scholarly journals In Vivo Imaging of Axonal and Dendritic Structures in Neonatal Mouse Cortex

2013 ◽  
Vol 2014 (1) ◽  
pp. pdb.prot080150 ◽  
Author(s):  
Alberto Cruz-Martin ◽  
Carlos Portera-Cailliau
2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Nicolas Snaidero ◽  
Martina Schifferer ◽  
Aleksandra Mezydlo ◽  
Bernard Zalc ◽  
Martin Kerschensteiner ◽  
...  

Abstract Myelin, rather than being a static insulator of axons, is emerging as an active participant in circuit plasticity. This requires precise regulation of oligodendrocyte numbers and myelination patterns. Here, by devising a laser ablation approach of single oligodendrocytes, followed by in vivo imaging and correlated ultrastructural reconstructions, we report that in mouse cortex demyelination as subtle as the loss of a single oligodendrocyte can trigger robust cell replacement and remyelination timed by myelin breakdown. This results in reliable reestablishment of the original myelin pattern along continuously myelinated axons, while in parallel, patchy isolated internodes emerge on previously unmyelinated axons. Therefore, in mammalian cortex, internodes along partially myelinated cortical axons are typically not reestablished, suggesting that the cues that guide patchy myelination are not preserved through cycles of de- and remyelination. In contrast, myelin sheaths forming continuous patterns show remarkable homeostatic resilience and remyelinate with single axon precision.


2017 ◽  
Vol 7 (2) ◽  
pp. 17153-17153 ◽  
Author(s):  
Yan-Jie Zhao ◽  
Ting-Ting Yu ◽  
Chao Zhang ◽  
Zhao Li ◽  
Qing-Ming Luo ◽  
...  

Abstract Imaging cells and microvasculature in the living brain is crucial to understanding an array of neurobiological phenomena. Here, we introduce a skull optical clearing window for imaging cortical structures at synaptic resolution. Combined with two-photon microscopy, this technique allowed us to repeatedly image neurons, microglia and microvasculature of mice. We applied it to study the plasticity of dendritic spines in critical periods and to visualize dendrites and microglia after laser ablation. Given its easy handling and safety, this method holds great promise for application in neuroscience research.


PLoS ONE ◽  
2010 ◽  
Vol 5 (5) ◽  
pp. e10589 ◽  
Author(s):  
Vivek K. Unni ◽  
Tamily A. Weissman ◽  
Edward Rockenstein ◽  
Eliezer Masliah ◽  
Pamela J. McLean ◽  
...  

2018 ◽  
Vol 7 (1) ◽  
Author(s):  
Yan-Jie Zhao ◽  
Ting-Ting Yu ◽  
Chao Zhang ◽  
Zhao Li ◽  
Qing-Ming Luo ◽  
...  

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.


2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S588-S588
Author(s):  
Vladimir Kepe ◽  
Gregory M Cole ◽  
Jie Liu ◽  
Dorothy G Flood ◽  
Stephen P Trusko ◽  
...  

2016 ◽  
Vol 54 (12) ◽  
pp. 1343-1404
Author(s):  
A Ghallab ◽  
R Reif ◽  
R Hassan ◽  
AS Seddek ◽  
JG Hengstler

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