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Article ; Online: Lipid Rafts Act as a Common Platform for Amyloid-β Oligomer-Induced Alzheimer's Disease Pathology.

Kawarabayashi, Takeshi / Nakamura, Takumi / Sato, Kaoru / Seino, Yusuke / Ichii, Sadanobu / Nakahata, Naoko / Takatama, Masamitsu / Westaway, David / George-Hyslop, Peter St / Shoji, Mikio

Journal of Alzheimer's disease : JAD

2022 Volume 87, Issue 3, Page(s) 1189–1203

Abstract: Background: Amyloid-β (Aβ) oligomers induce the overproduction of phosphorylated tau and neurodegeneration. These cascades gradually cause cognitive impairment in Alzheimer's disease (AD). While each pathological event in AD has been studied in detail ... ...

Abstract	Background: Amyloid-β (Aβ) oligomers induce the overproduction of phosphorylated tau and neurodegeneration. These cascades gradually cause cognitive impairment in Alzheimer's disease (AD). While each pathological event in AD has been studied in detail separately, the spatial and temporal relationships between pathological events in AD remain unclear. Objective: We demonstrated that lipid rafts function as a common platform for the pathological cascades of AD. Methods: Cellular and synaptosomal lipid rafts were prepared from the brains of Aβ amyloid model mice (Tg2576 mice) and double transgenic mice (Tg2576 x TgTauP301L mice) and longitudinally analyzed. Results: Aβ dimers, the cellular prion protein (PrPc), and Aβ dimer/PrPc complexes were detected in the lipid rafts. The levels of Fyn, the phosphorylated NR2B subunit of the N-methyl-D-aspartate receptor, glycogen synthase kinase 3β, total tau, phosphorylated tau, and tau oligomers increased with Aβ dimer accumulation in both the cellular and synaptosomal lipid rafts. Increases in the levels of these molecules were first seen at 6 months of age and corresponded with the early stages of Aβ accumulation in the amyloid model mice. Conclusion: Lipid rafts act as a common platform for the progression of AD pathology. The findings of this study suggest a novel therapeutic approach to AD, involving the modification of lipid raft components and the inhibition of their roles in the sequential pathological events of AD.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/analysis ; Amyloid beta-Peptides/metabolism ; Animals ; Disease Models, Animal ; Membrane Microdomains/metabolism ; Membrane Microdomains/pathology ; Mice ; Mice, Transgenic ; Phosphorylation ; Prion Proteins/analysis ; Prion Proteins/metabolism ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Prion Proteins ; tau Proteins
Language	English
Publishing date	2022-04-16
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-215662
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Article ; Online: Biomolecular condensate phase diagrams with a combinatorial microdroplet platform.

Arter, William E / Qi, Runzhang / Erkamp, Nadia A / Krainer, Georg / Didi, Kieran / Welsh, Timothy J / Acker, Julia / Nixon-Abell, Jonathan / Qamar, Seema / Guillén-Boixet, Jordina / Franzmann, Titus M / Kuster, David / Hyman, Anthony A / Borodavka, Alexander / George-Hyslop, Peter St / Alberti, Simon / Knowles, Tuomas P J

Nature communications

2022 Volume 13, Issue 1, Page(s) 7845

Abstract: The assembly of biomolecules into condensates is a fundamental process underlying the organisation of the intracellular space and the regulation of many cellular functions. Mapping and characterising phase behaviour of biomolecules is essential to ... ...

Abstract	The assembly of biomolecules into condensates is a fundamental process underlying the organisation of the intracellular space and the regulation of many cellular functions. Mapping and characterising phase behaviour of biomolecules is essential to understand the mechanisms of condensate assembly, and to develop therapeutic strategies targeting biomolecular condensate systems. A central concept for characterising phase-separating systems is the phase diagram. Phase diagrams are typically built from numerous individual measurements sampling different parts of the parameter space. However, even when performed in microwell plate format, this process is slow, low throughput and requires significant sample consumption. To address this challenge, we present here a combinatorial droplet microfluidic platform, termed PhaseScan, for rapid and high-resolution acquisition of multidimensional biomolecular phase diagrams. Using this platform, we characterise the phase behaviour of a wide range of systems under a variety of conditions and demonstrate that this approach allows the quantitative characterisation of the effect of small molecules on biomolecular phase transitions.
MeSH term(s)	Biomolecular Condensates ; Intracellular Space ; Microfluidics ; Phase Transition
Language	English
Publishing date	2022-12-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-35265-7
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Article ; Online: Beta amyloid aggregates induce sensitised TLR4 signalling causing long-term potentiation deficit and rat neuronal cell death.

