic alpha-synuclein (proteinase K-sensitive) and highly aggregated alpha-synuclein within Lewy bodies (proteinase K-resistant). These disease-associated conformers represent previously undetected Parkinson's disease pathology uncovered by the alpha-synuclein proximity ligation assay.
MeSH term(s)	Aged ; Aged, 80 and over ; Case-Control Studies ; Early Diagnosis ; Female ; Fluorescent Antibody Technique ; Gyrus Cinguli/metabolism ; Gyrus Cinguli/pathology ; HEK293 Cells ; Humans ; Lewy Bodies/metabolism ; Lewy Bodies/pathology ; Male ; Neurons/metabolism ; Parkinson Disease/diagnosis ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Polymerization ; Reticular Formation/metabolism ; Reticular Formation/pathology ; alpha-Synuclein/chemistry ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2015-03-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Validation Study
ZDB-ID	80072-7
ISSN	1460-2156 ; 0006-8950
ISSN (online)	1460-2156
ISSN	0006-8950
DOI	10.1093/brain/awv040
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Article ; Online: Tau-proximity ligation assay reveals extensive previously undetected pathology prior to neurofibrillary tangles in preclinical Alzheimer's disease.

Bengoa-Vergniory, Nora / Velentza-Almpani, Elisavet / Silva, Ana Maria / Scott, Connor / Vargas-Caballero, Mariana / Sastre, Magdalena / Wade-Martins, Richard / Alegre-Abarrategui, Javier

Acta neuropathologica communications

2021 Volume 9, Issue 1, Page(s) 18

Abstract: Background: Multimerization is a key process in prion-like disorders such as Alzheimer's disease (AD), since it is a requirement for self-templating tau and beta-amyloid amyloidogenesis. AT8-immunohistochemistry for hyperphosphorylated tau is currently ... ...

Abstract	Background: Multimerization is a key process in prion-like disorders such as Alzheimer's disease (AD), since it is a requirement for self-templating tau and beta-amyloid amyloidogenesis. AT8-immunohistochemistry for hyperphosphorylated tau is currently used for the diagnosis and staging of tau pathology. Given that tau-tau interactions can occur in the absence of hyperphosphorylation or other post-translational modifications (PTMs), the direct visualization of tau multimerization could uncover early pathological tau multimers. Methods: Here, we used bimolecular fluorescent complementation, rapamycin-dependent FKBP/FRB-tau interaction and transmission electron microscopy to prove the in vitro specificity of tau-proximity ligation assay (tau-PLA). We then analyzed MAPT KO and P301S transgenic mice, and human hippocampus and temporal isocortex of all Braak stages with tau-PLA and compared it with immunohistochemistry for the diagnostic antibody AT8, the early phosphorylation-dependent AT180, and the conformational-dependent antibody MC1. Finally, we performed proteinase-K treatment to infer the content of amyloidogenic beta-sheet fold. Results: Our novel tau-proximity ligation assay (tau-PLA) directly visualized tau-tau interactions in situ, and exclusively recognized tau multimers but not monomers. It elicited no signal in MAPT KO mouse brains, but extensively labelled P301S transgenic mice and AD brain. Two groups of structures were detected, a previously unreported widespread small-sized diffuse pathology and large, neurofibrillary-like lesions. Tau-PLA-labelled diffuse pathology appeared from the earliest Braak stages, mostly unaccompanied by tangle-like tau-immunohistochemistry, being significantly more sensitive than any small-sized dot-/thread-like pathology labelled by AT180-, AT8- and MC1-immunohistochemistry in most regions quantified at stages 0-II. Tau-PLA-labelled diffuse pathology was extremely sensitive to Proteinase-K, in contrast to large lesions. Conclusions: Tau-PLA is the first method to directly visualize tau multimers both in vitro and in situ with high specificity. We find that tau multimerization appears extensively from the earliest presymptomatic Braak stages as a previously unreported type of diffuse pathology. Importantly, in our study multimerization is the earliest detectable molecular event of AD tau pathology. Our findings open a new window to the study of early tau pathology, with potential implications in early diagnosis and the design of therapeutic strategies.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Asymptomatic Diseases ; Brain/metabolism ; Brain/pathology ; Humans ; Mice ; Mice, Knockout ; Mice, Transgenic ; Neurofibrillary Tangles/pathology ; Protein Multimerization ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	MAPT protein, human ; Mapt protein, mouse ; tau Proteins
Language	English
Publishing date	2021-01-28
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/s40478-020-01117-y
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Article ; Online: Alpha-synuclein oligomers: a new hope.

Bengoa-Vergniory, Nora / Roberts, Rosalind F / Wade-Martins, Richard / Alegre-Abarrategui, Javier

Acta neuropathologica

2017 Volume 134, Issue 6, Page(s) 819–838

Abstract: Alpha-synuclein is a protein implicated in Parkinson's disease and thought to be one of the main pathological drivers in the disease, although it remains unclear how this protein elicits its neurotoxic effects. Recent findings indicate that the assembly ... ...

