Apoptotic Stimulus Detection
Apoptotic Stimulus Detection - Related Videos
11:57
Organotypic Cerebellar Cultures: Apoptotic Challenges and Detection
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Cited by 17 •
2011
This method describes the generation of organotypic cerebellar cultures and the effect of certain apoptotic stimuli on the viability of different cerebellar cell types.
01:30
TUNEL Assay for Detecting Apoptotic Cell Death in a Brain Slice
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2025
To detect apoptotic cell death using the TUNEL assay, treat the brain slice with the enzyme proteinase-K.
12:17
Detection and Isolation of Apoptotic Bodies to High Purity
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Cited by 29 •
2018
A workflow using flow cytometry or differential centrifugation is developed to detect, quantify and isolate apoptotic bodies from an apoptotic sample to high purity.
13:21
In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila
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Cited by 5 •
2016
To detect healthy cells in whole animals that contain low levels of caspase activity, the highly sensitive biosensor designated CaspaseTracker was generated for Drosophila. Caspase-dependent biosensor activity is detected in long-lived healthy cells throughout the internal organs of adult animals reared under optimized conditions in the absence of death stimuli.
05:36
Analysis of Efferocytosis of Apoptotic Thymocytes by Peritoneal Macrophages
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2025
This video demonstrates a procedure for analyzing peritoneal macrophage-mediated efferocytosis of apoptotic mouse thymocytes by fluorescence microscopy.
FAQs
Cellular stress can alter the balance of BCL-2 family activity, allowing mitochondrial outer-membrane permeabilization. This change enables cytochrome c release, which is a measurable mitochondrial event associated with subsequent caspase activation. Tracking both cytochrome c release and caspase activity helps researchers connect an upstream neuronal stress signal with downstream execution of regulated cell death.
Mitochondrial signaling links stressors such as DNA damage, trophic-factor withdrawal, oxidative stress, and excitotoxic signaling to BCL-2 family regulation and mitochondrial membrane permeabilization. Death-receptor pathways provide a separate route into caspase signaling. Comparing these routes can help determine whether a neuronal death response is associated primarily with intracellular stress or receptor-mediated initiation.
Different stressors can initiate the same broad apoptotic program through distinct cellular signals. DNA damage, loss of trophic support, oxidative stress, and excitotoxic signaling therefore provide different experimental contexts for examining pathway activation. Identifying the initiating condition alongside caspase activity, cytochrome c release, or other markers improves interpretation of how neurons respond to injury.
A combined assessment is more informative than relying on one signal alone. Cytochrome c release indicates mitochondrial involvement, caspase activity reflects activation of the proteolytic death-signaling cascade, phosphatidylserine exposure marks a surface change, and DNA fragmentation provides a nuclear readout. Together, these measurements help distinguish regulated neuronal death from other forms of cellular injury.
A study can first expose neurons to a defined stress condition, such as DNA damage, trophic-factor withdrawal, oxidative stress, or excitotoxic signaling. Researchers then examine pathway-associated outcomes, including BCL-2 family changes, mitochondrial cytochrome c release, caspase activity, phosphatidylserine exposure, or DNA fragmentation. Selecting complementary readouts links the stimulus to its cellular consequences.
The approach is useful when investigators need to examine regulated neuronal death in contexts such as neurodevelopment or neurodegenerative disease. It can also support evaluation of potential neuroprotective interventions by showing whether a treatment changes apoptotic signaling or its downstream readouts. These measurements connect cellular stress responses with broader questions about neuronal survival and loss.