کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1910559 | 1046776 | 2008 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease
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کلمات کلیدی
MUFAAASAPrPscPrPcCJDDBIPrPCMLSFACarboxyethyllysineGSAMDALMCOBSECelAminoadipic SemialdehydeROS - ROSPolyunsaturated fatty acids - اسید چرب اشباع نشدهPUFA - اسید چرب چند غیراشباعmonounsaturated fatty acids - اسیدهای چرب غیر اشباعProtein oxidation - اکسیداسیون پروتئینMetal-catalyzed oxidation - اکسیداسیون کاتالیزور فلزیCreutzfeldt-Jakob disease - بیماری Creutzfeldt-JakobPrion disease - بیماری پریونBovine spongiform encephalopathy - جنون گاویdouble bond index - شاخص باند دوگانهPeroxidizability index - شاخص پراکسید پذیریMass spectrometry - طیف سنجی جرمیglutamic semialdehyde - نیمه آلدئید گلوتامیکPrion protein - پروتئین پریونCarboxymethyllysine - کربوکسی اتیلیزینReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
The basic molecular underpinnings of the pathological changes that unfold in prion disease remain elusive. A key role of increased oxidative stress has been hypothesized. Given the transient nature of most intermediate molecules implicated, increased oxidative stress is better assessed by quantitating the damage it causes to macromolecules. We used mass spectrometry-based methods to measure specific products of protein oxidation, glycoxidation, and lipoxidation in brains from patients suffering from Creutzfeldt-Jakob disease and Syrian hamsters affected by scrapie. In both cases, increased amounts of glutamic and aminoadipic semialdehydes, products of metal-catalyzed oxidation, malondialdehydelysine (a product of lipoxidation), N-É-carboxyethyllysine (a product of glycoxidation), and N-É-carboxymethyllysine (generated by lipoxidation and glycoxidation) were measured. PrPSc, the infectious isoform of the prion protein that accumulates in prion disease, was itself shown to be a target of increased oxidative modification. These changes were accompanied by alterations in fatty acid composition and increased phosphorylation of ERK1/2 and p38, protein kinases known to respond to increased flows of ROS. These data support an important role of oxidative damage in the pathology of prion disease.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 45, Issue 8, 15 October 2008, Pages 1159-1166
Journal: Free Radical Biology and Medicine - Volume 45, Issue 8, 15 October 2008, Pages 1159-1166
نویسندگان
Reinald Pamplona, Alba NaudÃ, Rosalina GavÃn, Miguel A. Pastrana, Gustavo Sajnani, Ekaterina V. Ilieva, José Antonio del RÃo, Manuel Portero-OtÃn, Isidre Ferrer, Jesús R. Requena,