A fluorogenic probe for imaging protein S-nitrosylation in live cells

2017 ◽  
Vol 94 ◽  
pp. 162-168 ◽  
Author(s):  
Shiyi Shao ◽  
Bo Chen ◽  
Juan Cheng ◽  
Chengkun Wang ◽  
Yanli Zhang ◽  
...  
Keyword(s):  
Protein S ◽  
Live Cells ◽  
Fluorogenic Probe

scholarly journals A Fluorescent Probe with Improved Water Solubility Permits the Analysis of Protein S-Depalmitoylation Activity in Live Cells

Biochemistry ◽  
2017 ◽  
Vol 57 (2) ◽  
pp. 221-225 ◽  
Author(s):  
Tian Qiu ◽  
Rahul S. Kathayat ◽  
Yang Cao ◽  
Michael W. Beck ◽  
Bryan C. Dickinson
Keyword(s):  
Fluorescent Probe ◽  
Water Solubility ◽  
Protein S ◽  
Live Cells

A ratiometric fluorogenic probe for the real-time detection of SO32−in aqueous medium: application in a cellulose paper based device and potential to sense SO32−in mitochondria

The Analyst ◽  
2018 ◽  
Vol 143 (1) ◽  
pp. 250-257 ◽  
Author(s):  
Soham Samanta ◽  
Senjuti Halder ◽  
Poulomi Dey ◽  
Utsab Manna ◽  
Aiyagari Ramesh ◽  
...  
Keyword(s):  
Aqueous Medium ◽  
Real Time ◽  
Water Soluble ◽  
Live Cells ◽  
The Real ◽  
Cellulose Paper ◽  
Fluorogenic Probe ◽  
Ratiometric Detection ◽  
Real Time Detection

A new water soluble and fluorogenic probe (L) that can demonstrate the specific ratiometric detection of a SO2derivative (SO32−) in 100% aqueous medium and live cells has been designed and synthesized.

scholarly journals A highly sensitive fluorogenic probe for cytochrome P450 activity in live cells

2008 ◽  
Vol 18 (22) ◽  
pp. 5864-5866 ◽  
Author(s):  
Melissa M. Yatzeck ◽  
Luke D. Lavis ◽  
Tzu-Yuan Chao ◽  
Sunil S. Chandran ◽  
Ronald T. Raines
Keyword(s):  
Cytochrome P450 ◽  
Live Cells ◽  
Cytochrome P450 Activity ◽  
Fluorogenic Probe ◽  
Highly Sensitive ◽  
P450 Activity

scholarly journals A Highly Sensitive Fluorogenic Probe for Imaging Glycoproteins and Mucine Activity in Live Cells in the Near-Infrared Region

2018 ◽  
Vol 24 (24) ◽  
pp. 6344-6348 ◽  
Author(s):  
Cecilia Samaniego Lopez ◽  
Jimena Hebe Martínez ◽  
María Laura Uhrig ◽  
Federico Coluccio Leskow ◽  
Carla Cecilia Spagnuolo
Keyword(s):  
Near Infrared ◽  
Infrared Region ◽  
Live Cells ◽  
Fluorogenic Probe ◽  
Highly Sensitive ◽  
Near Infrared Region

Ligand-displacement-based two-photon fluorogenic probe for visualizing mercapto biomolecules in live cells, Drosophila brains and zebrafish

The Analyst ◽  
2018 ◽  
Vol 143 (14) ◽  
pp. 3433-3441 ◽  
Author(s):  
Yanfei Zhao ◽  
Yun Ni ◽  
Liulin Wang ◽  
Chenchen Xu ◽  
Chenqi Xin ◽  
...  
Keyword(s):  
Rapid Detection ◽  
Live Cell ◽  
Live Cells ◽  
Two Photon ◽  
Ligand Displacement ◽  
Cell Tissue ◽  
Fluorogenic Probe ◽  
Displacement Based

We report the Fe(iii)-based complex TPFeS which acts as a novel ligand-displacement-based TP fluorogenic probe for the rapid detection of mercapto biomolecules both in vitro and in live cell/tissue/in vivo imaging.

