| Literature DB >> 20005201 |
Rajib Sengupta1, Timothy R Billiar, Valerian E Kagan, Detcho A Stoyanovsky.
Abstract
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. Copyright 2009 Elsevier Inc. All rights reserved.Entities:
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Year: 2009 PMID： 20005201 PMCID： PMC2812598 DOI： 10.1016/j.bbrc.2009.12.036
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575