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Interaction of cytocidal drugs and the inhibition of caspase‐3 by 3‐nitrosobenzamide
Author(s) -
Mihalik Rudolf,
Bauer Páll,
Peták István,
Krajcsi Péter,
Marton Attila,
Kun Ernest,
Kopper László
Publication year - 1999
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/(sici)1097-0215(19990909)82:6<875::aid-ijc17>3.0.co;2-t
Subject(s) - staurosporine , dna fragmentation , apoptosis , etoposide , programmed cell death , microbiology and biotechnology , caspase , biology , cancer research , caspase 3 , fragmentation (computing) , caspase 8 , chemistry , enzyme , biochemistry , genetics , chemotherapy , protein kinase c , ecology
The effect of 3‐nitrosobenzamide (NOBA) on the etoposide, staurosporine and dexamethason induced rapid (4–6 hr), caspase‐dependent apoptosis was investigated in thymocytes and lymphoma cells by flow cytometric assay of DNA fragmentation. When NOBA (ED 50 = 4 μM) was added to these cell systems, the rapid onset of apoptosis was prevented. Such apparent protection by NOBA was related to the inactivation of caspase‐3, by s‐nitrosylation of 1.3 mol –SH per enzyme molecule out of 7 –SH groups. Since NOBA by itself induces DNA fragmentation within 18 hr in lymphoma cells, our results indicate that at least two active cell death pathways exist with apparent dissimilar kinetics and molecular mechanisms. Int. J. Cancer 82:875–879, 1999. © 1999 Wiley‐Liss, Inc.