scholarly journals Asymmetric rhenium tricarbonyl complexes show superior luminescence properties in live cell imaging

2017 ◽  
Vol 53 (5) ◽  
pp. 905-908 ◽  
Author(s):  
Lukasz J. Raszeja ◽  
Daniel Siegmund ◽  
Anna L. Cordes ◽  
Jörn Güldenhaupt ◽  
Klaus Gerwert ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Cancer Cells ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Ligand Design ◽  
Live Cell ◽  
Luminescence Properties ◽  
Rhenium Tricarbonyl

Novel luminescent phenanthridinyl containing ReCO3 complexes with unusual asymmetric ligand design accumulate in the endoplasmic reticulum of living cancer cells.

scholarly journals EB1 binding restricts STIM1 translocation to ER–PM junctions and regulates store-operated Ca2+ entry

2018 ◽  
Vol 217 (6) ◽  
pp. 2047-2058 ◽  
Author(s):  
Chi-Lun Chang ◽  
Yu-Ju Chen ◽  
Carlo Giovanni Quintanilla ◽  
Ting-Sung Hsieh ◽  
Jen Liou
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Live Cell ◽  
Cellular Functions ◽  
Binding Ability ◽  
Trapping Mechanism ◽  
Spatiotemporal Regulation

The endoplasmic reticulum (ER) Ca2+ sensor STIM1 forms oligomers and translocates to ER–plasma membrane (PM) junctions to activate store-operated Ca2+ entry (SOCE) after ER Ca2+ depletion. STIM1 also interacts with EB1 and dynamically tracks microtubule (MT) plus ends. Nevertheless, the role of STIM1–EB1 interaction in regulating SOCE remains unresolved. Using live-cell imaging combined with a synthetic construct approach, we found that EB1 binding constitutes a trapping mechanism restricting STIM1 targeting to ER–PM junctions. We further showed that STIM1 oligomers retain EB1 binding ability in ER Ca2+-depleted cells. By trapping STIM1 molecules at dynamic contacts between the ER and MT plus ends, EB1 binding delayed STIM1 translocation to ER–PM junctions during ER Ca2+ depletion and prevented excess SOCE and ER Ca2+ overload. Our study suggests that STIM1–EB1 interaction shapes the kinetics and amplitude of local SOCE in cellular regions with growing MTs and contributes to spatiotemporal regulation of Ca2+ signaling crucial for cellular functions and homeostasis.

scholarly journals Live Cell Imaging of Protein Dislocation from the Endoplasmic Reticulum

2012 ◽  
Vol 287 (33) ◽  
pp. 28057-28066 ◽  
Author(s):  
Yongwang Zhong ◽  
Shengyun Fang
Keyword(s):  
Endoplasmic Reticulum ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Live Cell

Ruthenium(II) p-cymene complex of pyridine-2-carboxaldehyde and 2-amino benzothiazole based ligand: A cytoselective and in vitro live cell imaging agent†

2021 ◽  
Author(s):  
Anuja Plavuvalapill Kumar ◽  
Priyankar Paira
Keyword(s):  
Ambient Temperature ◽  
Cancer Cells ◽  
General Formula ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Live Cell ◽  
Imaging Agent ◽  
Arene Complexes ◽  
Mcf 7

Five Ru(II)-arene complexes ensuring the general formula [(η6-p-cymene)RuCl(k1L1-L5)(pyridine-2-carboxaldehyde)]Cl were synthesized under ambient temperature which exhibited 8-11 fold of cytoselectivity in two cancer cells (HeLa and MCF-7) with respect to normal...

Bionanoprobes with Excellent Two-Photon-Sensitized Eu3+ Luminescence Properties for Live Cell Imaging

2010 ◽  
Vol 16 (29) ◽  
pp. 8647-8651 ◽  
Author(s):  
Guangsheng Shao ◽  
Rongcheng Han ◽  
Yan Ma ◽  
Minxian Tang ◽  
Fumin Xue ◽  
...  
Keyword(s):  
Live Cell Imaging ◽  
Cell Imaging ◽  
Live Cell ◽  
Luminescence Properties ◽  
Two Photon

scholarly journals Multimodal optical contrast agents as new tools for monitoring and tuning nanoemulsion internalisation into cancer cells. From live cell imaging to in vivo imaging of tumours

2020 ◽  
Vol 2 (4) ◽  
pp. 1590-1602
Author(s):  
Geoffrey Prévot ◽  
Talia Bsaibess ◽  
Jonathan Daniel ◽  
Coralie Genevois ◽  
Guillaume Clermont ◽  
...  
Keyword(s):  
Contrast Agents ◽  
Cancer Cells ◽  
In Vivo Imaging ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Live Cell ◽  
Optical Contrast ◽  
Optical Probes ◽  
Optical Contrast Agents

Tailor-made NIR emitting dyes were designed as multimodal optical probes.

scholarly journals Impaired mitochondrial–endoplasmic reticulum interaction and mitophagy in Miro1-mutant neurons in Parkinson’s disease

2020 ◽  
Vol 29 (8) ◽  
pp. 1353-1364 ◽  
Author(s):  
Clara Berenguer-Escuder ◽  
Dajana Grossmann ◽  
Paul Antony ◽  
Giuseppe Arena ◽  
Kobi Wasner ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Endoplasmic Reticulum ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Mitochondrial Dynamics ◽  
Live Cell ◽  
Calcium Handling ◽  
Imaging Results ◽  
And Function

Abstract Mitochondrial Rho GTPase 1 (Miro1) protein is a well-known adaptor for mitochondrial transport and also regulates mitochondrial quality control and function. Furthermore, Miro1 was associated with mitochondrial-endoplasmic reticulum (ER) contact sites (MERCs), which are key regulators of cellular calcium homeostasis and the initiation of autophagy. Impairments of these mechanisms were linked to neurodegeneration in Parkinson’s disease (PD). We recently revealed that PD fibroblasts harboring Miro1 mutations displayed dysregulations in MERC organization and abundance, affecting mitochondrial homeostasis and clearance. We hypothesize that mutant Miro1 impairs the function of MERCs and mitochondrial dynamics, altering neuronal homeostasis and integrity in PD. PD skin fibroblasts harboring the Miro1-R272Q mutation were differentiated into patient-derived neurons. Live-cell imaging and immunocytochemistry were used to study mitophagy and the organization and function of MERCs. Markers of autophagy or mitochondrial function were assessed by western blotting. Quantification of organelle juxtapositions revealed an increased number of MERCs in patient-derived neurons. Live-cell imaging results showed alterations of mitochondrial dynamics and increased sensitivity to calcium stress, as well as reduced mitochondrial clearance. Finally, western blot analysis indicated a blockage of the autophagy flux in Miro1-mutant neurons. Miro1-mutant neurons display altered ER-mitochondrial tethering compared with control neurons. This alteration likely interferes with proper MERC function, contributing to a defective autophagic flux and cytosolic calcium handling capacity. Moreover, mutant Miro1 affects mitochondrial dynamics in neurons, which may result in disrupted mitochondrial turnover and altered mitochondrial movement.

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