scholarly journals Dynamic Cell Imaging: application to the diatom Phaeodactylum tricornutum under environmental stresses

2021 ◽  
Author(s):  
Houda Bey ◽  
Florent Charton ◽  
Helena Cruz de Carvalho ◽  
Shun Liu ◽  
Richard G Dorrell ◽  
...  

The dynamic movement of cell organelles is an important and poorly understood component of cellular organisation and metabolism. In this work we present a non-invasive non-destructive method (Dynamic Cell Imaging, DCI) based on light scattering and interferometry to monitor dynamic events within photosynthetic cells using the diatom Phaeodactylum tricornutum as a model system. For this monitoring we acquire few seconds movies of the signals that are related to the motion of dynamic structures within the cell (denoted scatterers), followed by a statistical analysis of each pixel time series. Illuminating P.tricornutum with LEDs of different wavelengths associated to short pulsed or continuous-wave modes of illumination revealed that dynamic movements depend on chloroplast activity, in agreement with the reduction in the number of pixels with dynamic behaviour after addition of photosystemII inhibitors. We studied P. tricornutum under two environmentally relevant stresses, iron and phosphate deficiency. The major dynamic sites were located within lipid droplets and chloroplast envelope membranes. By comparing standard deviation and cumulative sum analysis of the time series, we showed that within the droplets two types of scatterer movement could be observed: random motions (Brownian type) but also anomalous movements corresponding to a drift which may relate to molecular fluxes within a cell. The method appears valuable for studying the effects of various environments on a large variety of microalgae in the laboratory as well as in natural aquatic environments.

2005 ◽  
Vol 94 (12) ◽  
pp. 1203-1212 ◽  
Author(s):  
Doris Cerecedo ◽  
Dalila Martínez-Rojas ◽  
Oscar Chávez ◽  
Francisco Martínez-Pérez ◽  
Francisco García-Sierra ◽  
...  

SummaryPlatelets are dynamic cell fragments that modify their shape during activation. Utrophin and dystrophins are minor actin-binding proteins present in muscle and non-muscle cytoskeleton. In the present study, we characterised the pattern of Dp71 isoforms and utrophin gene products by immunoblot in human platelets. Two new dystrophin isoforms were found, Dp71f and Dp71d, as well as the Up71 isoform and the dystrophin-associated proteins, α and β-dystrobrevins. Distribution of Dp71d/Dp71Δ110 m, Up400/Up71 and dystrophin-associated proteins in relation to the actin cytoskeleton was evaluated by confocal microscopy in both resting and platelets adhered on glass. Formation of two dystrophin-associated protein complexes (Dp71d/Dp71Δ110 m ~DAPC and Up400/Up71~DAPC) was demonstrated by co-immunoprecipitation and their distribution in relation to the actin cytoskeleton was characterised during platelet adhesion. The Dp71d/Dp71Δ110 m ~DAPC is maintained mainly at the granulomere and is associated with dynamic structures during activation by adhesion to thrombin-coated surfaces. Participation of both Dp71d/Dp71Δ110 m ~DAPC and Up400/Up71~DAPC in the biological roles of the platelets is discussed.


2016 ◽  
Vol 7 (10) ◽  
pp. 6551-6562 ◽  
Author(s):  
Aisling Byrne ◽  
Christopher S. Burke ◽  
Tia E. Keyes

Using precision peptide targeting to discrete cell organelles, it is demonstrated that Ru(ii) polypyridyl complexes are highly effective probes for stimulated emission depletion microscopy.


2011 ◽  
Vol 27 (4) ◽  
pp. 913-924 ◽  
Author(s):  
Steven M. Chirieleison ◽  
Taylor A. Bissell ◽  
Christopher C. Scelfo ◽  
Jordan E. Anderson ◽  
Yong Li ◽  
...  

2005 ◽  
Vol 170 (4) ◽  
pp. 637-648 ◽  
Author(s):  
Vladimir Sirotkin ◽  
Christopher C. Beltzner ◽  
Jean-Baptiste Marchand ◽  
Thomas D. Pollard

Yeast actin patches are dynamic structures that form at the sites of cell growth and are thought to play a role in endocytosis. We used biochemical analysis and live cell imaging to investigate actin patch assembly in fission yeast Schizosaccharomyces pombe. Patch assembly proceeds via two parallel pathways: one dependent on WASp Wsp1p and verprolin Vrp1p converges with another dependent on class 1 myosin Myo1p to activate the actin-related protein 2/3 (Arp2/3) complex. Wsp1p activates Arp2/3 complex via a conventional mechanism, resulting in branched filaments. Myo1p is a weaker Arp2/3 complex activator that makes unstable branches and is enhanced by verprolin. During patch assembly in vivo, Wsp1p and Vrp1p arrive first independent of Myo1p. Arp2/3 complex associates with nascent activator patches over 6–9 s while remaining stationary. After reaching a maximum concentration, Arp2/3 complex patches move centripetally as activator proteins dissociate. Genetic dependencies of patch formation suggest that patch formation involves cross talk between Myo1p and Wsp1p/Vrp1p pathways.


2017 ◽  
Vol 5 (43) ◽  
pp. 8525-8531 ◽  
Author(s):  
Hengchang Ma ◽  
Manyi Yang ◽  
Caili Zhang ◽  
Yucheng Ma ◽  
Yanfang Qin ◽  
...  

Herein, we report a set of novel AIE-active fluorescent probes containing pyridiniums and boric acid groups with the applications of ATP recognition and specific tracking of different cell organelles.


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