Glutathione promotes prostaglandin H synthase (cyclooxygenase)-dependent formation of malondialdehyde and 15(S)-8-iso-prostaglandin F2α
| Autor: | Frank-Mathias Gutzki, Sabine Rothmann, Dirk O. Stichtenoth, Paschalis Tossios, Yessica Schneider, Jürgen C. Frölich, Maria-Theresia Suchy, Dimitrios Tsikas, Jonas Niemann |
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| Rok vydání: | 2012 |
| Předmět: |
Male
Biophysics Prostaglandin medicine.disease_cause Prostaglandin H synthase Dinoprost Biochemistry chemistry.chemical_compound Thromboxane A2 Structural Biology Malondialdehyde Genetics medicine Animals Humans Molecular Biology Aged chemistry.chemical_classification Arachidonic Acid Sheep biology Cell Biology Glutathione Biomarker Cyclooxygenase Enzyme chemistry Oxidative stress Cyclooxygenase 2 biology.protein Cyclooxygenase 1 lipids (amino acids peptides and proteins) Arachidonic acid Female |
| Zdroj: | FEBS letters. 586(20) |
| ISSN: | 1873-3468 |
| Popis: | Prostaglandin (PG) H synthases (PGHS) or cyclooxygenases (COX) catalyse the peroxidation of arachidonic acid (AA) to PGG(2) and PGH(2) which are further converted to a series of prostaglandins and thromboxane A(2). Here, we report that GSH promotes concomitant formation of the current oxidative stress biomarkers malondialdehyde (MDA) and 15(S)-8-iso-prostaglandin F(2α) from AA via PGHS. This illustrates an uncommon interplay of enzymatic and chemical reactions to produce species that are considered to be exclusively produced by free-radical-catalysed reactions. We propose mechanisms for the PGHS/AA/GSH-dependent formation of MDA, 15(S)-8-iso-prostaglandin F(2α) and other F(2)-isoprostanes. These mechanisms are supported by clinical observations. |
| Databáze: | OpenAIRE |
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