Late-stage difluoromethylation leading to a self-immobilizing fluorogenic probe for the visualization of enzyme activities in live cells

2019 ◽  
Vol 55 (99) ◽  
pp. 15000-15003 ◽  
Author(s):  
Jialing Jiang ◽  
Qingwei Tan ◽  
Shuxuan Zhao ◽  
Heng Song ◽  
Liqiang Hu ◽  
...  
Keyword(s):  
Late Stage ◽  
Enzyme Activities ◽  
Quinone Methide ◽  
Live Cells ◽  
Fluorogenic Probe

A novel p-quinone methide-based self-immobilizing and fluorogenic probe is reported for the visualization of β-galactosidase activities in live cells.

A wash-free SNAP-tag fluorogenic probe based on the additive effects of quencher release and environmental sensitivity

2017 ◽  
Vol 53 (48) ◽  
pp. 6448-6451 ◽  
Author(s):  
Shuang Leng ◽  
Qinglong Qiao ◽  
Lu Miao ◽  
Wuguo Deng ◽  
Jingnan Cui ◽  
...  
Keyword(s):  
Live Cells ◽  
Additive Effects ◽  
Environmental Sensitivity ◽  
Fluorogenic Probe

A 1,8-naphthalimide-derived SNAP-tag fluorogenic probe can specifically and rapidly label proteins in live cells without requiring a wash procedure.

scholarly journals Michael addition-based probes for ratiometric fluorescence imaging of protein S-depalmitoylases in live cells and tissues

2017 ◽  
Vol 8 (11) ◽  
pp. 7588-7592 ◽  
Author(s):  
Michael W. Beck ◽  
Rahul S. Kathayat ◽  
Candace M. Cham ◽  
Eugene B. Chang ◽  
Bryan C. Dickinson
Keyword(s):  
Fluorescence Imaging ◽  
Fluorescent Probes ◽  
Michael Addition ◽  
Enzyme Activities ◽  
Protein S ◽  
Live Cell ◽  
Tissue Imaging ◽  
Live Cells ◽  
Ratiometric Fluorescence

Ratiometric fluorescent probes for cysteine palmitoylation “erasers” permit live cell and tissue imaging of endogenous enzyme activities.

scholarly journals Correction: Michael addition-based probes for ratiometric fluorescence imaging of protein S-depalmitoylases in live cells and tissues

2017 ◽  
Vol 8 (11) ◽  
pp. 7879-7879
Author(s):  
Michael W. Beck ◽  
Rahul S. Kathayat ◽  
Candace M. Cham ◽  
Eugene B. Chang ◽  
Bryan C. Dickinson
Keyword(s):  
Fluorescence Imaging ◽  
Michael Addition ◽  
Protein S ◽  
Live Cells ◽  
Ratiometric Fluorescence

Correction for ‘Michael addition-based probes for ratiometric fluorescence imaging of protein S-depalmitoylases in live cells and tissues’ by Michael W. Beck et al., Chem. Sci., 2017, DOI: 10.1039/c7sc02805a

scholarly journals Pkc Epsilon Regulates Mitochondrial Redox Biology to Support the Differentiation Blockade in Acute Myeloid Leukemia

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 444-444
Author(s):  
Daniela Di Marcantonio ◽  
Jessica Vadaketh ◽  
Esteban Martinez ◽  
Prisco Mirandola ◽  
Giuliana Gobbi ◽  
...  
Keyword(s):  
Cell Lines ◽  
Myeloid Leukemia ◽  
Live Cells ◽  
Myeloid Differentiation ◽  
Redox Biology ◽  
Fluorogenic Probe ◽  
Intracellular Ros ◽  
O2 Production ◽  
Acute Myeloid

