Accéder au contenu
Merck
  • Hypoxia and reoxygenation induce endothelial nitric oxide synthase uncoupling in endothelial cells through tetrahydrobiopterin depletion and S-glutathionylation.

Hypoxia and reoxygenation induce endothelial nitric oxide synthase uncoupling in endothelial cells through tetrahydrobiopterin depletion and S-glutathionylation.

Biochemistry (2014-04-25)
Francesco De Pascali, Craig Hemann, Kindra Samons, Chun-An Chen, Jay L Zweier
RÉSUMÉ

Ischemia-reperfusion injury is accompanied by endothelial hypoxia and reoxygenation that trigger oxidative stress with enhanced superoxide generation and diminished nitric oxide (NO) production leading to endothelial dysfunction. Oxidative depletion of the endothelial NO synthase (eNOS) cofactor tetrahydrobiopterin can trigger eNOS uncoupling, in which the enzyme generates superoxide rather than NO. Recently, it has also been shown that oxidative stress can induce eNOS S-glutathionylation at critical cysteine residues of the reductase site that serves as a redox switch to control eNOS coupling. While superoxide can deplete tetrahydrobiopterin and induce eNOS S-glutathionylation, the extent of and interaction between these processes in the pathogenesis of eNOS dysfunction in endothelial cells following hypoxia and reoxygenation remain unknown. Therefore, studies were performed on endothelial cells subjected to hypoxia and reoxygenation to determine the severity of eNOS uncoupling and the role of cofactor depletion and S-glutathionylation in this process. Hypoxia and reoxygenation of aortic endothelial cells triggered xanthine oxidase-mediated superoxide generation, causing both tetrahydrobiopterin depletion and S-glutathionylation with resultant eNOS uncoupling. Replenishing cells with tetrahydrobiopterin along with increasing intracellular levels of glutathione greatly preserved eNOS activity after hypoxia and reoxygenation, while targeting either mechanism alone only partially ameliorated the decrease in NO. Endothelial oxidative stress, secondary to hypoxia and reoxygenation, uncoupled eNOS with an altered ratio of oxidized to reduced glutathione inducing eNOS S-glutathionylation. These mechanisms triggered by oxidative stress combine to cause eNOS dysfunction with shift of the enzyme from NO to superoxide production. Thus, in endothelial reoxygenation injury, normalization of both tetrahydrobiopterin levels and the glutathione pool are needed for maximal restoration of eNOS function and NO generation.

MATÉRIAUX
Référence du produit
Marque
Description du produit

Sigma-Aldrich
Acétonitrile, suitable for HPLC, gradient grade, ≥99.9%
Sigma-Aldrich
Méthanol, suitable for HPLC, ≥99.9%
Sigma-Aldrich
Méthanol, ACS reagent, ≥99.8%
Sigma-Aldrich
Phosphate de potassium monobasic, ACS reagent, ≥99.0%
Sigma-Aldrich
Acétonitrile, HPLC Plus, ≥99.9%
Sigma-Aldrich
Iodure de potassium, ACS reagent, ≥99.0%
Sigma-Aldrich
Méthanol, HPLC Plus, ≥99.9%
Sigma-Aldrich
Acétate d′ammonium, ACS reagent, ≥97%
Sigma-Aldrich
Acétonitrile, ACS reagent, ≥99.5%
Sigma-Aldrich
DAPI, for nucleic acid staining
Sigma-Aldrich
Iodure de potassium, ReagentPlus®, 99%
Sigma-Aldrich
Acétate d′ammonium, ≥99.99% trace metals basis
Sigma-Aldrich
Phosphate de potassium monobasic, powder, suitable for cell culture, suitable for insect cell culture, suitable for plant cell culture, ≥99.0%
Sigma-Aldrich
Acétonitrile, suitable for HPLC, gradient grade, ≥99.9%
Sigma-Aldrich
Méthanol, suitable for HPLC, gradient grade, suitable as ACS-grade LC reagent, ≥99.9%
Sigma-Aldrich
Acide citrique, meets analytical specification of Ph. Eur., BP, USP, E330, anhydrous, 99.5-100.5% (based on anhydrous substance)
Sigma-Aldrich
L-cystéine, 97%
Sigma-Aldrich
Méthanol, Laboratory Reagent, ≥99.6%
Sigma-Aldrich
L-cystéine, from non-animal source, BioReagent, suitable for cell culture, ≥98%
Sigma-Aldrich
Iodure de potassium, anhydrous, free-flowing, Redi-Dri, ACS reagent, ≥99%
Sigma-Aldrich
Acétate d′ammonium, for molecular biology, ≥98%
Sigma-Aldrich
Méthanol, ACS spectrophotometric grade, ≥99.9%
Sigma-Aldrich
Acétate d′ammonium solution, for molecular biology, 7.5 M
Sigma-Aldrich
Méthanol, BioReagent, ≥99.93%
Sigma-Aldrich
Diethylenetriaminepentaacetic acid, ≥98% (titration)
Sigma-Aldrich
Méthanol, ACS reagent, ≥99.8%
Sigma-Aldrich
Phosphate de potassium monobasic, for molecular biology, ≥98.0%
Sigma-Aldrich
L-cystéine, BioUltra, ≥98.5% (RT)
Sigma-Aldrich
Méthanol, Absolute - Acetone free
Sigma-Aldrich
Menadione, crystalline