Genetic responses against nitric oxide toxicity

The threat of free radical damage is opposed by coordinated responses that modulate expression of sets of gene products. In mammalian cells, 12 proteins are induced by exposure to nitric oxide (NO) levels that are sub-toxic but exceed the level needed to activate guanylate cyclase. Heme oxygenase 1...

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Published inBrazilian journal of medical and biological research Vol. 32; no. 11; pp. 1417 - 1427
Main Author Demple, B
Format Journal Article
LanguageEnglish
Portuguese
Published Brazil Associação Brasileira de Divulgação Científica 01.11.1999
Subjects
Animals
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
BIOLOGY
Blotting, Northern
Cell Line
Dose-Response Relationship, Drug
Drug Resistance
Enzyme Induction - drug effects
Fibroblasts - drug effects
Fibroblasts - enzymology
Gene Expression
HeLa Cells - drug effects
HeLa Cells - enzymology
Heme Oxygenase (Decyclizing) - antagonists & inhibitors
Heme Oxygenase (Decyclizing) - genetics
Heme Oxygenase (Decyclizing) - metabolism
Heme Oxygenase-1
Humans
MEDICINE, RESEARCH & EXPERIMENTAL
Membrane Proteins
Motor Neurons - drug effects
Motor Neurons - enzymology
Nitric Oxide - toxicity
Oxidative Stress
RNA stability
RNA, Messenger - genetics
RNA, Messenger - metabolism
SoxR protein
Time Factors
Transcription Factors - genetics
Transcription Factors - metabolism
Transcription, Genetic
transcriptional regulation
RNA stability
SoxR protein
transcriptional regulation
oxidative stress
heme oxygenase 1
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Abstract The threat of free radical damage is opposed by coordinated responses that modulate expression of sets of gene products. In mammalian cells, 12 proteins are induced by exposure to nitric oxide (NO) levels that are sub-toxic but exceed the level needed to activate guanylate cyclase. Heme oxygenase 1 (HO-1) synthesis increases substantially, due to a 30- to 70-fold increase in the level of HO-1 mRNA. HO-1 induction is cGMP-independent and occurs mainly through increased mRNA stability, which therefore indicates a new NO-signaling pathway. HO-1 induction contributes to dramatically increased NO resistance and, together with the other inducible functions, constitutes an adaptive resistance pathway that also defends against oxidants such as H2O2. In E. coli, an oxidative stress response, the soxRS regulon, is activated by direct exposure of E. coli to NO, or by NO generated in murine macrophages after phagocytosis of the bacteria. This response is governed by the SoxR protein, a homodimeric transcription factor (17-kDa subunits) containing [2Fe-2S] clusters essential for its activity. SoxR responds to superoxide stress through one-electron oxidation of the iron-sulfur centers, but such oxidation is not observed in reactions of NO with SoxR. Instead, NO nitrosylates the iron-sulfur centers of SoxR both in vitro and in intact cells, which yields a form of the protein with maximal transcriptional activity. Although nitrosylated SoxR is very stable in purified form, the spectroscopic signals for the nitrosylated iron-sulfur centers disappear rapidly in vivo, indicating an active process to reverse or eliminate them.
AbstractList The threat of free radical damage is opposed by coordinated responses that modulate expression of sets of gene products. In mammalian cells, 12 proteins are induced by exposure to nitric oxide (NO) levels that are sub-toxic but exceed the level needed to activate guanylate cyclase. Heme oxygenase 1 (HO-1) synthesis increases substantially, due to a 30- to 70-fold increase in the level of HO-1 mRNA. HO-1 induction is cGMP-independent and occurs mainly through increased mRNA stability, which therefore indicates a new NO-signaling pathway. HO-1 induction contributes to dramatically increased NO resistance and, together with the other inducible functions, constitutes an adaptive resistance pathway that also defends against oxidants such as H2O2. In E. coli, an oxidative stress response, the soxRS regulon, is activated by direct exposure of E. coli to NO, or by NO generated in murine macrophages after phagocytosis of the bacteria. This response is governed by the SoxR protein, a homodimeric transcription factor (17-kDa subunits) containing [2Fe-2S] clusters essential for its activity. SoxR responds to superoxide stress through one-electron oxidation of the iron-sulfur centers, but such oxidation is not observed in reactions of NO with SoxR. Instead, NO nitrosylates the iron-sulfur centers of SoxR both in vitro and in intact cells, which yields a form of the protein with maximal transcriptional activity. Although nitrosylated SoxR is very stable in purified form, the spectroscopic signals for the nitrosylated iron-sulfur centers disappear rapidly in vivo, indicating an active process to reverse or eliminate them.
Author Demple, B
AuthorAffiliation Harvard School of Public Health
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  surname: Demple
  fullname: Demple, B
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Issue 11
Keywords RNA stability
SoxR protein
transcriptional regulation
oxidative stress
heme oxygenase 1
Language English
Portuguese
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Snippet The threat of free radical damage is opposed by coordinated responses that modulate expression of sets of gene products. In mammalian cells, 12 proteins are...
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SubjectTerms Animals
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
BIOLOGY
Blotting, Northern
Cell Line
Dose-Response Relationship, Drug
Drug Resistance
Enzyme Induction - drug effects
Fibroblasts - drug effects
Fibroblasts - enzymology
Gene Expression
HeLa Cells - drug effects
HeLa Cells - enzymology
Heme Oxygenase (Decyclizing) - antagonists & inhibitors
Heme Oxygenase (Decyclizing) - genetics
Heme Oxygenase (Decyclizing) - metabolism
Heme Oxygenase-1
Humans
MEDICINE, RESEARCH & EXPERIMENTAL
Membrane Proteins
Motor Neurons - drug effects
Motor Neurons - enzymology
Nitric Oxide - toxicity
Oxidative Stress
RNA stability
RNA, Messenger - genetics
RNA, Messenger - metabolism
SoxR protein
Time Factors
Transcription Factors - genetics
Transcription Factors - metabolism
Transcription, Genetic
transcriptional regulation
Title Genetic responses against nitric oxide toxicity
URI https://www.ncbi.nlm.nih.gov/pubmed/10559844
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999001100013&lng=en&tlng=en
https://doaj.org/article/460e992fab084786b7f15fd7bbee609b
Volume 32
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