دورية أكاديمية
Inhibition of cytochrome c oxidase activity by 4-hydroxynonenal (HNE). Role of HNE adduct formation with the enzyme subunits.
| العنوان: | Inhibition of cytochrome c oxidase activity by 4-hydroxynonenal (HNE). Role of HNE adduct formation with the enzyme subunits. |
|---|---|
| المؤلفون: | Chen J; Department of Medicine, Division of Gastroenterology and Nutrition, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7878, USA., Schenker S, Frosto TA, Henderson GI |
| المصدر: | Biochimica et biophysica acta [Biochim Biophys Acta] 1998 May 08; Vol. 1380 (3), pp. 336-44. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam : Elsevier Pub. Co. |
| مواضيع طبية MeSH: | Aldehydes/*metabolism , Aldehydes/*pharmacology , Electron Transport Complex IV/*antagonists & inhibitors , Electron Transport Complex IV/*metabolism, Animals ; Enzyme Activation/drug effects ; Lipid Peroxidation/drug effects ; Liver/enzymology ; Male ; Mitochondria, Liver/drug effects ; Mitochondria, Liver/enzymology ; Oxidative Stress/drug effects ; Rats ; Rats, Sprague-Dawley |
| مستخلص: | The role of 4-hydroxynonenal (HNE), a major lipid peroxidation product, in oxidative damage to mitochondrial cytochrome c oxidase (COX) was examined. Oxidative stress was induced in mitochondria isolated from livers of male Sprague-Dawley rats by tert-butylhydroperoxide (t-BHP). COX activity was inhibited, with a concomitant increase in endogenous HNE level in mitochondria. COX activity was also inhibited following incubation of mitochondria with 50-450 microM HNE. Blocking HNE degradation intensified COX inhibition by HNE and by t-BHP-induced oxidative stress, the latter accompanied by a simultaneous increase in endogenous HNE production. On the other hand, COX inhibition by HNE was markedly reduced by potentiating HNE degradation via enhancing conjugation of HNE with reduced glutathione (GSH). Incubation of purified COX with 10-400 microM HNE resulted in HNE adduct formation with specific subunits of COX, correlated with inhibition of the enzyme activity. These data suggest that HNE may inhibit mitochondrial COX by forming adducts with the enzyme, and that this could be one mechanism underlying mitochondrial damage caused by oxidative stress. The findings also illustrate a role for GSH in protecting mitochondria from the deleterious effects of HNE. (Copyright 1998 Elsevier Science B.V.) |
| المشرفين على المادة: | 0 (Aldehydes) EC 1.9.3.1 (Electron Transport Complex IV) K1CVM13F96 (4-hydroxy-2-nonenal) |
| تواريخ الأحداث: | Date Created: 19980523 Date Completed: 19980519 Latest Revision: 20190610 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/s0304-4165(98)00002-6 |
| PMID: | 9555085 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0006-3002 |
|---|---|
| DOI: | 10.1016/s0304-4165(98)00002-6 |