Hughes, Craig / Choi, Minee L / Yi, Jee-Hyun / Kim, Seung-Chan / Drews, Anna / George-Hyslop, Peter St / Bryant, Clare / Gandhi, Sonia / Cho, Kwangwook / Klenerman, David

Communications biology

2020 Volume 3, Issue 1, Page(s) 79

Abstract: The molecular events causing memory loss and neuronal cell death in Alzheimer's disease (AD) over time are still unknown. Here we found that picomolar concentrations of soluble oligomers of synthetic beta amyloid (Aβ42) aggregates incubated with BV2 ... ...

Abstract	The molecular events causing memory loss and neuronal cell death in Alzheimer's disease (AD) over time are still unknown. Here we found that picomolar concentrations of soluble oligomers of synthetic beta amyloid (Aβ42) aggregates incubated with BV2 cells or rat astrocytes caused a sensitised response of Toll-like receptor 4 (TLR4) with time, leading to increased production of TNF-α. Aβ aggregates caused long term potentiation (LTP) deficit in hippocampal slices and predominantly neuronal cell death in co-cultures of astrocytes and neurons, which was blocked by TLR4 antagonists. Soluble Aβ aggregates cause LTP deficit and neuronal death via an autocrine/paracrine mechanism due to TLR4 signalling. These findings suggest that the TLR4-mediated inflammatory response may be a key pathophysiological process in AD.
MeSH term(s)	Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/pharmacology ; Amyloid beta-Peptides/physiology ; Animals ; Animals, Newborn ; Cell Death/drug effects ; Cells, Cultured ; Embryo, Mammalian ; Long-Term Potentiation/drug effects ; Male ; Mice ; Neurons/drug effects ; Neurons/physiology ; Protein Aggregates/physiology ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/physiopathology ; Protein Aggregation, Pathological/psychology ; Rats ; Rats, Sprague-Dawley ; Rats, Wistar ; Signal Transduction/drug effects ; Toll-Like Receptor 4/metabolism
Chemical Substances	Amyloid beta-Peptides ; Protein Aggregates ; Toll-Like Receptor 4
Language	English
Publishing date	2020-02-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-020-0792-9
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Article ; Online: Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition.

Shen, Yi / Ruggeri, Francesco Simone / Vigolo, Daniele / Kamada, Ayaka / Qamar, Seema / Levin, Aviad / Iserman, Christiane / Alberti, Simon / George-Hyslop, Peter St / Knowles, Tuomas P J

Nature nanotechnology

2020 Volume 15, Issue 10, Page(s) 841–847

Abstract: Membrane-less organelles resulting from liquid-liquid phase separation of biopolymers into intracellular condensates control essential biological functions, including messenger RNA processing, cell signalling and ... ...

Abstract	Membrane-less organelles resulting from liquid-liquid phase separation of biopolymers into intracellular condensates control essential biological functions, including messenger RNA processing, cell signalling and embryogenesis
MeSH term(s)	Animals ; Biomechanical Phenomena ; Bombyx/chemistry ; Cell Line ; Fibroins/chemistry ; Peptides/chemistry ; Phase Transition ; Protein Aggregates ; Proteins/chemistry ; Stress, Mechanical ; Tensile Strength ; Thermodynamics
Chemical Substances	Peptides ; Protein Aggregates ; Proteins ; Fibroins (9007-76-5)
Language	English
Publishing date	2020-07-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2254964-X
ISSN	1748-3395 ; 1748-3387
ISSN (online)	1748-3395
ISSN	1748-3387
DOI	10.1038/s41565-020-0731-4
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Article ; Online: Z-α

Chambers, Joseph E / Zubkov, Nikita / Kubánková, Markéta / Nixon-Abell, Jonathon / Mela, Ioanna / Abreu, Susana / Schwiening, Max / Lavarda, Giulia / López-Duarte, Ismael / Dickens, Jennifer A / Torres, Tomás / Kaminski, Clemens F / Holt, Liam J / Avezov, Edward / Huntington, James A / George-Hyslop, Peter St / Kuimova, Marina K / Marciniak, Stefan J

Science advances

2022 Volume 8, Issue 14, Page(s) eabm2094

Abstract: Misfolding of secretory proteins in the endoplasmic reticulum (ER) features in many human diseases. In ... ...

