Abstract
We found that a novel protease inhibitor, benzyloxycarbonyl-Asp-CH2OC(O)-2,6-dichlorobenzene (Z-Asp-CH2-DCB), which can preferentially inhibit interleukin-1 beta-converting enzyme (ICE), completely blocked the apoptotic cell death of human myeloid leukemia U937 cells caused by etoposide, camptothecin, 1-beta-D-arabinofuranosyl-cytosine and Adriamycin, as well as TNF-alpha, 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antineoplastic Agents / pharmacology*
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Apoptosis / drug effects*
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Aspartic Acid / analogs & derivatives*
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Aspartic Acid / pharmacology
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Camptothecin / pharmacology
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Caspase 1
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Cell Cycle / drug effects
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Cell Line
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Cysteine Endopeptidases / pharmacology*
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Cytarabine / pharmacology
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DNA, Neoplasm / analysis
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DNA, Neoplasm / drug effects
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Doxorubicin / pharmacology
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Etoposide / pharmacology
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Humans
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Kinetics
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Leukemia, Myeloid
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Time Factors
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Tumor Cells, Cultured
Substances
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Antineoplastic Agents
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DNA, Neoplasm
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benzyloxycarbonyl-Asp-CH2OC(O)-2,6-dichlorobenzene
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Cytarabine
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Aspartic Acid
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Etoposide
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Doxorubicin
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Cysteine Endopeptidases
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Caspase 1
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Camptothecin