کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9416642 | 1614337 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mechanisms of 4-hydroxynonenal-induced neuronal microtubule dysfunction
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
PBSDMEMFBS4-hydroxynonenalGTP4-hydroxy-2(E)-nonenalEGTADemGSHHRPBSOHNE2-[N-morpholino]ethanesulfonic acid - 2- [N-مورفولینو] اتان سولفونیک اسیدDulbecco's modified Eagle Medium - Eagle Medium اصلاح شده DulbeccoDisorders of the nervous system - اختلالات سیستم عصبیDegenerative disease: Alzheimer's—miscellaneous - بیماری تخریب پذیر: آلزایمر- متفرقهtubulin - توبولینdiethyl maleate - دی اتیل مولاناMicrotubule - ریزلوله یا میکروتوبولfetal bovine serum - سرم جنین گاوsulfhydryl - سولفیدریلPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریMeS - مسMaps - نقشه هاHorseradish peroxidase - پراکسیداز هوررادیشmicrotubule-associated proteins - پروتئین های مرتبط با میکروتوبولTubulin polymerization - پلیمریزاسیون توبولینGlutathione - گلوتاتیونguanosine 5′-triphosphate - گوانوزین 5'-تری فسفات
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Mechanisms of 4-hydroxynonenal-induced neuronal microtubule dysfunction Mechanisms of 4-hydroxynonenal-induced neuronal microtubule dysfunction](/preview/png/9416642.png)
چکیده انگلیسی
We have previously demonstrated that neuronal microtubules are exquisitely sensitive to the lipid peroxidation product 4-hydroxynonenal (HNE). The mechanism, however, by which HNE disrupts the microtubules, is not known. Sulfhydryl groups of protein-cysteines constitute main targets of HNE. Indeed, HNE is mainly detoxified by conjugation to glutathione (GSH), a reaction that leads to depletion of cellular GSH. GSH maintains protein sulfhydryl groups in the reduced form and has been implicated in the regulation of cytoskeletal function. Here, we assess what role depletion of cellular GSH plays in the HNE-induced microtubule disruption. We demonstrate that HNE and its intracellularly activated tri-ester analog, HNE(Ac)3, cause substantial GSH depletion in Neuro2A cells. However, other compounds inducing GSH depletion had no effect on the microtubule network. Therefore, HNE-induced depletion of cellular GSH does not contribute to the HNE-induced microtubule disruption. We previously demonstrated that another main cellular target of HNE is tubulin, the core protein of microtubules containing abundant cysteines. The functional relevance of this adduction, however, had not been evaluated. Here, we demonstrate that exposure of Neuro 2A cells to HNE or HNE(Ac)3 results in the inhibition of cytosolic taxol-induced tubulin polymerization. These and our previous observations strongly support the hypothesis that HNE-adduction to tubulin is the primary mechanism involved in the HNE-induced loss of the highly dynamic neuronal microtubule network.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Brain Research - Volume 1037, Issues 1â2, 10 March 2005, Pages 90-98
Journal: Brain Research - Volume 1037, Issues 1â2, 10 March 2005, Pages 90-98
نویسندگان
M. Diana Neely, A. Boutte, D. Milatovic, Thomas J. Montine,