Abstract	Misfolding of secretory proteins in the endoplasmic reticulum (ER) features in many human diseases. In α
Language	English
Publishing date	2022-04-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.abm2094
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Article ; Online: Genetic and epigenetic study of an Alzheimer's disease family with monozygotic triplets.

Zhang, Ming / Dilliott, Allison A / Khallaf, Roaa / Robinson, John F / Hegele, Robert A / Comishen, Michael / Sato, Christine / Tosto, Giuseppe / Reitz, Christiane / Mayeux, Richard / George-Hyslop, Peter St / Freedman, Morris / Rogaeva, Ekaterina

Brain : a journal of neurology

2019 Volume 142, Issue 11, Page(s) 3375–3381

Abstract: Age at onset of Alzheimer's disease is highly variable, and its modifiers (genetic or environmental) could act through epigenetic changes, such as DNA methylation at CpG sites. DNA methylation is also linked to ageing-the strongest Alzheimer's disease ... ...

Abstract	Age at onset of Alzheimer's disease is highly variable, and its modifiers (genetic or environmental) could act through epigenetic changes, such as DNA methylation at CpG sites. DNA methylation is also linked to ageing-the strongest Alzheimer's disease risk factor. DNA methylation age can be calculated using age-related CpGs and might reflect biological ageing. We conducted a clinical, genetic and epigenetic investigation of a unique Ashkenazi Jewish family with monozygotic triplets, two of whom developed Alzheimer's disease at ages 73 and 76, while the third at age 85 has no cognitive complaints or deficits in daily activities. One of their offspring developed Alzheimer's disease at age 50. Targeted sequencing of 80 genes associated with neurodegeneration revealed that the triplets and the affected offspring are heterozygous carriers of the risk APOE ε4 allele, as well as rare substitutions in APP (p.S198P), NOTCH3 (p.H1235L) and SORL1 (p.W1563C). In addition, we catalogued 52 possibly damaging rare variants detected by NeuroX array in affected individuals. Analysis of family members on a genome-wide DNA methylation chip revealed that the DNA methylation age of the triplets was 6-10 years younger than chronological age, while it was 9 years older in the offspring with early-onset Alzheimer's disease, suggesting accelerated ageing.
MeSH term(s)	Age of Onset ; Aged ; Aged, 80 and over ; Aging, Premature/genetics ; Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Apolipoproteins E/genetics ; DNA/genetics ; DNA Methylation ; Epigenesis, Genetic/genetics ; Female ; Genetic Variation ; Genotype ; Heterozygote ; Humans ; Jews ; Neurodegenerative Diseases/diagnostic imaging ; Neurodegenerative Diseases/pathology ; Pedigree ; Tomography, Emission-Computed, Single-Photon ; Tomography, X-Ray Computed ; Triplets/genetics
Chemical Substances	Apolipoproteins E ; DNA (9007-49-2)
Language	English
Publishing date	2019-10-02
Publishing country	England
Document type	Case Reports ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80072-7
ISSN	1460-2156 ; 0006-8950
ISSN (online)	1460-2156
ISSN	0006-8950
DOI	10.1093/brain/awz289
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Article ; Online: A TgCRND8 Mouse Model of Alzheimer's Disease Exhibits Sexual Dimorphisms in Behavioral Indices of Cognitive Reserve.

Granger, Matthew W / Franko, Bettina / Taylor, Matthew W / Messier, Claude / George-Hyslop, Peter St / Bennett, Steffany A L

Journal of Alzheimer's disease : JAD

2016 Volume 51, Issue 3, Page(s) 757–773

Abstract: Cognitive decline is sexually dimorphic in Alzheimer's disease (AD). Men show higher incidences of amnestic mild cognitive impairment yet women disproportionally phenoconvert to AD. It is hypothesized that men maintain greater cognitive reserve than ... ...

