|Protein Name||Caspase 3|
|Ref Sequence ID||NP_001071308.1|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Protein Function||Caspases are members of cysteinyl dependent aspartate directed proteases family which plays essential roles in regulating apoptosis at cellular level, and finally causes cellular demise through a cascade of molecular events; involved in disassembly of the cells into apoptotic bodies during apoptosis; member of the apoptosis executioner group|
|Biochemical Properties||intracellular proteases; activation is also appears to be associated with the increased mitochondrial transmembrane potential; Optimal pH for caspase-3 is 7.4; activity is relatively stable between 0 and 150 mM NaCl; caspases lose over 40% of their activity upon removal of CHAPS from the buffer, and the effect is more dramatic with caspase-6 than with caspases-3; active over a broader pH range with an optimum slightly higher than the other caspases; there is a faster than expected drop-off in activity at low pH, most clearly observed with caspases-3 and -6|
|Significance in milk||PMNs isolated from milk of mastitic cows showed revealing activities of caspase-3 which indicated that the milk PMNs undergo induced apoptosis and the process is programmed via the activation of initiator and executioner caspases|
|PTMs||phosphorylation at the highly conserved position S150; PKCd phosphorylates caspase-3 at S26; DEVD phosphorylates at the +3 (P3) position|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||No TM helices|
|Significance of PTMs||negatively controlled by p38 MAPK in neutrophils via phosphorylation at the highly conserved position S150; PKCd enhances caspase-3 activity and increase apoptotic cell death; DEVD promotes proteolysis of procaspase-3 by caspase-8 , demonstrating a functional significance of caspase-3 activation through phosphorylation for the execution step of apoptosis|
|Bibliography||1. Swain, D. K., Kushwah, M. S., Kaur, M., & Dang, A. K. (2015). Elucidation of Molecular Basis of Neutrophil Apoptosis during Staphylococcal Mastitis in Crossbred Cows . Journal of Animal Research, 5(1), 53. https://doi.org/10.5958/2277-940x.2015.00009.1. |
2. Jolivel, V., Arthaud, S., Botia, B., Portal, C., Delest, B., Clavé, G., … Vaudry, D. (2014). Biochemical characterization of a Caspase-3 far-red fluorescent probe for non-invasive optical imaging of neuronal apoptosis. Journal of Molecular Neuroscience : MN, 54(3), 451–462. https://doi.org/10.1007/s12031-014-0325-4.
3. Alvarado-Kristensson, M., & Andersson, T. (2005). Protein phosphatase 2A regulates apoptosis in neutrophils by dephosphorylating both p38 MAPK and its substrate caspase 3. The Journal of Biological Chemistry, 280(7), 6238–6244. https://doi.org/10.1074/jbc.M409718200.
4. Alvarado-Kristensson, M., Melander, F., Leandersson, K., Rönnstrand, L., Wernstedt, C., & Andersson, T. (2004). p38-MAPK Signals Survival by Phosphorylation of Caspase-8 and Caspase-3 in Human Neutrophils. Journal of Experimental Medicine, 199(4), 449–458. https://doi.org/10.1084/jem.20031771.