Abstract Acute myeloid leukemia (AML) is a genetically heterogeneous disease that is characterized by the clonal expansion of myeloid progenitors that have impaired differentiation capacity. Determining the molecular machinery that regulate the survival and differentiation blockade of AML cells could serve as a foundation for designing novel therapies. PKCε is a serine-threonine kinase belonging to the subgroup of the Protein Kinase C family called Novel PKCs. Aberrant PKCε expression and activation is associated with the pathogenesis and chemotherapy resistance of many solid cancers. However, the contribution of PKCε in blood malignances such as AML is not well defined. To evaluate the role of PKCe in AML biology, we employed short hairpin RNA (shRNA)-mediated approaches to down-regulate PKCε expression in human and murine AML cell lines. We found that shRNA-mediated knockdown of PKCε significantly reduces the in vitro expansion of several human AML cell lines (MOLM-14, NOMO-1, OCI-AML3, THP-1 and U937). We also observed that blocking PKCε induces caspase-3 cleavage and increases the number of annexin V-positive cells (P<0.05), suggesting that PKCε antagonizes AML cell apoptosis. Additionally, we have also found that prior to cell death, AML cells expressing PKCε-targeting shRNAs display characteristics of myeloid differentiation. Specifically, down-regulation of PKCε results in altered expression of the myeloid differentiation transcription factors C/EBPa and PU.1 and increased expression of the mature myeloid marker CD11b (P<0.001). Moreover, upon PKCε inhibition, AML cells acquire morphological changes associated with differentiation, such as increased cytoplasmic volume, granule formation and nuclear segmentation. Interestingly, we observed similar phenotypic changes when we inhibited PKCε expression in murine AML cell lines driven by the leukemogenic fusion protein MLL-AF9 alone (MLL-AF9) or in combination with the internal tandem duplication mutation of murine Flt3 (MLL-AF9;Flt3-ITD). Specifically, we observed that PKCε down-modulation significantly reduces murine AML cell survival (P<0.001) and colony formation in methylcellulose (P<0.001) of both MLL-AF9 and MLL-AF9;Flt3-ITD cells compared to non-targeting shRNA-expressing cells. We are currently investigating how PKCε inhibition impacts AML progression in vivo using mouse models of AML driven by MLL-AF9 or MLL-AF9;Flt3-ITD. At the molecular level, we have found that PKCε is a key regulator of reactive oxygen species (ROS) biology in AML cells. Specifically, using a fluorogenic probe (CellRox) that indiscriminately detects most types of ROS, we have observed that PKCε knockdown in human AML cell lines results in increased steady-state levels of intracellular ROS compared to shRNA control cells (P<0.002). Total intracellular ROS levels are influenced by the production and clearance of distinct ROS types in various cellular compartments. To further characterize the localization and specific type(s) of ROS regulated by PKCε, we utilized four redox-sensitive GFP (roGFP) probes, which allow for direct measurement of cytoplasmic and mitochrondrial glutathione redox potential (Grx1-roGFP-Cyto and Grx1-roGFP-Mito, respectively) and hydrogen peroxide (H2O2) levels (Orp1-roGFP-Cyto and Orp1-roGFP-Mito, respectively) in live cells. Down-modulation of PKCε in NOMO-1 and OCI-AML-3 cells expressing each of these roGFP constructs resulted in a significant increase in the oxidation of Grx1-roGFP (P<.0007) and Orp1-roGFP-Mito (P<0.02) but not either of cytoplasmic constructs, suggesting that PKCε regulates the production of ROS in the mitochondria of AML cells. Since increased H2O2 production and glutathione oxidation results from increased superoxide (O2-) production in mitochondria, we next evaluated the impact of PKCε on O2- production. Using a fluorogenic probe (MitoSOX) that specifically detects O2- in live cells, we found that PKCε down-modulation increases the production of O2- in AML cells (P<0.05). Our future studies are focused on determining the precise molecular events that connect alterations in redox biology with the survival and differentiation of AML cells. Collectively, these results uncover the previously unrecognized role of PKCε as a critical regulator of mitochondrial redox biology and supporter of cell survival and impaired differentiation in AML. Disclosures No relevant conflicts of interest to declare.

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