Abstract	Cognitive decline is sexually dimorphic in Alzheimer's disease (AD). Men show higher incidences of amnestic mild cognitive impairment yet women disproportionally phenoconvert to AD. It is hypothesized that men maintain greater cognitive reserve than women under comparable amyloid-β (Aβ) challenge. One behavioral aspect of cognitive reserve in mice is the capacity to cope with Aβ-associated stereotypies by switching to increasingly effective navigational search strategies in the Morris water maze. To explore inherent sex differences in this paradigm, however, we require an AβPP mouse model wherein behavioral flexibility is impaired earlier in females than males despite equivalent Aβ load. Here, we show that when F1 C57Bl/6×C3H/HeJ TgCRND8 mice are placed on C57Bl/6 background, N5 Tg males and females exhibit equivalent Aβ pathologies at 2, 4, 6, and 8 months of age yet females display learning and memory deficits earlier than males. We further show that this N5 line does not carry the autosomal recessive pde6brd1 mutation that impairs visual acuity and that the estrous cycle is not disrupted on this genetic background. At 5.5 months of age, Tg males, but not females, compensate for Aβ-associated stereotypic behaviors (i.e., hyperactive tight circling) by alternating navigational search strategies and adopting increasingly productive spatial search strategies. Females fail to overcome Aβ-associated stereotypies and do not efficiently switch from systematic to spatial learning strategies. Together, these data identify a novel AβPP mouse model that can be used for preclinical testing of interventions targeting sexual dimorphisms in behavioral indices of cognitive reserve.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Alzheimer Disease/physiopathology ; Alzheimer Disease/psychology ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Brain/pathology ; Brain/physiopathology ; Cognitive Reserve ; Cyclic Nucleotide Phosphodiesterases, Type 6/genetics ; Cyclic Nucleotide Phosphodiesterases, Type 6/metabolism ; Disease Models, Animal ; Female ; Humans ; Male ; Maze Learning/physiology ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mice, Transgenic ; Plaque, Amyloid/genetics ; Plaque, Amyloid/pathology ; Plaque, Amyloid/physiopathology ; Plaque, Amyloid/psychology ; Psychomotor Performance/physiology ; Sex Characteristics ; Spatial Memory/physiology ; Spatial Navigation/physiology ; Survival Analysis
Chemical Substances	APP protein, human ; Amyloid beta-Protein Precursor ; Cyclic Nucleotide Phosphodiesterases, Type 6 (EC 3.1.4.35) ; PDE6B protein, human (EC 3.1.4.35)
Language	English
Publishing date	2016
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-150587
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Article ; Online: Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.

Krainer, Georg / Welsh, Timothy J / Joseph, Jerelle A / Espinosa, Jorge R / Wittmann, Sina / de Csilléry, Ella / Sridhar, Akshay / Toprakcioglu, Zenon / Gudiškytė, Giedre / Czekalska, Magdalena A / Arter, William E / Guillén-Boixet, Jordina / Franzmann, Titus M / Qamar, Seema / George-Hyslop, Peter St / Hyman, Anthony A / Collepardo-Guevara, Rosana / Alberti, Simon / Knowles, Tuomas P J

Nature communications

2021 Volume 12, Issue 1, Page(s) 1085

Abstract: Liquid-liquid phase separation of proteins underpins the formation of membraneless compartments in living cells. Elucidating the molecular driving forces underlying protein phase transitions is therefore a key objective for understanding biological ... ...

Abstract	Liquid-liquid phase separation of proteins underpins the formation of membraneless compartments in living cells. Elucidating the molecular driving forces underlying protein phase transitions is therefore a key objective for understanding biological function and malfunction. Here we show that cellular proteins, which form condensates at low salt concentrations, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, can reenter a phase-separated regime at high salt concentrations. By bringing together experiments and simulations, we demonstrate that this reentrant phase transition in the high-salt regime is driven by hydrophobic and non-ionic interactions, and is mechanistically distinct from the low-salt regime, where condensates are additionally stabilized by electrostatic forces. Our work thus sheds light on the cooperation of hydrophobic and non-ionic interactions as general driving forces in the condensation process, with important implications for aberrant function, druggability, and material properties of biomolecular condensates.
MeSH term(s)	Animals ; Annexins/chemistry ; Cell Cycle Proteins/chemistry ; DNA-Binding Proteins/chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Molecular Dynamics Simulation ; Phase Transition ; Proteins/chemistry ; RNA-Binding Protein FUS/chemistry ; SOXB1 Transcription Factors/chemistry ; Sf9 Cells ; Spodoptera ; Static Electricity ; Transcription Factors/chemistry
Chemical Substances	Annexins ; BRD4 protein, human ; Cell Cycle Proteins ; DNA-Binding Proteins ; Proteins ; RNA-Binding Protein FUS ; SOX2 protein, human ; SOXB1 Transcription Factors ; TARDBP protein, human ; Transcription Factors
Language	English
Publishing date	2021-02-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-21181-9
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Article ; Online: Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition

