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Catechin derivatives: Specific inhibitor for caspases‐3, 7 and 2, and the prevention of apoptosis at the cell and animal levels
Author(s) -
Katunuma Nobuhiko,
Ohashi Atsushi,
Sano Etsuko,
Ishimaru Naozumi,
Hayashi Yoshio,
Murata Etsuko
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.087
Subject(s) - apoptosis , caspase , catechin , chemistry , hela , biochemistry , microbiology and biotechnology , in vitro , pharmacology , biology , programmed cell death , polyphenol , antioxidant
Tea‐catechin derivatives are shown to inhibit activities of caspases‐3, 2 and 7 in vitro, and prevented experimental apoptosis at the cell and animal levels. Epigallo‐catechin‐gallate showed the strongest inhibition at 1 × 10 −7 M to these caspases, but cysteine cathepsins and caspase‐8 were not inhibited. Caspase‐3 inhibition showed a 2nd‐order allosteric‐type, but the inhibition of caspases‐2 and 7 showed a non‐competitive‐type. The apoptosis‐test using cultured HeLa cells was inhibited by these catechins. In rat hepatocytes, apoptosis was induced by d ‐galactosamine in vivo. In this case, caspase‐3 activity in the cytoplasm, the serum aminotransferases and dUTP nick formation detected by TUNNEL‐staining were effects, and these elevations were suppressed by administration of catechin.