Combined fluorimetric caspase-3/7 assay and bradford protein determination for assessment of polycation-mediated cytotoxicity
Methods in Molecular Biology, ISSN: 1064-3745, Vol: 1943, Page: 301-311
2019
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
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Book Chapter Description
Cationic polyplexes and lipoplexes are widely used as artificial systems for nucleic acid delivery into the cells, but they can also induce cell death. Mechanistic understanding of cell toxicity and biological side effects of these cationic entities is essential for optimization strategies and design of safe and efficient nucleic acid delivery systems. Numerous methods are presently available to detect and delineate cytotoxicity and cell death-mediated signals in cell cultures. Activation of caspases is part of the classical apoptosis program and increased caspase activity is therefore a well-established hallmark of programmed cell death. Additional methods to monitor cell-death related signals must, however, also be carried out to fully define the type of cell toxicity in play. These may include methods that detect plasma membrane damage, loss of mitochondrial membrane potential, phosphatidylserine exposure, and cell morphological changes (e.g., membrane blebbing, nuclear changes, cytoplasmic swelling, cell rounding). Here we describe a 96-well format protocol for detection of caspase-3/7 activity in cell lysates, based on a fluorescent caspase-3 assay, combined with a method to simultaneously determine relative protein contents in the individual wells.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85062603114&origin=inward; http://dx.doi.org/10.1007/978-1-4939-9092-4_19; http://www.ncbi.nlm.nih.gov/pubmed/30838624; http://link.springer.com/10.1007/978-1-4939-9092-4_19; https://dx.doi.org/10.1007/978-1-4939-9092-4_19; https://link.springer.com/protocol/10.1007/978-1-4939-9092-4_19
Springer Science and Business Media LLC
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