Abstract	Alpha-synuclein is a protein implicated in Parkinson's disease and thought to be one of the main pathological drivers in the disease, although it remains unclear how this protein elicits its neurotoxic effects. Recent findings indicate that the assembly of toxic oligomeric species of alpha-synuclein may be one of the key processes for the pathology and spread of the disease. The absence of a sensitive in situ detection method has hindered the study of these oligomeric species and the role they play in the human brain until recently. In this review, we assess the evidence for the toxicity and prion-like activity of oligomeric forms of alpha-synuclein and discuss the advances in our understanding of the role of alpha-synuclein in Parkinson's disease that may be brought about by the specific and sensitive detection of distinct oligomeric species in post-mortem patient brain. Finally, we discuss current approaches being taken to therapeutically target alpha-synuclein oligomers and their implications.
MeSH term(s)	Animals ; Antiparkinson Agents/pharmacology ; Antiparkinson Agents/therapeutic use ; Biomarkers/metabolism ; Humans ; Parkinson Disease/metabolism ; Parkinson Disease/therapy ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/therapy ; alpha-Synuclein/metabolism ; alpha-Synuclein/toxicity
Chemical Substances	Antiparkinson Agents ; Biomarkers ; alpha-Synuclein
Language	English
Publishing date	2017-08-12
Publishing country	Germany
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-017-1755-1
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Article ; Online: Selective vulnerability in α-synucleinopathies.

Alegre-Abarrategui, Javier / Brimblecombe, Katherine R / Roberts, Rosalind F / Velentza-Almpani, Elisavet / Tilley, Bension S / Bengoa-Vergniory, Nora / Proukakis, Christos

Acta neuropathologica

2019 Volume 138, Issue 5, Page(s) 681–704

Abstract: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy are neurodegenerative disorders resulting in progressive motor/cognitive deficits among other symptoms. They are characterised by stereotypical brain cell loss accompanied by the ...

Abstract	Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy are neurodegenerative disorders resulting in progressive motor/cognitive deficits among other symptoms. They are characterised by stereotypical brain cell loss accompanied by the formation of proteinaceous aggregations of the protein α-synuclein (α-syn), being, therefore, termed α-synucleinopathies. Although the presence of α-syn inclusions is a common hallmark of these disorders, the exact nature of the deposited protein is specific to each disease. Different neuroanatomical regions and cellular populations manifest a differential vulnerability to the appearance of protein deposits, cell dysfunction, and cell death, leading to phenotypic diversity. The present review describes the multiple factors that contribute to the selective vulnerability in α-synucleinopathies. We explore the intrinsic cellular properties in the affected regions, including the physiological and pathophysiological roles of endogenous α-syn, the metabolic and genetic build-up of the cells and their connectivity. These factors converge with the variability of the α-syn conformational strains and their spreading capacity to dictate the phenotypic diversity and regional vulnerability of each disease. Finally, we describe the exogenous and environmental factors that potentially contribute by igniting and modulating the differential pathology in α-synucleinopathies. In conclusion, we think that it is the confluence of this disruption of the cellular metabolic state and α-syn structural equilibrium through the anatomical connectivity which appears to initiate cascades of pathological processes triggered by genetic, environmental, or stochastic events that result in the "death by a thousand cuts" profile of α-synucleinopathies.
MeSH term(s)	Animals ; Brain/pathology ; Humans ; Lewy Bodies/pathology ; Lewy Body Disease/pathology ; Multiple System Atrophy/pathology ; Parkinson Disease/pathology ; Synucleinopathies/pathology
Language	English
Publishing date	2019-04-20
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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/s00401-019-02010-2
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Article ; Online: Insights into LRRK2 function and dysfunction from transgenic and knockout rodent models.

Sloan, Maximilian / Alegre-Abarrategui, Javier / Wade-Martins, Richard

Biochemical Society transactions

2012 Volume 40, Issue 5, Page(s) 1080–1085

Abstract: Mutations in the LRRK2 (leucine-rich repeat kinase 2) gene on chromosome 12 cause autosomal dominant PD (Parkinson's disease), which is indistinguishable from sporadic forms of the disease. Numerous attempts have therefore been made to model PD in ... ...

Abstract	Mutations in the LRRK2 (leucine-rich repeat kinase 2) gene on chromosome 12 cause autosomal dominant PD (Parkinson's disease), which is indistinguishable from sporadic forms of the disease. Numerous attempts have therefore been made to model PD in rodents via the transgenic expression of LRRK2 and its mutant variants and to elucidate the function of LRRK2 by knocking out rodent Lrrk2. Although these models often only partially recapitulate PD pathology, they have helped to elucidate both the normal and pathological function of LRRK2. In particular, LRRK2 has been suggested to play roles in cytoskeletal dynamics, synaptic machinery, dopamine homoeostasis and autophagic processes. Our understanding of how these pathways are affected, their contribution towards PD development and their interaction with one another is still incomplete, however. The present review summarizes the findings from LRRK2 rodent models and draws potential connections between the apparently disparate cellular processes altered, in order to better understand the underlying mechanisms of LRRK2 dysfunction and illuminate future therapeutic interventions.
MeSH term(s)	Animals ; Disease Models, Animal ; Gene Deletion ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 ; Mice ; Mice, Knockout ; Mice, Transgenic ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Protein-Serine-Threonine Kinases/deficiency ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism
Chemical Substances	Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1) ; Lrrk2 protein, mouse (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2012-09-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20120151
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