Effect of glutathione on endothelial prostacyclin synthesis after anoxia
Autor: | A. A. Spector, S. L. Hempel, D. A. Wessels |
---|---|
Rok vydání: | 1993 |
Předmět: |
medicine.medical_specialty
Antioxidant Endothelium Physiology medicine.medical_treatment Glutathione reductase Prostaglandin Prostacyclin GPX4 chemistry.chemical_compound Internal medicine medicine Humans Hypoxia chemistry.chemical_classification Arachidonic Acid Chemistry Glutathione peroxidase Intracellular Membranes Cell Biology Glutathione Oxidants Epoprostenol Oxygen Endocrinology medicine.anatomical_structure Prostaglandin-Endoperoxide Synthases Endothelium Vascular medicine.drug |
Zdroj: | American Journal of Physiology-Cell Physiology. 264:C1448-C1457 |
ISSN: | 1522-1563 0363-6143 |
DOI: | 10.1152/ajpcell.1993.264.6.c1448 |
Popis: | We previously observed decreased prostacyclin (PGI2) formation after reoxygenation of anoxic endothelium. In the present study, the effects of glutathione on endothelial prostaglandin (PG) H synthase activity after reoxygenation were explored. Intracellular glutathione content decreased 70% after 24 h of anoxia; reoxygenation did not produce any additional decrease in glutathione content. Intracellular glutathione was maintained in the reduced state by the endothelium even during the oxidant stress caused by reoxygenation or the addition of peroxide. Glutathione depletion produced by DL-buthionine-(S,R)-sulfoximine (BSO), 1,3-bis(chloroethyl)1-nitrosourea (BCNU), or incubation in a sulfhydryl-free medium resulted in increased sensitivity of PGH synthase to the effects of added H2O2. However, glutathione depletion resulting from BSO or culture in sulfhydryl-free medium during anoxia did not increase the sensitivity of PGH synthase to reoxygenation. In addition, anoxia did not make the endothelium more sensitive to H2O2. Glutathione peroxidase and glutathione reductase activities were preserved after anoxia-reoxygenation. When glutathione reductase was inhibited with BCNU during reoxygenation, PGI2 release was decreased further. These findings demonstrate that, although anoxia decreases endothelial glutathione content, the endothelium is able to utilize its remaining glutathione to protect against additional oxidant stress because glutathione peroxidase and glutathione reductase retain their activity. |
Databáze: | OpenAIRE |
Externí odkaz: |