Nitric oxide and thioredoxin type 1 modulate the activity of caspase 8 in HepG2 cells

Rajib Sengupta; Timothy R. Billiar; Valerian E. Kagan; Detcho A. Stoyanovsky

doi:10.1016/j.bbrc.2009.12.036

Nitric oxide and thioredoxin type 1 modulate the activity of caspase 8 in HepG2 cells

Rajib Sengupta, Timothy R. Billiar, Valerian E. Kagan, Detcho A. Stoyanovsky^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

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.

Original language	English
Pages (from-to)	1127-1130
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	391
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2009.12.036
State	Published - 1 Jan 2010
Externally published	Yes

Keywords

Apoptosis
Caspase 8
Lipoic acid
Nitric oxide
Thioredoxin

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10.1016/j.bbrc.2009.12.036

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title = "Nitric oxide and thioredoxin type 1 modulate the activity of caspase 8 in HepG2 cells",

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.",

keywords = "Apoptosis, Caspase 8, Lipoic acid, Nitric oxide, Thioredoxin",

author = "Rajib Sengupta and Billiar, {Timothy R.} and Kagan, {Valerian E.} and Stoyanovsky, {Detcho A.}",

note = "Funding Information: This work was funded by U.S. Public Health Service Grants R37-GM44100 , RO1HL094488 and RO1HL70755 from the National Institute of Health .",

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AU - Billiar, Timothy R.

AU - Kagan, Valerian E.

AU - Stoyanovsky, Detcho A.

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N2 - 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.

AB - 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.

KW - Apoptosis

KW - Caspase 8

KW - Lipoic acid

KW - Nitric oxide

KW - Thioredoxin

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Nitric oxide and thioredoxin type 1 modulate the activity of caspase 8 in HepG2 cells

Abstract

Keywords

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