Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 391, Issue 1, Pages 1127-1130Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.12.036
Keywords
Caspase 8; Thioredoxin; Nitric oxide; Lipoic acid; Apoptosis
Categories
Funding
- U.S. Public Health Service [R37-GM44100, RO1HL094488, RO1HL70755]
- National institute of Health
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL070755, R01HL094488] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM044100] Funding Source: NIH RePORTER
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Herein, we report that nitric oxide (NO) and the thioredoxin/thioredoxin reductase system affect the activity of caspase 8 in HepG2 cells. Exposure of cells to NO resulted in inhibition of caspase 8, while a subsequent incubation of the cells in NO-free medium resulted in spontaneous reactivation of the protease. The latter process was inhibited in thioredoxin reductase-deficient HepG2 cells, in which, however, lipoic acid markedly reactivated caspase 8. The data obtained suggest that extrinsic apoptosis can be subjected to redox regulation before induction of proteolytic damage by caspase 3. (C) 2009 Elsevier Inc. All rights reserved.
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