| First Author | Lamkanfi M | Year | 2010 |
| Journal | Int J Biochem Cell Biol | Volume | 42 |
| Issue | 1 | Pages | 21-4 |
| PubMed ID | 19782763 | Mgi Jnum | J:320305 |
| Mgi Id | MGI:6871006 | Doi | 10.1016/j.biocel.2009.09.013 |
| Citation | Lamkanfi M, et al. (2010) Caspase-7: a protease involved in apoptosis and inflammation. Int J Biochem Cell Biol 42(1):21-4 |
| abstractText | Caspase-7 was considered to be redundant with caspase-3 because these related cysteine proteases share an optimal peptide recognition sequence and have several endogenous protein substrates in common. In addition, both caspases are proteolytically activated by the initiator caspase-8 and -9 during death receptor- and DNA-damage-induced apoptosis, respectively. However, a growing body of biochemical and physiological data indicate that caspase-7 also differs in significant ways from caspase-3. For instance, several substrates are specifically cleaved by caspase-7, but not caspase-3. Moreover, caspase-7 activation requires caspase-1 inflammasomes under inflammatory conditions, while caspase-3 processing proceeds independently of caspase-1. Finally, caspase-7 deficient mice are resistant to endotoxemia, whereas caspase-3 knockout mice are susceptible. These findings suggest that specifically interfering with caspase-7 activation may hold therapeutic value for the treatment of cancer and inflammatory ailments. |
