Regular ArticleCalpain Inhibitors and Serine Protease Inhibitors Can Produce Apoptosis in HL-60 Cells
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Chymotrypsin-like serine proteinases are involved in the maintenance of cell viability
2012, BiochimieCitation Excerpt :TPCK, originally designed as an irreversible inhibitor of chymotrypsin has however, been found to impact on apoptosis in a variety of ways which may not be due to its inhibition of serine proteases e.g. TPCK causes the release of pro-apoptotic factors from the mitochondria, can act as efficient direct inhibitors of mature caspases and may interfere with the cell cycle [33,34]. Activation of apoptosis by TPCK also appears to be dependent upon whether apoptotic stimulation is present [33–35]. We found that when co-incubated with staurosporine, an apoptotic inducer, TPCK had a protective effect on HeLa cell viability (data not shown), which is in agreement with O'Connell et al. [36] and King et al. [33].
Induction of apoptosis in Eμ-myc lymphoma cells in vitro and in vivo through calpain inhibition
2012, Experimental HematologyCitation Excerpt :Previous studies have investigated the use of calpain inhibitors of varying specificity to treat cancer cells in vitro. These include ALLN [22], calpain inhibitor I [42], calpain inhibitor II [23], and aldehyde calpain inhibitors [24]. However, given the similarities in structure among various cysteine proteases, it is not surprising that active site inhibitors have varying degrees of cross-reactivity with other enzymes, such as cathepsins.
Role of the calpain-calpastatin system in the density-dependent growth arrest
2008, Archives of Biochemistry and BiophysicsCitation Excerpt :At concentrations of CI-1 between 0 and 1 μM cell accumulation became similar to that observed in calpastatin transfected cells, promoting 2.5–3 times increase in the density at which cells stop to grow (Fig. 5B, inset). At concentrations of CI-1 higher than 5 μM, a condition providing an almost complete calpain inhibition, cell growth was almost completely arrested, in agreement with previous observations [5,15,16,47,48]. These data indicate that calpain could be required for the transition throughout the cell cycle check points, as well as for favouring the cell entry into the ungrowing G0 stage, both mechanisms probably involved in the regulation of cell proliferation.
Protein phosphatase-1 inhibitor-3 is an in vivo target of caspase-3 and participates in the apoptotic response
2008, Journal of Biological ChemistryCitation Excerpt :All three agents induced the cleavage of Inh3 as well as PARP (Fig. 2F). Cleavage of Inh3 in Vivo during Apoptosis Is Mediated by Caspase-3—As Inh3 is highly sensitive to proteolysis (18), it could be degraded by other caspases or non-caspase proteases that are activated during apoptosis (e.g. the calpains) (58). In order to obtain further evidence that caspase-3 is the agent for the degradation of Inh3 in vivo during apoptosis, the effects of the caspase-3 inhibitor Z-DEVD-fmk (59) were examined.
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