Dendrimer Internalization and Intracellular Trafficking in Living Cells

2010 ◽  
Vol 7 (3) ◽  
pp. 680-688 ◽  
Author(s):  
Lorenzo Albertazzi ◽  
Michela Serresi ◽  
Alberto Albanese ◽  
Fabio Beltram
2019 ◽  
Vol 6 (04) ◽  
Author(s):  
JESHIMA KHAN YASIN ◽  
ANIL KUMAR SINGH

Cytoplasmic streaming is one among the vital activities of the living cells. In plants cytolplasmic streaming could clearly be seen in hypocotyls of growing seedlings. To observe cytoplsmic streaming and its correlated intracellular trafficking an investigation was conducted in legumes in comparison with GFP-AtRab75 and 35S::GFP:δTIP tonoplast fusion protein expressing arabidopsis lines. These seedlings were observed under confocal microscopy with different buffer incubation treatments and under different stress conditions. GFP expressing 35S::GFP:δTIP tonoplast lines were looking similar to the control lines and differ under stress conditions. Movement of cytoplasmic invaginations within the tonoplast and cytoplasmic sub vesicle or bulb budding during cytoplasmic streaming was observed in hypocotyls of At-GFP tonoplast plants. We found the cytoplasmic bulbs/ vesicles or sub vesicle formation from the plasma membrane. The streaming speed also depends on the incubation medium in which the specimen was incubated, indicating that the external stimuli as well as internal stimuli can alter the speed of streaming


2015 ◽  
Vol 104 (9) ◽  
pp. 2845-2854 ◽  
Author(s):  
Yuma Yamada ◽  
Sandra Milena Vergara Perez ◽  
Mai Tabata ◽  
Jiro Abe ◽  
Yukari Yasuzaki ◽  
...  

Soft Matter ◽  
2012 ◽  
Vol 8 (30) ◽  
pp. 7919 ◽  
Author(s):  
Stefano Coppola ◽  
Laura C. Estrada ◽  
Michelle A. Digman ◽  
Daniela Pozzi ◽  
Francesco Cardarelli ◽  
...  

2021 ◽  
Vol 2021 ◽  
pp. 1-9
Author(s):  
Masayuki Takahashi ◽  
Mineaki Seki ◽  
Masayuki Nashimoto ◽  
Tomohiro Kabuta

Although antisense oligonucleotide (ASO) therapeutics can be taken up by living cells without carrier molecules, a large part of incorporated ASOs are trapped in the endosomes and do not exert therapeutic effects. To improve their therapeutic effects, it would be important to elucidate the mechanism of cellular uptake and intracellular trafficking of ASOs. In this study, we investigated how SIDT1 affects cellular uptake and intracellular trafficking of ASOs. Fluorescence microscopic analysis suggested that most of naked ASOs are trafficked to the lysosomes via the endosomes. The data obtained from flow cytometry and fluorescence microscopy together showed that although the SIDT1 level barely affects the total cellular uptake of ASOs, it appears to affect the intracellular trafficking of ASOs. We also showed that SIDT1 exists mainly in the endoplasmic reticulum and that perturbing the normal level of SIDT1 suppresses the antisense effect of the naked ASO targeting miR-16.


Virology ◽  
1998 ◽  
Vol 251 (1) ◽  
pp. 38-48 ◽  
Author(s):  
Roland H. Stauber ◽  
Elena Afonina ◽  
Sergei Gulnik ◽  
John Erickson ◽  
George N. Pavlakis

2012 ◽  
Vol 23 (5) ◽  
pp. 1059-1068 ◽  
Author(s):  
Lorenzo Albertazzi ◽  
Marcos Fernandez-Villamarin ◽  
Ricardo Riguera ◽  
Eduardo Fernandez-Megia

Author(s):  
R. Y. Tsien ◽  
A. Minta ◽  
M. Poenie ◽  
J.P.Y. Kao ◽  
A. Harootunian

Recent technical advances now enable the continuous imaging of important ionic signals inside individual living cells with micron spatial resolution and subsecond time resolution. This methodology relies on the molecular engineering of indicator dyes whose fluorescence is strong and highly sensitive to ions such as Ca2+, H+, or Na+, or Mg2+. The Ca2+ indicators, exemplified by fura-2 and indo-1, derive their high affinity (Kd near 200 nM) and selectivity for Ca2+ to a versatile tetracarboxylate binding site3 modeled on and isosteric with the well known chelator EGTA. The most commonly used pH indicators are fluorescein dyes (such as BCECF) modified to adjust their pKa's and improve their retention inside cells. Na+ indicators are crown ethers with cavity sizes chosen to select Na+ over K+: Mg2+ indicators use tricarboxylate binding sites truncated from those of the Ca2+ chelators, resulting in a more compact arrangement of carboxylates to suit the smaller ion.


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