کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9989565 | 1580760 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Proteomic analysis of glial fibrillary acidic protein in Alzheimer's disease and aging brain
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کلمات کلیدی
2-DEPost-mortem delayPTMAPPβACTM2-DNFTN-acetylgalactosamineGFAP1-DAUC - AUCPMd - PMDReactive astrocytes - آستروسیتهای واکنشیpost-translational modification - اصلاح post-translationaltwo-dimensional gel electrophoresis - الکتروفورز ژل دو بعدیOxidation - اکسیداسیونImmunoblotting - ایمن سازیBeta-amyloid - بتا آمیلوئیدAlzheimer's disease - بیماری آلزایمرNeurofibrillary tangle - خلط نوروفیبریلاtwo-dimensional - دو بعدیendoplasmatic reticulum - سلولهای اندوپلاسمیPhosphorylation - فسفریلاسیونBrain - مغزarea under curve - منطقه تحت منحنیIsoelectric point - نقطه ایزوالکتریکMolecular weight - وزن مولکولیProteomics - پروتئومیکسGlial fibrillary acidic protein - پروتئین اسیدی فیبریلاسیون گلایالamyloid precursor protein - پروتئین پیش ماده آمیلوئیPost-mortem - پس از مرگGlycosylation - گلیکوزیله شدنone-dimensional - یک بعدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
عصب شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Chronic inflammation is known to play an important role in the heterogeneous pathogenesis of Alzheimer's disease (AD). Activated astrocytes expressing glial fibrillary acidic protein (GFAP) are closely associated with AD pathology, such as tangles, neuritic plaques and amyloid depositions. Altogether, 46 soluble isoforms of GFAP were separated and most of them quantified by two-dimensional immunoblotting in frontal cortices of AD patients and age-matched controls. A 60% increase in the amount of more acidic isoforms of GFAP was observed in AD and these isoforms were both phosphorylated and N-glycosylated, while more basic isoforms were O-glycosylated and exhibited no quantitative differences between post-mortem AD and control brains. These data highlight the importance of exploring isoform-specific levels of proteins in pathophysiological conditions since modifications of proteins determine their activity state, localization, turnover and interaction with other molecules. Mechanisms, structures and functional consequences of modification of GFAP isoforms remain to be clarified.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neurobiology of Disease - Volume 20, Issue 3, December 2005, Pages 858-870
Journal: Neurobiology of Disease - Volume 20, Issue 3, December 2005, Pages 858-870
نویسندگان
Minna A. Korolainen, Seppo Auriola, Tuula A. Nyman, Irina Alafuzoff, Tuula Pirttilä,