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Correlative optical photothermal infrared and X-ray fluorescence for chemical imaging of trace elements and relevant molecular structures directly in neurons

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Light(Science & Applications) 2021年第8期10卷 1536-1545页

作者： Nadja Gustavsson Agnes Paulus Isak Martinsson Anders Engdahl kadda Medjoubi konstantin klementiev Andrea Somogyi Tomas Deierborg Ferenc Borondics gunnar k gouras Oxana klementieva Medical Microspearoscopy Department of Experimental Medical ScienceLund University22180 LundSweden. Experimental Neuroinflammation Lab Department of Experimental Medical ScienceLund University22180 LundSweden. Experimental Dementia Research Department of Experimental Medical ScienceLund University22180 LundSweden. Synchrotron SOLEIL L'Orme des Merisiers91192 Gif Sur Yvette CedexFrance. MAX IV Laboratory 22100 LundSweden. Lund Institute for advanced Neutron and X-ray Science(LINXS) 22370 LundSweden

Alzheimer's disease(AD)is the most common cause of dementia,costing about 1%of the global economy.Failures of clinical trials targeting amyloid-βprotein(Aβ),a key trigger of AD,have been explained by drug inefficiency regardless of the mechanisms of amyloid neurotoxicity,which are very difficult to address by available technologies.Here,we combine two imaging modalities that stand at opposite ends of the electromagnetic spectrum,and therefore,can be used as complementary tools to assess structural and chemical information directly in a single neuron.Combining label-free super-resolution microspectroscopy for sub-cellular imaging based on novel optical photothermal infrared(O-PTIR)and synchrotron-based X-ray fluorescence(S-XRF)nano-imaging techniques,we capture elemental distribution and fibrillary forms of amyloid-βproteins in the same neurons at an unprecedented resolution.Our results reveal that in primary AD-like neurons,iron clusters co-localize with elevated amyloidβ-sheet structures and oxidized lipids.Overall,our O-PTIR/S-XRF results motivate using high-resolution multimodal microspectroscopic approaches to understand the role of molecular structures and trace elements within a single neuronal cell.

关键词： elevated elements complementary

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Differential seeding and propagating efficiency ofα-synuclein strains generated in different conditions

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Translational Neurodegeneration 2021年第2期10卷 257-271页

作者： Di Liu Jian-Jun Guo Ji-Hui Su Alexander Svanbergsson Lin Yuan Caroline Haikal Wen Li gunnar gouras Jia-Yi Li Institute of Neuroscience College of Life and Health SciencesNortheastern UniversityShenyang 110169China Neural Plasticity and Repair Unit Wallenberg Neuroscience CenterLund UniversityBMC A1022184 LundSweden Experimental Dementia Research Lund UniversityBMC B1122184 LundSweden Institute of Health Sciences China Medical UniversityShenyang 110122China

Background:Accumulation of alpha-synuclein(α-syn)is a main pathological hallmark of Parkinson’s and related diseases,which are collectively known as synucleinopathies.Growing evidence has supported that the same protein can induce remarkably distinct pathological progresses and disease phenotypes,suggesting the existence of strain difference amongα-syn fibrils.Previous studies have shown thatα-syn pathology can propagate from the peripheral nervous system(PNS)to the central nervous system(CNS)in a“prion-like”manner.However,the difference of the propagation potency from the periphery to CNS among differentα-syn strains remains unknown and the effect of different generation processes of these strains on the potency of seeding and propagation remains to be revealed in more detail.Methods:Three strains of preformedα-syn fibrils(PFFs)were generated in different buffer conditions which varied in pH and ionic concentrations.Theα-syn PFFs were intramuscularly(IM)injected into a novel bacterial artificial chromosome(BAC)transgenic mouse line that expresses wild-type humanα-syn,and the efficiency of seeding and propagation of these PFFs from the PNS to the CNS was evaluated.Results:The three strains ofα-syn PFFs triggered distinct propagation patterns.The fibrils generated in mildly acidic buffer led to the most severeα-syn pathology,degeneration of motor neurons and microgliosis in the spinal cord.Conclusions:The differentα-syn conformers generated in different conditions exhibited strain-specific pathology and propagation patterns from the periphery to the CNS,which further supports the view thatα-syn strains may be responsible for the heterogeneity of pathological features and disease progresses among synucleinopathies.

关键词： α-Synuclein Strains Prion-like propagation Parkinson’s disease

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