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Nitric Oxide & Oxidative Stress 
Targets for NO in Plants

Nitric oxide (NO) can mediate cellular effects through the second messenger cGMP or by direct interaction with target proteins. The mechanisms of direct interaction of NO with target proteins includes S-nitrosylation of thiol-containing proteins and tyrosine nitration, as well as direct interaction of NO with metal-containing proteins. NO signaling is essential for pathogen defense pathways in plants. Navarre et al. have discovered that tobacco aconitase (an iron-sulfur-containing enzyme) is inhibited in vitro by NO via a direct interaction. Animal aconitases play an important role in regulating cellular metabolism in response to oxidative stress and in regulating iron homeostasis by controlling translation of iron-responsive genes. It remains to be determined whether the plant aconitases have similar functions.

Navarre, D.A., Wendehenne, D., Durner, J., Noad, R., and Klessig, D.F. (2000) Nitric oxide modulates the activity of tobacco aconitase. Plant Phys. 122: 573-582. [Abstract] [Full Text]

FEBS Lett 2000 Jan 21;466(1):187-191 Related Articles, LinkOut
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Peroxynitrite generated from constitutive nitric oxide synthase mediates the early biochemical injury in short-term cultured hepatocytes .

Lopez-Garcia MP, Sanz-Gonzalez SM

Departamento de Bioquimica y Biologia Molecular, Facultad de Farmacia, Universidad de Valencia, Valencia, Spain

[Record supplied by publisher]

Early loss of P450 in rat hepatocyte cultures appears directly related to nitric oxide (NO) overproduction. This study provides experimental evidence for the induction - shortly after isolation through the classical procedure - of strong oxidative stress that involves both oxygen-derived and NO-derived species. NO formation at this stage is due to the early activation of liver constitutive NO synthase (cNOS). Immunodetection of nitrated proteins provides direct evidence of endogenous peroxynitrite (PN) formation upon hepatocyte isolation. On the basis of the combined use of dihydrorhodamine 123 and NOS inhibitors, the analysis of the amount, time course and nature of the species involved supports the view that PN generated from cNOS-derived NO, while not affecting cell viability and hepatocyte monolayer development, is the main species likely responsible for the early biochemical injury commonly observed in hepatocyte cultures.

: FEBS Lett 1998 Nov 6;438(3):145-9 Related Articles

Endogenous nitric oxide is responsible for the early loss of P450 in cultured rat hepatocytes .

Lopez-Garcia MP

Department of Biochemistry and Molecular Biology, Facultad de Farmacia, Universidad de Valencia, Spain.

Loss of P450 during the early hours of monolayer formation is known to be the more serious limitation of primary cultured hepatocytes as an adequate model for the study of drug metabolism , toxicity and P450 induction. This study reports that endogenous nitric oxide (NO) formation is activated shortly after isolation by the classical collagenase -based liver perfusion methods. Both rapid P450 loss and aerobic mitochondrial energy metabolism impairment -- with subsequent changes on glucose metabolism -- are directly related to the high local generation of the radical at this stage. These effects can be reverted by the sole addition of NO biosynthesis inhibitors during liver perfusion and early culture hours, which allows catalytically active P450 to be preserved at levels close to those of the intact liver.

Rauhala P, Khaldi A, Mohanakumar KP, Chiueh CC. Pitfalls of SNP Related Articles
Apparent role of hydroxyl radicals in oxidative brain injury induced by sodium nitroprusside.
Free Radic Biol Med. 1998 May;24(7-8):1065-73.
PMID: 9626559; UI: 98289861

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