Engineering of a bioluminescent probe for imaging nitroxyl in live cells and mice

2019 ◽  
Vol 55 (12) ◽  
pp. 1758-1761 ◽  
Author(s):  
Jun-Bin Li ◽  
Qianqian Wang ◽  
Hong-Wen Liu ◽  
Xia Yin ◽  
Xiao-Xiao Hu ◽  
...  
Keyword(s):  
Turn On ◽  

A turn-on bioluminescent probe (BP-HNO) that is free of autofluorescence for bioimaging nitroxyl in live cells and mice is reported for the first time.

RSC Advances ◽  
2016 ◽  
Vol 6 (71) ◽  
pp. 66774-66778 ◽  
Author(s):  
Prithidipa Sahoo ◽  
Himadri Sekhar Sarkar ◽  
Sujoy Das ◽  
Kalipada Maiti ◽  
Md Raihan Uddin ◽  
...  

A new ‘turn-ON’ fluorescent probe, pyrene appended thymine acetamide (PTA), with high sensitivity and selectivity for the detection of uric acid (UA) was developed and first time imaging of uric acid in living cells in water was achieved.


2019 ◽  
Vol 55 (31) ◽  
pp. 4487-4490 ◽  
Author(s):  
Jun-Bin Li ◽  
Qianqian Wang ◽  
Hong-Wen Liu ◽  
Lin Yuan ◽  
Xiao-Bing Zhang

A turn-on bioluminescent probe (BP-PS) for bioimaging endogenous H2Sn in live cells and a murine model of bacterial infection was, for the first time, reported.


2021 ◽  
Vol 1157 ◽  
pp. 338394
Author(s):  
Xiao-Yue Tang ◽  
Yi-Ming Liu ◽  
Xiao-Lin Bai ◽  
Hao Yuan ◽  
Yi-Kao Hu ◽  
...  

2015 ◽  
Vol 44 (9) ◽  
pp. 4123-4132 ◽  
Author(s):  
Chirantan Kar ◽  
Soham Samanta ◽  
Sudeep Goswami ◽  
Aiyagari Ramesh ◽  
Gopal Das

Selective recognition of Al3+and Cd2+by UV-Vis and fluorescence based techniques using a cinnamaldehyde functionalized conjugated ligand, and its applications in paper strip and live cell imaging.


2009 ◽  
Vol 14 (8) ◽  
pp. 956-969 ◽  
Author(s):  
Christophe Antczak ◽  
Toshimitsu Takagi ◽  
Christina N. Ramirez ◽  
Constantin Radu ◽  
Hakim Djaballah

Caspases are central to the execution of programmed cell death, and their activation constitutes the biochemical hallmark of apoptosis. In this article, the authors report the successful adaptation of a high-content assay method using the DEVDNucView488™ fluorogenic substrate, and for the first time, they show caspase activation in live cells induced by either drugs or siRNA. The fluorogenic substrate was found to be nontoxic over an exposure period of several days, during which the authors demonstrate automated imaging and quantification of caspase activation of the same cell population as a function of time. Overexpression of the antiapoptotic protein Bcl-XL, alone or in combination with the inhibitor Z-VAD-FMK, attenuated caspase activation in HeLa cells exposed to doxorubicin, etoposide, or cell death siRNA. This method was further validated against 2 well-characterized NSCLC cell lines reported to be sensitive (H3255) or refractory (H2030) to erlotinib, where the authors show a differential time-dependent activation was observed for H3255 and no significant changes in H2030, consistent with their respective chemosensitivity profile. In summary, the results demonstrate the feasibility of using this newly adapted and validated high-content assay to screen chemical or RNAi libraries for the identification of previously uncovered enhancers and suppressors of the apoptotic machinery in live cells. ( Journal of Biomolecular Screening 2009:956-969)


The Analyst ◽  
2014 ◽  
Vol 139 (24) ◽  
pp. 6352-6356 ◽  
Author(s):  
Narendra Reddy Chereddy ◽  
M. V. Niladri Raju ◽  
Peethani Nagaraju ◽  
Venkat Raghavan Krishnaswamy ◽  
Purna Sai Korrapati ◽  
...  

A naphthalimide based Fe3+ selective fluorescence ‘turn-on’ probe that operates based on a PET mechanism has been synthesized, and its application in the detection of Fe3+ ions in aqueous samples and in live cells is explored.


2012 ◽  
Vol 41 (24) ◽  
pp. 7212 ◽  
Author(s):  
Lin Xu ◽  
Yufang Xu ◽  
Weiping Zhu ◽  
Chunmei Yang ◽  
Le Han ◽  
...  

2017 ◽  
Vol 8 (10) ◽  
pp. 7014-7024 ◽  
Author(s):  
Xiujuan Shi ◽  
Chris Y. Y. Yu ◽  
Huifang Su ◽  
Ryan T. K. Kwok ◽  
Meijuan Jiang ◽  
...  

For the first time, an AIEgen-conjugated monoclonal antibody is designed for “turn-on” and “wash-free” imaging of EGFR-overexpressed cancer cells.


2001 ◽  
Vol 21 (16) ◽  
pp. 5312-5320 ◽  
Author(s):  
Anna Polesskaya ◽  
Irina Naguibneva ◽  
Arnaud Duquet ◽  
Eyal Bengal ◽  
Philippe Robin ◽  
...  

ABSTRACT Acetylation is emerging as a posttranslational modification of nuclear proteins that is essential to the regulation of transcription and that modifies transcription factor affinity for binding sites on DNA, stability, and/or nuclear localization. Here, we present both in vitro and in vivo evidence that acetylation increases the affinity of myogenic factor MyoD for acetyltransferases CBP and p300. In myogenic cells, the fraction of endogenous MyoD that is acetylated was found associated with CBP or p300. In vitro, the interaction between MyoD and CBP was more resistant to high salt concentrations and was detected with lower doses of MyoD when MyoD was acetylated. Interestingly, an analysis of CBP mutants revealed that the interaction with acetylated MyoD involves the bromodomain of CBP. In live cells, MyoD mutants that cannot be acetylated did not associate with CBP or p300 and were strongly impaired in their ability to cooperate with CBP for transcriptional activation of a muscle creatine kinase-luciferase construct. Taken together, our data suggest a new mechanism for activation of protein function by acetylation and demonstrate for the first time an acetylation-dependent interaction between the bromodomain of CBP and a nonhistone protein.


2020 ◽  
Author(s):  
Chi Zhang ◽  
Stephen Boppart

Abstract The mitochondrion is one of the key organelles for maintaining cellular homeostasis. External environmental stimuli and internal regulatory processes alter the metabolism and functions of mitochondria. To understand these activities of mitochondria, it is critical to probe the key metabolic molecules inside these organelles. In this study, we used label-free chemical imaging modalities including coherent anti-Stokes Raman scattering and multiphoton-excited autofluorescence to study the mitochondrial activities in living cancer cells. We found that hypothermia exposure tends to induce fatty-acid (FA) accumulation in some mitochondria of MIAPaCa-2 cells. Autofluorescence images show that the FA-accumulated mitochondria also have abnormal NADH and FAD metabolism, likely induced by the dysfunction of the electron transport chain. We also found that when the cells were re-warmed to physiological temperature after a period of hypothermia, the FA-accumulated mitochondria changed their structural features, likely caused by the mitophagy process. To the best of our knowledge, this is the first time that FA accumulation in mitochondria was observed in live cells. Our research also demonstrates that multimodal label-free chemical imaging is an attractive tool to discover abnormal functions of mitochondria at the single-organelle level and can be used to quantify the dynamic changes of this organelle under perturbative conditions.


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