کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10739599 | 1046881 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
N-acetylcysteine amide, a novel cell-permeating thiol, restores cellular glutathione and protects human red blood cells from oxidative stress
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کلمات کلیدی
G-6-PDCFHRBCGSSGDCFH-DAGPXNACGSHG-6-PDDTTBuOHDcfRed blood cells - سلولهای قرمز خون2′,7′-dichlorofluorescein - 2 '، 7'-dichlorofluorescein2′,7′-dichlorofluorescin - 2 '، 7'-dichlorofluorescin2′,7′-dichlorofluorescin diacetate - 2 '، 7'-dichlorofluorescin diacetateN-acetylcysteine - N-استیل سیستئینdithiobis-2-nitrobenzoic acid - اسید دیاتیوئیک 2-نیتربنزوئیکOxidative stress - تنش اکسیداتیوNeurodegeneration - تولید نوروژنیکdithiothreitol - دیتیوتریتولFree radicals - رادیکال آزادHemoglobin - هموگلوبینHuman red blood cells - گلبول های قرمز انسانGlutathione - گلوتاتیونGlutathione (reduced) - گلوتاتیون (کاهش یافته)glutathione disulfide - گلوتاتیون دی سولفیدglutathione reductase - گلوتاتیون ردوکتازglutathione peroxidase - گلوتاتیون پراکسیدازGlucose 6-phosphate - گلوکز 6-فسفاتglucose-6-phosphate dehydrogenase - گلوکز 6-فسفات دهیدروژناز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Oxidative stress plays an important role in the progression of neurodegenerative and age-related diseases, causing damage to proteins, DNA, and lipids. A novel thiol N-acetylcysteine amide (AD4), the amide form of N-acetylcysteine (NAC) and a Cu2+ chelator, was assessed for its antioxidant and protective effects using human red blood cells (RBCs) as a model. AD4 was shown by flow cytometry to inhibit tert.-butylhydroxyperoxide (BuOOH)-induced intracellular oxidation in RBCs stained with the oxidant-sensitive probe 2â²,7â²-dichlorofluorescein diacetate. In addition, AD4 retarded BuOOH-induced thiol depletion and hemoglobin oxidation. Restoration of the thiol-depleted RBCs by externally applied AD4 was significantly greater compared with NAC and, unlike NAC, was accompanied by hemoglobin protection from oxidation. In a cell-free system we have demonstrated that AD4 reacted with oxidized glutathione (GSSG) to generate reduced glutathione (GSH). The formation of GSH was determined enzymatically using GSH peroxidase and by HPLC. Based on these results a thiol-disulfide exchange between AD4 and GSSG is proposed as the mechanism underlying the antioxidant effects of AD4 on BuOOH-treated RBCs. Together, these studies demonstrate that AD4 readily crosses cell membranes, replenishes intracellular GSH, and, by incorporating into the redox machinery, defends the cell from oxidation. These results provide further evidence for the efficient membrane permeation of AD4 over NAC, and support the possibility that it could be explored for treatment of neurodegeneration and other oxidation-mediated disorders.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 38, Issue 1, 1 January 2005, Pages 136-145
Journal: Free Radical Biology and Medicine - Volume 38, Issue 1, 1 January 2005, Pages 136-145
نویسندگان
Leonid Grinberg, Eitan Fibach, Johnny Amer, Daphne Atlas,