Abstract
Caspase inhibitor Z-VAD-FMK potentiated heat shock-induced apoptosis in macrophages. Z-VAD-FMK did not activate HSP70 synthesis, but significantly increased the intensity of this process during heat shock. It cannot be excluded that caspases abolish HSP70 accumulation under these conditions. The HSP70 synthesis inhibitor quercetin potentiated DNA fragmentation in macrophages cocultured with Z-VAD-FMK after heat shock. HSP70 play an important role in the protection of macrophages from caspase-independent apoptosis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Chloromethyl Ketones / pharmacology*
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Animals
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Apoptosis*
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Caspase Inhibitors*
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Caspases / metabolism
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Cysteine Proteinase Inhibitors / pharmacology*
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HSP70 Heat-Shock Proteins / antagonists & inhibitors
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HSP70 Heat-Shock Proteins / metabolism*
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Heat-Shock Response*
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Macrophages / drug effects*
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Macrophages / enzymology
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Male
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Mice
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Quercetin / pharmacology
Substances
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Amino Acid Chloromethyl Ketones
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Caspase Inhibitors
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Cysteine Proteinase Inhibitors
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HSP70 Heat-Shock Proteins
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benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone
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Quercetin
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Caspases