Caspase-7: A protease involved in apoptosis and inflammation

Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium
The international journal of biochemistry & cell biology (Impact Factor: 4.05). 09/2009; 42(1):21-4. DOI: 10.1016/j.biocel.2009.09.013
Source: PubMed


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.

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    • "The recurrent elimination of hair follicle keratinocytes by apoptosis is a process involving caspases (reviewed in Botchkareva et al. 2006). Caspase-7 belongs to the trio of apoptotic executors but also has been shown to participate in inflammation (Lamkanfi and Kanneganti 2010). Additionally , activated caspase-7 has been reported in nonapoptotic cells in relation to cell differentiation (Matalova et al. 2012; Svandova et al. 2014). "
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    ABSTRACT: Hair follicles are unique organs undergoing regular cycles of proliferation, differentiation, and apoptosis. The final step of apoptosis is, in general, mediated by executioner caspases comprising caspase-3, -6 and -7. Despite their commonly accepted apoptotic function, executioner caspases also participate in non-apoptotic processes. In the present study, we investigated activation (cleavage) of caspase-7 in mouse hair follicles and surrounding tissue during embryonic development into adulthood. Casp7 −/− mice were examined to understand the effect of caspase-7 deficiency in the skin. The activated form of caspase-7 was observed during embryonic hair follicle development, as well as in the first hair cycle. In general, activation of caspase-7 did not correlate with apoptosis and activation of caspase-3, except during physiological hair follicle regression. Notably, cleaved caspase-7 was observed in mast cells and its deficiency in the adult skin resulted in increased mast cell number. Our study shows for the first time activated caspase-7 in hair follicles and mast cells and indicates its non-apoptotic roles in the skin.
    Journal of molecular histology 08/2015; 46(4-5). DOI:10.1007/s10735-015-9636-1 · 1.82 Impact Factor
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    • "During the last few years, an extensive research of apoptosis becomes increasingly publicized (Elmore, 2007; Lockshin and Zakeri, 2007; Fulda, 2008; 2009; 2010; Li, 2008; Fulda and Debatin, 2008; Taylor et al., 2008; Vazquez et al., 2008; Youle and Strasser, 2008; Chen and Pervaiz, 2009; Deng et al., 2009; Engel and Henshall, 2009; Lu and El-Deiry, 2009; Circu and Aw; 2010; da Fonseca et al., 2010; Fulda and Pervaiz, 2010; Galluzzi et al., 2010; Lamkanfi and Kanneganti, 2010; Speidel, 2010). This wealth of literature is elaborated for investigating the mechanisms by which different proteins and enzymes are altered and consequently lead to deregulation of apoptosis that is implicated in different diseases (Zhivotovsky and Orrenius, 2010) such as cancers (Chen and Lai, 2009; Buggins and Pepper, 2010; Pennarun et al., 2010), immunologic disorders (Elkon, 2006; Muñoz et al., 2010), neurodegenerative diseases (Yin and Dong, 2003), respiratory diseases; COPD (Makriset et al., 2009), pulmonary hypertension (Jurasz et al., 2010), acute respiratory Distress Syndrome (ARDS) (Galani et al., 2010) and many others. "

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    • "Caspase-7 is highly related to caspase-3, and these two caspases are activated by both death receptorand mitochondria-induced apoptosis (Soung et al., 2003). Besides its activation during apoptosis, proteolytic maturation of caspase-7 has also been observed under inflammatory conditions (Lamkanfi and Kanneganti, 2010). "

    03/2015; DOI:10.4267/2042/56404
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