Use of a Fluorescently Labeled Poly-Caspase Inhibitor for <i>in Vivo</i> Detection of Apoptosis Related to Vascular-Targeting Agent Arsenic Trioxide for Cancer Therapy

Griffin, Robert J.; Williams, Brent; Bischof, John C.; Olin, Michael R.; Johnson, Gary L.; Lee, Brian W.

doi:10.1177/153303460700600609

Cited by 27 publications

(26 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Noncovalent hydrophobic interactions between fluorochrome domain and intracellular targets have also been postulated to play a role in FLICA retention (Pozarowski et al , 2003). It should be stressed that the covalent labeling of apoptotic cells with FLICA make these probes, called FLIVO, the markers of choice for detection of apoptosis in vivo , both in real time and after fixation of the tissue (Griffin et al , 2007). …”

Section: Cytometric Methods To Detect Apoptosismentioning

confidence: 99%

Apoptosis and Beyond: Cytometry in Studies of Programmed Cell Death

Wlodkowic

Telford

Skommer

et al. 2011

Methods in Cell Biology

395

340

View full text Add to dashboard Cite

A cell undergoing apoptosis demonstrates multitude of characteristic morphological and biochemical features, which vary depending on the inducer of apoptosis, cell type and the “time window” at which the process of apoptosis is observed. Because the gross majority of apoptotic hallmarks can be revealed by flow and image cytometry, the cytometric methods become a technology of choice in diverse studies of cellular demise. Variety of cytometric methods designed to identify apoptotic cells, detect particular events of apoptosis and probe mechanisms associated with this mode of cell death have been developed during the past two decades. In the present review, we outline commonly used methods that are based on the assessment of mitochondrial transmembrane potential, activation of caspases, DNA fragmentation, and plasma membrane alterations. We also present novel developments in the field such as the use of cyanine SYTO and TO-PRO family of probes. Strategies of selecting the optimal multiparameter approaches, as well as potential difficulties in the experimental procedures, are thoroughly summarized.

show abstract

Section: Cytometric Methods To Detect Apoptosismentioning

confidence: 99%

Apoptosis and Beyond: Cytometry in Studies of Programmed Cell Death

Wlodkowic

Telford

Skommer

et al. 2011

Methods in Cell Biology

395

340

View full text Add to dashboard Cite

show abstract

“…FAM-YVAD-FMK is also a common reagent to visualize caspase-1 activity during inflammasome-dependent cell death [39]. New versions called FLIVO are currently being marketed for use in in vivo studies [40, 41]. …”

Section: Applications Of Substrate- and Activity-based Probesmentioning

confidence: 99%

Functional imaging of proteases: recent advances in the design and application of substrate-based and activity-based probes

Edgington

Verdoes

Bogyo

2011

Current Opinion in Chemical Biology

159

184

View full text Add to dashboard Cite

Proteases are enzymes that cleave peptide bonds in protein substrates. This process can be important for regulated turnover of a target protein but it can also produce protein fragments that then perform other functions. Because the last few decades of protease research have confirmed that proteolysis is an essential regulatory process in both normal physiology and in multiple disease-associated conditions, there has been an increasing interest in developing methods to image protease activity. Proteases are also considered to be one of the few druggable classes of proteins and therefore a large number of small molecule based inhibitors of proteases have been reported. These compounds serve as a starting point for the design of probes that can be used to target active proteases for imaging applications. Currently, several classes of fluorescent probes have been developed to visualize protease activity in live cells and even whole organisms. The two primary classes of protease probes make use of either peptide/protein substrates or covalent inhibitors that produce a fluorescent signal when bound to an active protease target. This review outlines some of the most recent advances in the design of imaging probes for proteases. In particular, it highlights the strengths and weaknesses of both substrate- and activity- based probes and their applications for imaging cysteine proteases that are important biomarkers for multiple human diseases.

show abstract

“…Cell apoptosis and autophagy are two major morphologically distinctive forms of programmed cell death. During apoptotic death, the process is executed by a class of cysteine proteases, caspases [12,13]. The death receptor pathway and the mitochondria-mediated pathway are two main pathways to induce cell apoptosis, while cell autophagy is characterized by massive degradation of cellular contents [14], which is independent on the activation of caspases.…”

Section: Introductionmentioning

confidence: 99%

Oridonin phosphate-induced autophagy effectively enhances cell apoptosis of human breast cancer cells

Wang²,

Wang

et al. 2014

Med Oncol

View full text Add to dashboard Cite

Oridonin is an active diterpenoid, which was extracted from traditional Chinese herbs and had been widely used in clinical treatment nowadays. Oridonin phosphate is one of the derivatives of oridonin. In the present study, we explored its anti-tumor effect and investigated the molecular mechanism of oridonin phosphate in breast cancer cell lines. Firstly, cell viability was analyzed by MTT assay. The breast cancer cells were treated with increasing concentrations of oridonin phosphate for 24, 48 and 72 h, respectively. The results demonstrated that oridonin phosphate inhibited the proliferation of MDA-MB-436 and MDA-MB-231 cells in a dose- and time-dependent manner. Next, cell apoptosis rate was detected in oridonin phosphate-treated breast cancer cells by Annexin V-FITC/PI dual staining analysis and the data demonstrated that oridonin phosphate induced cell apoptosis of breast cancer cells in time- and dose-dependent manner. Moreover, apoptosis-related proteins were detected by Western blotting analysis. The results showed that the expression level of Bax was up-regulated and the expression level of Bcl-2 was down-regulated. Meanwhile, the level of cleaved caspase-9 was significantly increased when the cells were treated with 40 μM of oridonin phosphate for 48 h, although the expression level of pro-caspase-9 was not obviously changed. All of the data revealed that mitochondrial apoptosis pathway may be involved in the cell apoptosis induced by oridonin phosphate in breast cancer cells. Importantly, the expression levels of autophagy-related protein beclin-1 and LC3-II were significantly higher in oridonin phosphate-treated breast cancer cell lines MDA-MB-436 and MDA-MB-231 for 48 h. Additionally, we further explored the relationship between apoptosis and autophagy specifically induced by oridonin phosphate in breast cancer cells. The result showed that inhibition of autophagy suppressed the cell apoptosis in oridonin phosphate-treated MDA-MB-436 cells. Taken together, the compound of oridonin phosphate simultaneously induced cell apoptosis and autophagy in breast cancer cells. Inhibition oridonin phosphate-induced cell autophagy suppressed the progression of cell apoptosis, which revealed that oridonin phosphate-induced autophagy participated in up-regulation of apoptosis in human breast cancer cells. It would provide some new clues for the therapy of breast cancer.

show abstract

Use of a Fluorescently Labeled Poly-Caspase Inhibitor for in Vivo Detection of Apoptosis Related to Vascular-Targeting Agent Arsenic Trioxide for Cancer Therapy

Cited by 27 publications

References 19 publications

Apoptosis and Beyond: Cytometry in Studies of Programmed Cell Death

Apoptosis and Beyond: Cytometry in Studies of Programmed Cell Death

Functional imaging of proteases: recent advances in the design and application of substrate-based and activity-based probes

Oridonin phosphate-induced autophagy effectively enhances cell apoptosis of human breast cancer cells

Contact Info

Product

Resources

About