Shen, Yi / Ruggeri, Francesco Simone / Vigolo, Daniele / Kamada, Ayaka / Qamar, Seema / Levin, Aviad / Iserman, Christiane / Alberti, Simon / George-Hyslop, Peter St / Knowles, Tuomas P.J.

Nature Nanotechnology

2020 Volume 15, Issue 10

Abstract: Membrane-less organelles resulting from liquid–liquid phase separation of biopolymers into intracellular condensates control essential biological functions, including messenger RNA processing, cell signalling and embryogenesis1–4. It has recently been ... ...

Abstract	Membrane-less organelles resulting from liquid–liquid phase separation of biopolymers into intracellular condensates control essential biological functions, including messenger RNA processing, cell signalling and embryogenesis1–4. It has recently been discovered that several such protein condensates can undergo a further irreversible phase transition, forming solid nanoscale aggregates associated with neurodegenerative disease5–7. While the irreversible gelation of protein condensates is generally related to malfunction and disease, one case where the liquid-to-solid transition of protein condensates is functional, however, is that of silk spinning8,9. The formation of silk fibrils is largely driven by shear, yet it is not known what factors control the pathological gelation of functional condensates. Here we demonstrate that four proteins and one peptide system, with no function associated with fibre formation, have a strong propensity to undergo a liquid-to-solid transition when exposed to even low levels of mechanical shear once present in their liquid–liquid phase separated form. Using microfluidics to control the application of shear, we generated fibres from single-protein condensates and characterized their structural and material properties as a function of shear stress. Our results reveal generic backbone–backbone hydrogen bonding constraints as a determining factor in governing this transition. These observations suggest that shear can play an important role in the irreversible liquid-to-solid transition of protein condensates, shed light on the role of physical factors in driving this transition in protein aggregation-related diseases and open a new route towards artificial shear responsive biomaterials.
Keywords	Life Science
Subject code	612
Language	English
Publishing country	nl
Document type	Article ; Online
ZDB-ID	2254964-X
ISSN	1748-3395 ; 1748-3387
ISSN (online)	1748-3395
ISSN	1748-3387
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Genetic complexity of Alzheimer's disease: successes and challenges.

Rogaeva, Ekaterina / Kawarai, Toshitaka / George-Hyslop, Peter St

Journal of Alzheimer's disease : JAD

2006 Volume 9, Issue 3 Suppl, Page(s) 381–387

Abstract: About 1% of Alzheimer's Disease (AD) cases have an early-onset autosomal dominant familial form of the disease, genetic analyses of which have found three causal genes: amyloid beta-protein precursor (AbetaPP), presenilin 1 (PS1) and presenilin 2 (PS2). ... ...

Abstract	About 1% of Alzheimer's Disease (AD) cases have an early-onset autosomal dominant familial form of the disease, genetic analyses of which have found three causal genes: amyloid beta-protein precursor (AbetaPP), presenilin 1 (PS1) and presenilin 2 (PS2). The APOE gene is the only robustly replicated risk factor for the common form of AD with onset after 65 years of age. In at least half of the AD cases, there is no known cause of the disease. Here we provide an overview on known AD-linked genes and discuss the strategies of searching for novel AD genetic risk factors.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Apolipoproteins E/genetics ; Apolipoproteins E/metabolism ; Brain/metabolism ; Brain/pathology ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Presenilin-1 ; Presenilin-2
Chemical Substances	Amyloid beta-Protein Precursor ; Apolipoproteins E ; Membrane Proteins ; PSEN1 protein, human ; PSEN2 protein, human ; Presenilin-1 ; Presenilin-2
Language	English
Publishing date	2006-07-10
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/jad-2006-9s343
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