Single Step Fluorescent Caspase 3 Activity Assay: Quantifying the Inhibition of Cell Permeable Compounds in a Cell-Based System | Zendy

Jean Humpal-Winter | Zendy; Andrew L. Niles | Zendy; Martha A. O’Brien | Zendy; Bob Bulleit | Zendy

Open Access

Single Step Fluorescent Caspase 3 Activity Assay: Quantifying the Inhibition of Cell Permeable Compounds in a Cell-Based System

Author(s) -

Jean Humpal-Winter,

Andrew L. Niles,

Martha A. O’Brien,

Bob Bulleit

Publication year - 2001

Publication title -

the scientific world journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.453

H-Index - 93

eISSN - 2356-6140

pISSN - 1537-744X

DOI - 10.1100/tsw.2001.236

Subject(s) - fluorescence , cell , chemistry , caspase 3 , caspase , biophysics , apoptosis , biochemistry , biology , programmed cell death , physics , quantum mechanics

. Caspases are a family of cysteine aspartyl proteases that are involved in the cleavage of key structural, cell signaling, and DNA repair substrates leading to apoptotic cell death (1). As a result, the modulation of caspase response is the object of intense study in clinical research. Caspase 3 is recognized as a pivotal effector and logical target for therapeutic intervention (2). To this end, we have developed a robust, highly sensitive, and rapid homogeneous caspase 3 assay that is quantifiable in cell-based assays and with purified active caspase 3. We have used this assay to monitor the efficiency of several cell-permeable caspase 3 inhibitors in the cell-based Jurkat/Fas-induction model system (3). The evaluation of these compounds by caspase activity was supported and correlated with the CaspACE FITCVAD-FMK in situ cell imaging assay.

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