کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8260897 | 1534669 | 2013 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains
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کلمات کلیدی
PSD-95HypF-NCLUCM-H2DCFDAD-PBSMWMNBMPMSFAβEGTADTTGFAPFBSNGS2′,7′-dichlorodihydrofluorescein diacetate - 2 '، 7'-dichlorodihydrofluorescein diacetate3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide - 3- (4،5-dimethylthiazol-2-yl) -2،5-difenyltetrazolium bromideα2M - a2mBSA - BSADMSO - DMSOIba-1 - IBA-1MTT - MTTα2-macroglobulin - α2-ماگروگلوبولینHippocampal injury - آسیب هیپوکامپbovine serum albumin - آلبومین سرم گاوEDTA - اتیلن دی آمین تترا استیک اسید ethylene diamine tetraacetic acid - اتیلن دیامین تتراستیک اسیدethylene glycol tetraacetic acid - اتیلن گلیکول تتراستیک اسیدLearning impairment - اختلال یادگیریAlzheimer's disease - بیماری آلزایمرMorris water maze test - تست ماز آب موریسclusterin - خوسترینCNS - دستگاه عصبی مرکزیdithiothreitol - دیتیوتریتولDimethylsulfoxide - دیمتیل سولفواکسیدembryonic day - روز جنینیfetal bovine serum - سرم جنین گاوnormal goat serum - سرم طبیعی بزcentral nervous system - سیستم عصبی مرکزیDulbecco's phosphate-buffered saline - فسفات باسیل نمک Dulbeccophenylmethylsulfonyl fluoride - فنیل متیل سولفونیل فلورایدneurobasal medium - محیط عصبیHaptoglobin - هاپتوگلوبینneuronal nuclei - هسته های نورونیGlial fibrillary acidic protein - پروتئین اسیدی فیبریلاسیون گلایالpostsynaptic density protein 95 - پروتئین چگالی Postynaptic 95amyloid-beta peptide - پپتید آمیلوئید بتا
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterised by cognitive decline, formation of the extracellular amyloid β (Aβ42) plaques, neuronal and synapse loss, and activated microglia and astrocytes. Extracellular chaperones, which are known to inhibit amyloid fibril formation and promote clearance of misfolded aggregates, have recently been shown to reduce efficiently the toxicity of HypF-N misfolded oligomers to immortalised cell lines, by binding and clustering them into large species. However, the role of extracellular chaperones on Aβ oligomer toxicity remains unclear, with reports often appearing contradictory. In this study we microinjected into the hippocampus of rat brains Aβ42 oligomers pre-incubated for 1 h with two extracellular chaperones, namely clusterin and α2-macroglobulin. The chaperones were found to prevent Aβ42-induced learning and memory impairments, as assessed by the Morris Water Maze test, and reduce Aβ42-induced glia inflammation and neuronal degeneration in rat brains, as probed by fluorescent immunohistochemical analyses. Moreover, the chaperones were able to prevent Aβ42 colocalisation with PSD-95 at post-synaptic terminals of rat primary neurons, suppressing oligomer cytotoxicity. All such effects were not effective by adding pre-formed oligomers and chaperones without preincubation. Molecular chaperones have therefore the potential to prevent the early symptoms of AD, not just by inhibiting Aβ42 aggregation, as previously demonstrated, but also by suppressing the toxicity of Aβ42 oligomers after they are formed. These findings elect them as novel neuroprotectors against amyloid-induced injury and excellent candidates for the design of therapeutic strategies against AD.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease - Volume 1832, Issue 8, August 2013, Pages 1217-1226
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease - Volume 1832, Issue 8, August 2013, Pages 1217-1226
نویسندگان
Roberta Cascella, Simona Conti, Francesca Tatini, Elisa Evangelisti, Tania Scartabelli, Fiorella Casamenti, Mark R. Wilson, Fabrizio Chiti, Cristina Cecchi,