What does cleaved caspase-3 indicate?

What does cleaved caspase-3 indicate?

Cleaved caspase-3 propagates an apoptotic signal through enzymatic activity on downstream targets, including poly ADP ribose polymerase (PARP) and other substrates (2). In cell biology, caspase-3 antibodies that detect both uncleaved and cleaved versions of the enzyme are strong indicators of cell death induction.

Is cleaved caspase-3 active?

The active Caspase 3 proteolytically cleaves and activates other caspases (e.g. Caspases 6, 7 and 9), as well as relevant targets in the cells (e.g. PARP and DFF). Variations in levels of Caspase 3 have been reported in cells of short-lived nature and those with a longer life cycle.

Does caspase-3 Cleave PARP?

Caspase-3, a member of the caspase family of 13 aspartate- specific cysteine proteases that play a central role in the exe- cution of the apoptotic program (6–8), is primarily responsible for the cleavage of PARP during cell death (4, 5, 9).

Is caspase-3 an enzyme?

Caspase 3 is a lysosomal enzyme involved in the apoptotic pathway, and is more specific in the detection of apoptotic cells than TUNEL (Figure 59.18).

What is Tunel staining?

‘TUNEL’ stands for Terminal deoxynucleotidyl transferase dUTP nick end labeling. Otherwise known as the TUNEL assay, TUNEL staining is used to detect DNA breaks formed during the final phase of apoptosis, when DNA fragmentation takes place.

What happens after caspase-3 is activated?

Once activated, caspase-3 will cleave key structural proteins, cell cycle proteins, and DNase proteins, such as poly(ADP-ribose) polymerase, gelsolin, ICAD/DFF, and DNA-dependent kinase11,12,13. These cleavage events result in the blebbing and condensing of cells that ultimately leads to cell death14.

What is the function of caspase-3?

Caspases are crucial mediators of programmed cell death (apoptosis). Among them, caspase-3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins.

What happens when PARP is cleaved?

Once cleaved, PARP1 loses its activity, thereby suppressing DNA repair. Caspase cleavage of PARP1 occurs within a nuclear localization signal near the DNA-binding domain, resulting in the formation of 24-kDa and 89-kDa fragments.