Abstract
We found that a novel protease inhibitor, benzyloxycarbonyl-Asp-CH2OC(O)-2,6,-dichlorobenzene (Z-Asp-CH2-DCB), which can preferentially inhibit interleukin-1β-converting enzyme (ICE), completely blocked the apoptotic cell death of human myeloid leukemia U937 cells caused by etoposide, camptothecin, 1-β-D-arabinofuranosyl-cytosine and Adriamycin, as well as TNF-α ,anti-Fas antibody and staurosporine. However, Z-Asp-CH2-DCB did not block non-apoptotic cell death of U937 cells caused by etoposide during prolonged incubation periods. These results indicate that ICE or ICE-like proteases inhibited by Z-Asp-CH2-DCB are involved in a common pathway of apoptotic cell death in U937 cells.
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