Substitutionally Enhanced STEM (SE-STEM) Imaging of Protein Aggregates Inside Cells

McGuire, Eva; Motskin, Michael; Dobson, Christopher M.; Porter, Andrew C.G.; McComb, David W.

doi:10.1017/s1431927611001747

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“…C = cytoplasm; ES = extracellular space; A = aggregates; PM = plasma membrane; IV = intracellular vesicle; N = nucleus. (p) Included in proceedings of a conference …”

Section: Resultsmentioning

confidence: 99%

“…Acknowledgment. Some data relating to parts of this study have been previously presented at scientific conferences including Figure 1eÀg, 39 Figure 2p, 40 Figure 3d,e, 39 and Supporting Information Figure S3a,b. 39 This research was supported by a Titan Grant EPSRC (EP/C51596X), a European starting grant for AP (Project number 257182), The Wellcome Trust, FEI Life Sciences Division, the BBSRC for L.L.…”

Section: Methodsmentioning

confidence: 96%

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Selenium-Enhanced Electron Microscopic Imaging of Different Aggregate Forms of a Segment of the Amyloid β Peptide in Cells

et al. 2012

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The aggregation of misfolded proteins is a common feature underlying a wide range of age-related degenerative disorders, including Alzheimer's and Parkinson's diseases. A key aspect of understanding the molecular origins of these conditions is to define the manner in which specific types of protein aggregates influence disease pathogenesis through their interactions with cells. We demonstrate how selenium-enhanced electron microscopy (SE-EM), combined with tomographic reconstruction methods, can be used to image, here at a resolution of 5-10 nm, the interaction with human macrophage cells of amyloid aggregates formed from Aβ(25-36), a fragment of the Aβ peptide whose self-assembly is associated with Alzheimer's disease. We find that prefibrillar aggregates and mature fibrils are distributed into distinct subcellular compartments and undergo varying degrees of morphological change over time, observations that shed new light on the origins of their differential toxicity and the mechanisms of their clearance. In addition, the results show that SE-EM provides a powerful and potentially widely applicable means to define the nature and location of protein assemblies in situ and to provide detailed and specific information about their partitioning and processing.

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“…C = cytoplasm; ES = extracellular space; A = aggregates; PM = plasma membrane; IV = intracellular vesicle; N = nucleus. (p) Included in proceedings of a conference …”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 96%

Selenium-Enhanced Electron Microscopic Imaging of Different Aggregate Forms of a Segment of the Amyloid β Peptide in Cells

et al. 2012

View full text Add to dashboard Cite

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Substitutionally Enhanced STEM (SE-STEM) Imaging of Protein Aggregates Inside Cells

Abstract: Extended abstract of a paper presented at Microscopy and Microanalysis 2011 in Nashville, Tennessee, USA, August 7–August 11, 2011.

Cited by 1 publication

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Selenium-Enhanced Electron Microscopic Imaging of Different Aggregate Forms of a Segment of the Amyloid β Peptide in Cells

Selenium-Enhanced Electron Microscopic Imaging of Different Aggregate Forms of a Segment of the Amyloid β Peptide in Cells

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