Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 57, Issue 4, Pages 612-622Publisher
BIRKHAUSER VERLAG AG
DOI: 10.1007/PL00000723
Keywords
nitric oxide; S-nitrosylation; apoptosis
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Nitric oxide (NO) and its related molecules are important messengers that play central roles in pathophysiology. Redox modulation of thiol groups on protein cysteine residues by S-nitrosylation can modulate protein function. NO has emerged as a potent regulator of apoptosis in many cell types, either preventing cell death or driving an apoptotic response into a necrotic one. NO protects neuroblastoma cells from retinoid- and cisplatin-induced apoptosis, without significantly increasing necrotic cell damage. Nitrosylation of thiol groups of several critical factors may be important for cell survival. Indeed, S-nitrosylation of the active-site cysteine residue of apoptotic molecules, such as caspases and tissue transglutaminase, results in the inhibition of their catalytic activities and has important implications for the regulation of apoptosis by NO. On the other hand, NO is able to shift the anti-CD95- and ceramide-triggered apoptotic response of Jurkat T cells into necrotic cell death, in these apoptotic models, NO is therefore unable to solely inhibit cell death, indicating that it may act below the Feint of no return elicited by CD95-ligation and ceramide stimulation.
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