کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9015862 | 1127575 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cellular abnormalities linked to endoplasmic reticulum dysfunction in cerebrovascular disease-therapeutic potential
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کلمات کلیدی
GADDeIF2αGRPPKRXBP1IREUPR4-PBAuORFNOSATFAβORFERADsarcoplasmic/endoplasmic reticulum Ca2+-ATPasefamilial amyotrophic lateral sclerosis - اسکلروز جانبی جانبی آمیوتروفی فامیلی4-phenylbutyric acid - اسید 4-فنیل بوتیریکIschemia - ایسکمیFAD - بدfamilial Alzheimer's disease - بیماری آلزایمر خانوادگیDegenerative diseases - بیماری های تخریبیendoplasmic reticulum-associated degradation - تداخل وابسته به شبکیه آندوپلاسمیfALS - جعل اسنادSarcoplasmic reticulum - رتیکولوم سارکوپلاسمیکSOD - سدSuperoxide dismutase - سوکسوکس دیسموتازStroke - سکته مغزیendoplasmic reticulum - شبکه آندوپلاسمی upstream open reading frame - فریم خواندن باز بارگذاری بالادستactivating transcription factor - فعال کردن عامل رونویسیopen reading frame - قاب خواندن بازSERCA - قلبNitric oxide - نیتریک اکسیدnitric oxide synthase - نیتریک اکسید سنتازUnfolded protein response - پاسخ پروتئین آشکارX-box binding protein 1 - پروتئین اتصال X جعبه 1glucose-regulated protein - پروتئین تنظیم شده با گلوکزDouble-stranded RNA-dependent protein kinase - پروتئین کیناز وابسته به RNA دوجانبهPERK - پرک
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
داروشناسی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Unfolded proteins accumulate in the lumen of the endoplasmic reticulum (ER) as part of the cellular response to cerebral hypoxia/ischemia and also to the overexpression of the mutant genes responsible for familial forms of degenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, amyothrophic lateral sclerosis, and Huntington's disease, as well as other disorders that are caused by an expanded CAG repeat. This accumulation arises from an imbalance between the load of proteins that need to be folded and processed in the ER lumen and the ER folding/processing capacity. To withstand such potentially lethal conditions, stress responses are activated that includes the shutdown of translation to reduce the ER work load and the activation of the expression of genes coding for proteins involved in the folding and processing reactions, to increase folding/processing capacity. In transient cerebral ischemia, ER stress-induced suppression of protein synthesis is believed to be too severe to permit sufficient activation of the genetic arm of the ER stress response. Mutations associated with Alzheimer's disease down-regulate the ER stress response and make cells more vulnerable to conditions associated with ER stress. When the functioning of the ER is severely impaired and affected cells can no longer withstand these stressful conditions, programmed cell death is induced, including a mitochondria-driven apoptotic pathway. Raising the resistance of cells to conditions that interfere with ER functions and activating the degradation and refolding of unfolded proteins accumulated in the ER lumen are possible strategies for blocking the pathological process leading to cell death at an early stage.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Pharmacology & Therapeutics - Volume 108, Issue 3, December 2005, Pages 362-375
Journal: Pharmacology & Therapeutics - Volume 108, Issue 3, December 2005, Pages 362-375
نویسندگان
Wulf Paschen, Thorsten Mengesdorf,